CHAPARRO RODOLFO J (US)
ROSS JOHN F (US)
LOW CHEE MENG (US)
WO2015027082A1 | 2015-02-26 | |||
WO2011109789A2 | 2011-09-09 | |||
WO2019113464A1 | 2019-06-13 |
Claims 1. A construct comprising as a first polypeptide: i) a scaffold polypeptide sequence; ii) a TGF-β polypeptide sequence; iii) a masking polypeptide sequence optionally comprising a TGF-β receptor polypeptide sequence or an anti-TGF-β polypeptide sequence; iv) optionally, one or more independently selected MOD polypeptide sequences; and v) optionally, one or more independently selected linker polypeptide sequences; a construct comprising these elements being collectively referred to as a “masked TGF-β construct,” wherein the masking polypeptide sequence and the TGF-β polypeptide sequence bind to each other. 2. The masked TGF-β construct of claim 1, wherein the first polypeptide comprises, in order from N- terminus to C-terminus: i) the scaffold polypeptide sequence, the masking polypeptide sequence, and the TGF-β polypeptide sequence; ii) a first MOD polypeptide sequence, the scaffold polypeptide sequence, the masking polypeptide sequence, and the TGF-β polypeptide sequence; or iii) a first independently selected MOD polypeptide sequence, a second independently selected MOD polypeptide sequence, the scaffold polypeptide sequence, the masking polypeptide sequence, and the TGF-β polypeptide sequence; wherein the masked TGF-β construct optionally comprise one or more independently selected linker polypeptide sequences. 3. The masked TGF-β construct of claim 1 or claim 2, wherein the scaffold polypeptide comprises a dimerization sequence, optionally wherein the scaffold polypeptide comprises an interspecific dimerization sequence. 4. The masked TGF-β construct of any one of claims 1- 3, further comprising a second polypeptide dimerized with the first polypeptide to form a masked TGF-β complex heterodimer; wherein the second polypeptide comprises: i) a scaffold polypeptide sequence; ii) a TGF-β polypeptide sequence; iii) a masking polypeptide sequence optionally comprising a TGF-β receptor polypeptide sequence or an anti-TGF-β polypeptide sequence; iv) optionally, one or more independently selected MOD polypeptide sequences; and v) optionally, one or more independently selected linker polypeptide sequences. 5. The masked TGF-β construct of claim 4, wherein the first polypeptide comprises a scaffold polypeptide that comprises an interspecific dimerization sequence, wherein the second polypeptide comprises a scaffold polypeptide sequence that comprises a counterpart interspecific dimerization sequence to the interspecific binding sequence of the first polypeptide; and wherein the interspecific binding sequence and the counterpart interspecific binding sequence interact with each other in the heterodimer. 6. A TGF-β complex comprising a first polypeptide and a second polypeptide as a heterodimer, wherein: (i) the first polypeptide comprises a) a scaffold polypeptide sequence comprising an interspecific dimerization sequence, b) a masking polypeptide sequence optionally comprising a TGF-β receptor polypeptide sequence or an anti-TGF-β polypeptide sequence, c) optionally, one or more independently selected MOD polypeptide sequences, and d) optionally, one or more independently selected linker polypeptide sequences; and (ii) the second polypeptide comprises a) a scaffold polypeptide sequence comprising a counterpart interspecific dimerization sequence to the interspecific dimerization sequence in the first polypeptide, b) a TGF-β polypeptide sequence, c) optionally, one or more independently selected MOD polypeptide sequences, and d) optionally, one or more independently selected linker polypeptide sequences; a complex comprising these elements being collectively referred to as a “masked TGF-β complex,” wherein the masking polypeptide sequence and the TGF-β polypeptide sequence bind to each other; wherein the interspecific binding sequence and the counterpart interspecific binding sequence interact with each other (e.g., bind covalently or non-covalently) in the heterodimer; and wherein the masked TGF-β first polypeptide and/or the second polypeptide optionally comprise one or more independently selected linker polypeptide sequences. 7. The masked TGF-β complex heterodimer of claim 6, wherein: the first polypeptide comprises, from N-terminus to C-terminus, a) one or two (or more) independently selected MOD sequences, the scaffold polypeptide sequence comprising the interspecific dimerization sequence, and the masking polypeptide sequence; or b) a scaffold polypeptide sequence comprising an interspecific dimerization sequence, and the masking polypeptide sequence (e.g., TGF-β receptor polypeptide sequence); and the second polypeptide comprises, from N-terminus to C-terminus one or two (or more) independently selected MOD sequences, the scaffold polypeptide sequence comprising the counterpart interspecific dimerization sequence, and the TGF-β polypeptide sequence. 8. The masked TGF-β construct or the complex of any of claims 1-12, wherein the scaffold polypeptide sequence(s) are selected from the group consisting of Ig Fc polypeptide sequences and variants thereof, optionally wherein the Ig Fc polypeptide sequences include mutations that reduce binding of the polypeptide to complement component 1q (C1q) and/or Fc lambda receptor (FcλR) and/or substantially reduce or eliminate the ability of the Ig polypeptide to induce cell lysis, e.g., though complement- dependent cytotoxicity (CDC) and antibody-dependent cellular cytotoxicity (ADCC). 9. The masked TGF-β construct or complex of any of claims 1 to 13, wherein the one or more independently selected MOD polypeptide sequences are selected from the group consisting of: PD-L1, FAS-L, IL-1, IL-2, IL-4, IL-6, IL-7, IL-10, IL-15, IL-21, IL-23 MOD polypeptide sequences, and variants of any thereof. 10. The masked TGF-β construct or complex of any of claims 1 to 9, wherein at least one of the MOD polypeptide sequences is a wt. IL-2 MOD polypeptide sequence or variant IL-2 MOD polypeptide sequence (i) having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, or at least 99% aa sequence identity to at least 80, 90, 100, 110, 120, 130 or 133 contiguous aas of SEQ ID NO:9; or (ii) having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, or at least 99% aa sequence identity or 100% sequence identity to at least 80, 90, 100, 110, 120, 130 or 133 contiguous aas of one of SEQ ID NOs: 13-27. 11. The masked TGF-β construct or complex of any of claims 1 to 10, wherein the masking polypeptide sequence is a TGF-β receptor (“TβR”) polypeptide sequence that comprises an ectodomain fragment of a type I (TβRI), type II (TβRII) or type III (TβRIII) TβR. 12. The masked TGF-β complex of claim 7, wherein the complex is formed from the combination of polypetide construct 4033 (SEQ. ID. NO.:191) and polypetide construct 4039 (SEQ. ID. NO.:192). 13. One or more nucleic acids encoding a masked TGF-β complex of any of claims 1-12. 14. A method of inducing Treg cells in a mammalian subject or treating a disease or condition in a subject comprising administering to the subject one or more masked TGF-β constructs or complexes according to any one of claims 1-12 or a nucleic acid of claim 13. 15. The method of claim 14, wherein the method is for the treatment of an autoimmune condition or disease selected from the group consisting of: Addison's disease, alopecia areata, ankylosing spondylitis, autoimmune encephalomyelitis, autoimmune hemolytic anemia, autoimmune hepatitis, autoimmune- associated infertility, autoimmune thrombocytopenic purpura, bullous pemphigoid, celiac disease, Crohn's disease, Goodpasture's syndrome, glomerulonephritis, Grave's disease, Hashimoto's thyroiditis, mixed connective tissue disease, multiple sclerosis, myasthenia gravis (MG), pemphigus, pernicious anemia, polymyositis, psoriasis, psoriatic arthritis, rheumatoid arthritis, scleroderma, Sjögren's syndrome, systemic lupus erythematosus (SLE), type 1 diabetes (T1D), celiac disease, vasculitis, and vitiligo. |
AMENDED CLAIMS received by the International Bureau on 05 April 2021 (05.04.2021) 1. A construct comprising as a first polypeptide: i) a scaffold polypeptide sequence; ii) a TGF-β polypeptide sequence; iii) a masking polypeptide sequence comprising a TGF-β receptor polypeptide sequence or an anti-TGF-β polypeptide sequence; iv) optionally, one or more independently selected MOD polypeptide sequences; and v) optionally, one or more independently selected linker polypeptide sequences; a constmct comprising these elements being collectively referred to as a “masked TGF-β construct,” wherein the masking polypeptide sequence and the TGF-β polypeptide sequence bind to each other. 2. The masked TGF-β construct of claim 1, wherein the first polypeptide comprises, in order from N-terminus to C-terminus: i) the scaffold polypeptide sequence, the masking polypeptide sequence, and the TGF-β polypeptide sequence; ii) a first MOD polypeptide sequence, the scaffold polypeptide sequence, the masking polypeptide sequence, and the TGF-β polypeptide sequence; or iii) a first independently selected MOD polypeptide sequence, a second independently selected MOD polypeptide sequence, the scaffold polypeptide sequence, the masking polypeptide sequence, and the TGF-β polypeptide sequence; wherein the masked TGF-β construct optionally comprises one or more independently selected linker polypeptide sequences. 3. The masked TGF-β construct of claim 2, wherein the scaffold polypeptide comprises a dimerization sequence, optionally wherein the scaffold polypeptide comprises an interspecific dimerization sequence. 4. The masked TGF-β construct of claim 3, further comprising a second polypeptide dimerized with the first polypeptide to form a masked TGF-β complex heterodimer; wherein the second polypeptide comprises: i) a scaffold polypeptide sequence; ii) a TGF-β polypeptide sequence; iii) a masking polypeptide sequence optionally comprising a TGF-β receptor polypeptide sequence or an anti-TGF-β polypeptide sequence; iv) optionally, one or more independently selected MOD polypeptide sequences; and v) optionally, one or more independently selected linker polypeptide sequences. 5. The masked TGF-β construct of claim 4, wherein the first polypeptide comprises a scaffold polypeptide that comprises an interspecific dimerization sequence, wherein the second polypeptide comprises a scaffold polypeptide sequence that comprises a counterpart interspecific dimerization sequence to the interspecific binding sequence of the first polypeptide; and wherein the interspecific binding sequence and the counterpart interspecific binding sequence interact with each other in the heterodimer. 6. A TGF-β complex comprising a first polypeptide and a second polypeptide as a heterodimer, wherein: (i) the first polypeptide comprises a) a scaffold polypeptide sequence comprising an interspecific dimerization sequence, b) a masking polypeptide sequence comprising a TGF-β receptor polypeptide sequence or an anti-TGF-β polypeptide sequence, c) optionally, one or more independently selected MOD polypeptide sequences, and d) optionally, one or more independently selected linker polypeptide sequences; and (ii) the second polypeptide comprises a) a scaffold polypeptide sequence comprising a counterpart interspecific dimerization sequence to the interspecific dimerization sequence in the first polypeptide, b) a TGF-β polypeptide sequence, c) one or more independently selected MOD polypeptide sequences, and d) optionally, one or more independently selected linker polypeptide sequences; a complex comprising these elements being collectively referred to as a “masked TGF-β complex,” wherein the masking polypeptide sequence and the TGF-β polypeptide sequence bind to each other; wherein the interspecific binding sequence and the counterpart interspecific binding sequence interact with each other (e.g., bind covalently or non-covalently) in the heterodimer; and wherein the masked TGF-β first polypeptide and/or the second polypeptide optionally comprise one or more independently selected linker polypeptide sequences. 7. The masked TGF-β complex heterodimer of claim 6, wherein: the first polypeptide comprises, from N-terminus to C-terminus, a) one or two (or more) independently selected MOD sequences, the scaffold polypeptide sequence comprising the interspecific dimerization sequence, and the masking polypeptide sequence; or b) the scaffold polypeptide sequence comprising an interspecific dimerization sequence, and the masking polypeptide sequence (e.g., TGF-β receptor polypeptide sequence); and the second polypeptide comprises, from N-terminus to C-terminus one or two (or more) independently selected MOD sequences, the scaffold polypeptide sequence comprising the counterpart interspecific dimerization sequence, and the TGF-β polypeptide sequence. 8. The masked TGF-β construct or the complex of any of claims 1-7, wherein the scaffold polypeptide sequence(s) are selected from the group consisting of Ig Fc polypeptide sequences and variants thereof, optionally wherein the Ig Fc polypeptide sequences include mutations that reduce binding of the polypeptide to complement component lq (Clq) and/or Fc lambda receptor (FckR) and/or substantially reduce or eliminate the ability of the Ig polypeptide to induce cell lysis, e.g., though complement-dependent cytotoxicity (CDC) and antibody- dependent cellular cytotoxicity (ADCC). 9. The masked TGF-β construct or complex of any of claims 1-7, wherein the one or more independently selected MOD polypeptide sequences are selected from the group consisting of: PD-L1, FAS-L, IL-1, IL-2, IL-4, IL-6, IL-7, IL-10, IL-15, IL-21, IL-23 MOD polypeptide sequences, and variants of any thereof. 10. The masked TGF-β construct or complex of any of claims 1 to 7, wherein at least one of the MOD polypeptide sequences is a wt. IL-2 MOD polypeptide sequence or variant IL-2 MOD polypeptide sequence (i) having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, or at least 99% aa sequence identity to at least 80, 90, 100, 110, 120, 130 or 133 contiguous aas of SEQ ID NO:9; or (ii) having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99% or 100% aa sequence identity to at least 80, 90, 100, 110, 120, 130 or 133 contiguous aas of one of SEQ ID NOs: 13-27. 11. The masked TGF-β construct or complex of any of claims 1 to 7, wherein the masking polypeptide sequence is a TGF-β receptor (“TβR”) polypeptide sequence that comprises an ectodomain fragment of a type I (TβRI), type II (TβRII) or type III (TβRIII) TβR 12. The masked TGF-β complex of claim 7, wherein the complex is formed from the combination of polypeptide construct 4033 (SEQ. ID. NO.: 191) and polypeptide construct 4039 (SEQ. ID. NO.: 192). 13. One or more nucleic acids encoding a masked TGF-β complex of any of claims 1-7. 14. A method of inducing Treg cells in a mammalian subject or treating a disease or condition in a subject comprising administering to the subject one or more masked TGF-β constructs or complexes according to any one of claims 1-7 or a nucleic acid encoding a masked TGF-β complex of any of claims 1-7. 15. The method of claim 14, wherein the method is for the treatment of an autoimmune condition or disease selected from the group consisting of: Addison's disease, alopecia areata, ankylosing spondylitis, autoimmune encephalomyelitis, autoimmune hemolytic anemia, autoimmune hepatitis, autoimmune-associated infertility, autoimmune thrombocytopenic purpura, bullous pemphigoid, celiac disease, Crohn's disease, Goodpasture's syndrome, glomerulonephritis, Grave's disease, Hashimoto's thyroiditis, mixed connective tissue disease, multiple sclerosis, myasthenia gravis (MG), pemphigus, pernicious anemia, polymyositis, psoriasis, psoriatic arthritis, rheumatoid arthritis, scleroderma, Sjogren's syndrome, systemic lupus erythematosus (SLE), type 1 diabetes (T1D), celiac disease, vasculitis, and vitiligo. |
Table 1 modified from Ha et al., Frontiers in Immunol.7:1-16 (2016). * aa forms a stabilizing disulfide bond. [00266] In addition to the interspecific pairs of sequences in Table 1, interspecific “SEED” sequences having 45 residues derived from IgA in an IgG1 CH3 domain of the interspecific sequence and 57 residues derived from IgG1 in the IgA CH3 on the counterpart interspecific sequence. See Ha et al., Frontiers in Immunol.7:1-16 (2016). [00267] In an embodiment, the scaffold sequences found in a masked TGF-β construct or complex comprise an interspecific binding sequence or its counterpart interspecific binding sequence selected from the group consisting of: knob-in-hole (KiH); knob-in-hole with a stabilizing disulfide (KiHs-s); HA-TF; ZW-1; 7.8.60; DD-KK; EW-RVT; EW-RVTs-s; A107; or SEED sequences. [00268] In an embodiment, a masked TGF-β complex comprises a first polypeptide comprising an IgG1 scaffold with a T146W KiH sequence substitution, and a second polypeptide comprising an IgG1 scaffold with T146W, L148A, and Y187V KiH sequence substitutions, where the scaffolds comprises a sequence having at least 80%, 90%.95%, 98%, 99%, or 100% sequence identity to at least 170, at least 180, at least 190, at least 200, at least 210, at least 220, or all 227 contiguous aas of the IgG1 of SEQ ID NO:71. One or both scaffold aa sequences optionally comprising substitutions at one of more of L234 and L235 (e.g., L234A/L235A “LALA” or L234F/L235E), N297 (e.g., N297A), P331 (e.g. P331S), L351 (e.g., L351K), T366 (e.g., T366S), P395 (e.g., P395V), F405 (e.g., F405R), Y407 (e.g., Y407A), and K409 (e.g., K409Y) using Kabat numbering. Those substitutions appear at L14 and L15 (e.g., L14A/L15A “LALA” or L14F/L15E), N77 (e.g., N77A), P111 (e.g. P111S), L131 (e.g., L131K), T146 (e.g., T146S), P175 (e.g., P175V), F185 (e.g., F185R), Y187 (e.g., Y187A), and K189 (e.g., K189Y) in the IgG1 sequence of SEQ ID NO:71. [00269] In an embodiment, a masked TGF-β complex comprises a first polypeptide comprising an IgG1 scaffold with a T146W KiH sequence substitution, and a second polypeptide comprising an IgG1 scaffold with T146S, L148A, and Y187V KiH sequence substitutions, where the scaffolds comprises a sequence having at least 80%, 90%.95%, 98%, 99%, or 100% sequence identity to at least 170, at least 180, at least 190, at least 200, at least 210, at least 220, or all 227 contiguous aas of the IgG1 of SEQ ID NO:71; with none, one, or both of the scaffold aa sequences comprising L14 and L15 substitutions (e.g., L234A and L235A “LALA” in Kabat numbering), and/or N77 substitution to remove effector function by blocking interactions with Fcγ receptors (N297 e.g., N297A or N297G in Kabat numbering). See e.g., FIG 2D SEQ ID NOs: 77 and 78, [00270] In an embodiment, the first and second polypeptide of a masked TGF-β complex comprise in the first scaffold sequence T146W and S134C KiHs-s substitutions, and in the second scaffold sequence T146S, L148A, Y187V and Y129C KiHs-s substitutions, where the scaffolds comprise a sequence having at least 80%, 90%.95%, 98%, 99%, or 100% sequence identity to at least 170, at least 180, at least 190, at least 200, at least 210, at least 220, or all 227 contiguous aas of the IgG1 of SEQ ID NO:71; with none, one, or both of the scaffold aa sequences comprising L14 and L15 substitutions (e.g., L234A and L235A “LALA” in Kabat numbering), and/or N77 substitution to remove effector function by blocking interactions with Fcγ receptors (N297 e.g., N297A or N297G in Kabat numbering). [00271] In an embodiment, the first and second polypeptide of a masked TGF-β complex comprise in the first scaffold sequence S144H and F185A HA-TF substitutions, and in the second scaffold sequence Y129T and T174F HA-TF substitutions, where the scaffolds comprise a sequence having at least 80%, 90%.95%, 98%, 99%, or 100% sequence identity to at least 170, at least 180, at least 190, at least 200, at least 210, at least 220, or all 227 contiguous aas of the IgG1 of SEQ ID NO:71; with none, one, or both of the scaffold aa sequences comprising L14 and L15 substitutions (e.g., L234A and L235A “LALA” in Kabat numbering), and/or N77 substitution to remove effector function by blocking interactions with Fcγ receptors (N297 e.g., N297A or N297G in Kabat numbering). [00272] In an embodiment, the first and second polypeptides of a masked TGF-β complex comprise in the first scaffold sequence T130V, L131Y, F185A, and Y187V ZW1 substitutions, and in the second scaffold sequence T130V, T146L, K172L, and T174W ZW1 substitutions, where the scaffolds comprise a sequence having at least 80%, 90%.95%, 98%, 99%, or 100% sequence identity to at least 170, at least 180, at least 190, at least 200, at least 210, at least 220, or all 227 contiguous aas of the IgG1 of SEQ ID NO:71; with none, one, or both of the scaffold aa sequences comprising L14 and L15 substitutions (e.g., L234A and L235A “LALA” in Kabat numbering), and/or N77 substitution to remove effector function by blocking interactions with Fcγ receptors (N297 e.g., N297A or N297G in Kabat numbering). [00273] In an embodiment, the first and second polypeptides of a masked TGF-β complex comprise in the first scaffold sequence K140D, D179M, and Y187A 7.8.60 substitutions, and in the second scaffold sequence E125R, Q127R, T146V, and K189V 7.8.60 substitutions, where the scaffolds comprise a sequence having at least 80%, 90%.95%, 98%, 99%, or 100% sequence identity to at least 170, at least 180, at least 190, at least 200, at least 210, at least 220, or all 227 contiguous aas of the IgG1 of SEQ ID NO:71; with none, one, or both of the scaffold aa sequences comprising L14 and L15 substitutions (e.g., L234A and L235A “LALA” in Kabat numbering), and/or N77 substitution to remove effector function by blocking interactions with Fcγ receptors (N297 e.g., N297A or N297G in Kabat numbering). [00274] In an embodiment, the first and second β polypeptides of a masked TGF-β complex comprise in the first scaffold sequence K189D, and K172D DD-KK substitutions, and in the second scaffold sequence D179K and E136K DD-KK substitutions, where the scaffolds comprise a sequence having at least 80%, 90%.95%, 98%, 99%, or 100% sequence identity to at least 170, at least 180, at least 190, at least 200, at least 210, at least 220, or all 227 contiguous aas of the IgG1 of SEQ ID NO:71; with none, one, or both of the scaffold aa sequences comprising L14 and L15 substitutions (e.g., L234A and L235A “LALA” in Kabat numbering), and/or N77 substitution to remove effector function by blocking interactions with Fcγ receptors (N297 e.g., N297A or N297G in Kabat numbering), [00275] In an embodiment, the first and second polypeptides of a masked TGF-β complex comprise in the first scaffold sequence K140E and K189W EW-RVT substitutions, and in the second scaffold sequence Q127R, D179V, and F185T EW-RVT substitutions, where the scaffolds comprise a sequence having at least 80%, 90%.95%, 98%, 99%, or 100% sequence identity to at least 170, at least 180, at least 190, at least 200, at least 210, at least 220, or all 227 contiguous aas of the IgG1 of SEQ ID NO:71; with none, one, or both of the scaffold aa sequences comprising L14 and L15 substitutions (e.g., L234A and L235A “LALA” in Kabat numbering), and/or N77 substitution to remove effector function by blocking interactions with Fcγ receptors (N297 e.g., N297A or N297G in Kabat numbering). [00276] In an embodiment, the first and second polypeptides of a masked TGF-β complex comprise in the first scaffold sequence K140E, K189W, and Y129C EW-RVTs-s substitutions, and in the second scaffold sequence Q127R, D179V, F185T, and S134C EW-RVTs-s substitutions, where the scaffolds comprise a sequence having at least 80%, 90%.95%, 98%, 99%, or 100% sequence identity to at least 170, at least 180, at least 190, at least 200, at least 210, at least 220, or all 227 contiguous aas of the IgG1 of SEQ ID NO:71; with none, one, or both of the scaffold aa sequences comprising L14 and L15 substitutions (e.g., L234A and L235A “LALA” in Kabat numbering), and/or N77 substitution to remove effector function by blocking interactions with Fcγ receptors (N297 e.g., N297A or N297G in Kabat numbering). [00277] In an embodiment, the first and second polypeptides of a masked TGF-β complex comprise in the first scaffold sequence K150E and K189W A107 substitutions, and in the second scaffold sequence E137N, D179V, and F185T A107substitutions, where the scaffolds comprise a sequence having at least 80%, 90%.95%, 98%, 99%, or 100% sequence identity to at least 170, at least 180, at least 190, at least 200, at least 210, at least 220, or all 227 contiguous aas of the IgG1 of SEQ ID NO:71; with none, one, or both of the scaffold aa sequences comprising L14 and L15 substitutions (e.g., L234A and L235A “LALA” in Kabat numbering), and/or N77 substitution to remove effector function by blocking interactions with Fcγ receptors (N297 e.g., N297A or N297G in Kabat numbering). [00278] As an alternative to the use of immunoglobulin heavy chain constant regions as scaffolds, immunoglobulin light chain constant regions can be paired with heavy chain CH1 sequences as dimerization sequences that form, or are a part of, scaffold polypeptide sequences. In an embodiment, the first and second polypeptides of a masked TGF-β complex comprise in the first scaffold sequence an Ig CH1 domain (e.g., the polypeptide of SEQ ID NO:85), and in the second scaffold sequence Ig κ chain constant region sequence SEQ ID NO:86), where the scaffolds comprise a sequence having at least 80%, 85%, 90%.95%, 98%, 99%, or 100% sequence identity to at least 70, at least 80, at least 90, at least 100, or at least 110 contiguous aas of SEQ ID NOs: 85 and/or 86 respectively). See FIGs.2J and 2K. The CH1 and Ig κ sequenes may be modified to increase their affinity for each other, and accordingly the stability of any heterodimer formed utilizing them as a dimerization sequences. Among the substitutions that increase the stability of CH1- Ig κ heterodimers are those identified as the MD13 combination in Chen et al., MAbs, 8(4):761-774 (2016). In MD13 two substitutions are introduced into to each of the CH1 and Ig κ sequenes. The CH1 sequence is modified to contain S64E and S66V substitutions (S70E and S72V in SEQ ID NO:85 shown in FIG 2J). The Ig κ sequence is modified to contain S69L and T71S substitutions (S68L and T70S in SEQ ID NO:86 shown in FIG.2K). [00279] In another embodiment, the first and second polypeptide of a masked TGF-β complex comprise in the first scaffold sequence an Ig CH1 domain (e.g., the polypeptide of SEQ ID NO:85), and in the second scaffold sequence Ig λ chain constant region sequence SEQ ID NO:87), where the scaffolds comprise a sequence having at least 80%, 85%, 90%.95%, 98%, 99%, or 100% sequence identity to at least 70, at least 80, at least 90, at least 100, or at least 110 contiguous aas of SEQ ID NOs: 85 and/or 87 respectively. See FIGs.2J and 2K. [00280] In some cases, the scaffold polypeptide sequence of a first and a second polypeptide of a masked TGF-β complex each comprise a leucine zipper polypeptide as a dimerization sequence. The leucine zipper polypeptides bind to one another to form dimer (e.g., homodimer). Non-limiting examples of leucine-zipper polypeptides include, for example, a peptide of any one of the following aa sequences: RMKQIEDKIEEILSKIYHIENEIARIKKLIGER (SEQ ID NO:88); LSSIEKKQEEQTS- WLIWISNELTLIRNELAQS (SEQ ID NO:89); LSSIEKKLEEITSQLIQISNELTLIRNELAQ (SEQ ID NO:90; LSSIEKKLEEITSQLIQIRNELTLIRNELAQ (SEQ ID NO:91); LSSIEKKLEEITSQLQQ- IRNELTLIRNELAQ (SEQ ID NO:92); LSSLEKKLEELTSQLIQLRNELTLLRNELAQ (SEQ ID NO:93); ISSLEKKIEELTSQIQQLRNEITLLRNEIAQ (SEQ ID NO:94). In some cases, a leucine zipper polypeptide comprises the following aa sequence: LEIEAAFLERENTALETRVAELRQR- VQRLRNRVSQYRTRYGPLGGGK (SEQ ID NO:95). Additional leucine-zipper polypeptides are known in the art, any of which is suitable for use as scaffold or incorporation into a scaffold as a dimerization sequence. [00281] In some cases, the scaffold polypeptide sequence of a first and a second polypeptide of a masked TGF-β complex each comprise a coiled-coil peptide that forms a dimer (e.g., homodimer). Non-limiting examples of coiled-coil polypeptides include, for example, a peptide of any one of the following aa sequences: LKSVENRLAVVENQLKTVIEELKTVKDLLSN (SEQ ID NO:96); LARIE- EKLKTIKAQLSEIASTLNMIREQLAQ (SEQ ID NO:97); VSRLEEKVKTLKSQVTELASTVSLL- REQVAQ (SEQ ID NO:98); IQSEKKIEDISSLIGQIQSEITLIRNEIAQ (SEQ ID NO:99); LMSLE- KKLEELTQTLMQLQNELSMLKNELAQ (SEQ ID NO:100). [00282] In some cases, a scaffold polypeptide sequence that permits dimerization (homodimerization) of a first and a second polypeptide of a masked TGF-β complex each comprise a polypeptide sequence having at least one cysteine residue that can form a disulfide bond. Examples of such polypeptide sequences include: a human FasL polypeptide VDLEGSTSNGRQCAGIRL (SEQ ID NO:101); EDDVTTTEELAPALVPPPKGTCAGWMA (SEQ ID NO:102); and GHDQETTTQGPGVLL- PLPKGACTGQMA (SEQ ID NO:103). [00283] Peptides suitable as multimerization (oligomerization) sequences permit formation of masked TGF-β complexes greater than dimers (e.g., trimers tetramers, pentamers, hexamers, etc.) include, but are not limited to, IgM constant regions (see e.g., FIG 2 H) which forms hexamer, or pentamers (particularly when combined with a mature j-chain peptide lacking a signal sequence such as that provided in FIG.2I). Collagen domains, which form trimers, can also be employed. Collagen domains can comprise (Gly-Xaa-Xaa)n, where Xaa is any aa, or and where n is an integer (e.g., from 10 to 40); where Xaa and Yaa are independently any aa and n is an integer from 10 to 40. In Gly-Xaa-Yaa sequences, Xaa and Yaa are frequently proline and hydroxyproline respectively in greater than 25%, 50%, 75%, 80% 90% or 95% of the Gly-Xaa-Yaa occurrences, or in each of the Gly-Xaa-Yaa occurrences. In some cases, a collagen domain comprises the sequence (Gly-Xaa-Pro)n, where n is an integer (e.g., from 10 to 40). A collagen oligomerization peptide can comprise the following aa sequence: VTAFSNMDDMLQKAHLVIEGTFIYLRDSTEFFIRVRDGWKKLQLGELIPIPADSPPPP- ALSSNP (SEQ ID NO:104). F. TGF-β polypeptides [00284] As noted above, a masked TGF-β construct or complex comprises at least one TGF-β polypeptide (e.g., one or more independently selected TGF-β polypeptides). Amino acid sequences of TGF-β polypeptides are known in the art. In some cases, the TGF-β polypeptide present in a masked TGF-β construct or complex is a TGF-β1 polypeptide. In some cases, the TGF-β polypeptide present in a masked TGF-β construct or complex is a TGF-β2 polypeptide. In some cases, the TGF-β polypeptide present in a masked TGF-β construct or complex is a TGF-β3 polypeptide. [00285] While TGF-β1, TGF-β2, or TGF-β3 polypeptide sequences may be incorporated into a masked TGF-β construct or complex, a variety of factors may influence the choice of the specific TGF-β polypeptide, and the specific sequence and aa substitutions that will be employed. For example, TGF-β1 and TGF-β3 are subject to “clipping” of their amino acid sequences when expressed in a number of mammalian cell systems (e.g., CHO cell). In addition, dimerized TGF-β (e.g., TGF-β2) has a higher affinity for the TβR3 (beta glycan receptor) than for the TβR2 receptor, which could lead to off target binding and loss of biological active masked protein to the large in vivo pool of non-signaling TβR3 molecules. In order to minimize high-affinity off target binding to TβR3, it may be desirable to substitute the residues leading to dimeric TGF-β molecules, which are joined by a disulfide bond. Accordingly, cysteine 77 (C77) may be substituted by an amino acid other than cysteine (e.g., a serine forming a C77S substitution) [00286] A suitable TGF-β polypeptide can have a length from about 70 aas to about 125 aas; for example, a suitable TGF-β polypeptide can have a length from about 70 aas to about 80 aas from about 80 aas to about 90 aas; from about 90 aas to about 100 aas; from about 100 aas to about 105 aas, from about 105 aas to about 110 aas, from about 110 aas to about 112 aas, from about 113 aas to about 120 aas, or from about 120 aas to about 125 aas. A suitable TGF-β polypeptide can comprise an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%, aa sequence identity to at least 80, at least 90, at least 100, or at least 110 contiguous aas of the mature form of a human TGF-β1 polypeptide, a human TGF- β2 polypeptide, or a human TGF-β3 polypeptide. 1 TGF-β1 polypeptides [00287] A suitable TGF-β1 polypeptide can comprise an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%, aa sequence identity to at least 70, at least 80, at least 90, at least 100, at least 110, or 112 aas of the following TGF- β1 amino acid sequence: AL DTNYCFSSTE KNCCVRQLYI DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA SAAPCCVPQA LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS (SEQ ID NO:105, 112 aas in length); where the TGF-β1 polypeptide has a length of about 112 aas. A TGF-β1 preproprotein is provided in FIG.3 as SEQ ID NO:106. Amino acids R25, C77, V92 and R94 are bolded and italicized see FIG.4. [00288] In some cases, a suitable TGF-β1 polypeptide comprises a C77S substitution. Thus, in some cases, a suitable TGF-β1 polypeptide comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%, aa sequence identity to at least 70, at least 80, at least 90, at least 100, at least 110, or 112 aas of the following TGF-β1 amino acid sequence: AL DTNYCFSSTE KNCCVRQLYI DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA SAAPSCVPQA LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS (SEQ ID NO:107), where amino acid 77 is Ser. Positions 25, 77, 92 and 94 are bolded and italicized. 2 TGF-β2 polypeptides [00289] A suitable TGF-β2 polypeptide can comprise an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%, aa sequence identity to at least 70, at least 80, at least 90, at least 100, at least 110, or 112 aas of the following TGF- β2 amino acid sequence: ALDAAYCFR NVQDNCCLRP LYIDFKRDLG WKWIHEPKGY NANFCAGACP YLWSSDTQHS RVLSLYNTIN PEASASPCCV SQDLEPLTIL YYIGKTPKIE QLSNMIVKSC KCS (SEQ ID NO:108), where the TGF-β2 polypeptide has a length of about 112 aas. A TGF-β2 preproprotein is provided in FIG.3 as SEQ ID NO:109. Residues Lys 25, Ile 92, and/or Lys 94 are bolded and italicized. [00290] In some cases, a suitable TGF-β2 polypeptide comprises a C77S substitution. Thus, in some cases, a suitable TGF-β2 polypeptide comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%, aa sequence identity to at least 70, at least 80, at least 90, at least 100, at least 110, or 112 aas of the following TGF-β2 amino acid sequence: ALDAAYCFR NVQDNCCLRP LYIDFKRDLG WKWIHEPKGY NANFCAGACP YLWSSDTQHS RVLSLYNTIN PEASASPSCV SQDLEPLTIL YYIGKTPKIE QLSNMIVKSC KCS (SEQ ID NO110), where amino acid 77 is Ser. 3 TGF-β3 polypeptides [00291] A suitable TGF-β3 polypeptide can comprise an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%, aa sequence identity to at least 70, at least 80, at least 90, at least 100, at least 110, or 112 aas of the following TGF- β3 amino acid sequence: ALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS (SEQ ID NO:111), where the TGF-β3 polypeptide has a length of about 112 aas. A TGF-β3 isoform 1 preproprotein is provided in FIG.3 as SEQ ID NO:112. Positions 25, 92 and 94 are bolded and italicized. [00292] In some cases, a suitable TGF-β3 polypeptide comprises a C77S substitution. In some cases, a suitable TGF-β3 polypeptide comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%, aa sequence identity to at least 70, at least 80, at least 90, at least 100, at least 110, or 112 aas of the following TGF-β3 amino acid sequence: ALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPSCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS (SEQ ID NO:113), where amino acid 77 is Ser. Positions 25, 92 and 94 are bolded and italicized. 4 Additional TGF-β polypeptide sequence variations [00293] In addition to sequence variations that alter TGF-β molecule dimerization (e.g., cysteine 77 substitutions such as C77S), TGF-β1-3 polypeptides having sequence variations that affect affinity and other properties may be incorporated into a masked TGF-β construct or complex. When a masked TGF- β construct or complex comprises a TGF-β variant with reduced affinity for the masking polypeptide (e.g. TβR polypeptide such as a TβRII polypeptide) those components dissociate more readily, making the masked TGF-β polypeptide more available to cellular TβR proteins. Because the TβRII protein is generally the first peptide of the heteromeric TβR signaling complex to interact with TGF-β, interactions with TβRII effectively controls entry of TGF-β into active signaling complexes. Accordingly, variants controlling the affinity of TGF-β for TβRII effectively control entry of masked TGF-β constructs and complexes into active signaling complexes. [00294] The present disclosure includes and provides for masked TGF-β constructs and complexes comprising a variant masking TβR (e.g., TβRII) polypeptide sequence and/or a variant TGF-β polypeptide having altered (e.g., reduced) affinity for each other (relative to an otherwise identical masked TGF-β construct or complex without the sequence variation(s)). Affinity between a TGF-β polypeptide and a TβR (e.g., TβRII) polypeptide may be determined using (BLI) as described above for MODs and their co-MODs. a. Additional TGF-β2 sequence variants [00295] The present disclosure includes and provides for masked TGF-β2 constructs and complexes comprising a masking TβR (e.g., TβRII) polypeptide sequence and either a wt. or a variant TGF-β2 polypeptide; where the variant polypeptide has a reduced affinity for the masking TβR (relative to an otherwise identical wt. TGF-β polypeptide sequence without the sequence variations). [00296] The disclosure provides for a masked TGF-β construct or complex comprises a masking TβRII receptor sequence and a variant TGF-β2 polypeptide having greater than 85% (e.g., greater than 90%, 95%, 98% or 99%) sequence identity to at least 100 contiguous aa of SEQ ID NO. 108, and comprising a substitution reducing the affinity of the variant TGF-β2 polypeptide for the TβRII receptor sequence. [00297] In some cases, a masked TGF-β construct or complex comprises a masking TβRII polypeptide and a variant TGF-β (e.g. TGF-β2) polypeptide comprising a substitution at one or more, two or more, or all three of Lys 25, Ile 92, and/or Lys 94 (see SEQ ID NO:108 for the location of the residues, and FIG.4 for the corresponding residues in TGF-β1 and TGF-β3). Those aa residues have been shown to affect the affinity of TGF-β2 for TβRII polypeptides (see Crescenzo et al., J. Mol. Biol.355: 47–62 (2006)). The masked TGF-β polypeptide optionally comprises one or more independently selected MODs such as IL-2 or a variant thereof. In one instance, the masked TGF-β construct or complex comprises a masking TβRII polypeptide and a TGF-β2 polypeptide having an aa other than Lys or Arg at position 25 of SEQ ID NO:108; and optionally comprises one or more independently selected MODs (e.g., one or more IL-2 MOD polypeptide or reduced affinity variant thereof). A masked TGF-β construct or complex with a masking TβRII polypeptide may comprises a TGF-β2 polypeptide having an aa other than Ile or Val at position 92 of SEQ ID NO:108 (or an aa other than Ile, Val, or Leu at postion 92); and optionally comprises one or more independently selected MODs (e.g., one or more IL-2 MOD polypeptide or reduced affinity variant thereof). A masked TGF-β construct or complex with a masking TβRII polypeptide may comprise a TGF-β2 polypeptide having an aa other than Lys or Arg at position 94 of SEQ ID NO:108; and optionally comprises one or more independently selected MODs (e.g., one or more IL-2 MOD polypeptide or reduced affinity variant thereof). A masked TGF-β construct or complex with a masking TβRII polypeptide may comprise a TGF-β2 polypeptide comprising a substitution at one or more, two or more or all three of Lys 25, Ile 92, and/or Lys 94, and further comprises one or more independently selected MODs. A masked TGF-β construct or complex with a masking TβRII polypeptide may comprise a TGF-β2 polypeptide comprising a substitution at one or more, two or more or all three of Lys 25, Ile 92, and/or Lys 94, and further comprises one or more independently selected IL-2 MODs or reduced affinity variants thereof b. Additional TGF-β1 and TGF-β3 sequence variants [00298] In some cases, a masked TGF-β construct or complex comprises a masking TβRII polypeptide and a variant TGF-β1 or TGF-β3 polypeptide comprising a substitution at one or more, two or more or all three aa positions corresponding to Lys 25, Ile 92, and/or Lys 94 in TGF-β2 SEQ ID NO:108. In TGF-β1 or TGF-β3, the aa that corresponds to: Lys 25 is an Arg 25, Ile 92 is Val 92, and Lys 94 is Arg 94, each of which is a conservative substitution. See e.g., SEQ ID NOs: 106 and 107 for TGF-β1 and SEQ ID NOs: 112 and 113 for TGF-β3. [00299] As noted above, the masked TGF-β construct or complex optionally comprises one or more independently selected MODs such as IL-2 or a variant thereof. In one instance, the masked TGF-β construct or complex with a masking TβRII polypeptide comprises a TGF-β1 or β3 polypeptide having an aa other than Arg or Lys at position 25; and optionally comprises one or more independently selected MODs (e.g., one or more IL-2 MOD polypeptide or reduced affinity variant thereof). In one instance, the masked TGF-β construct or complex with a masking TβRII polypeptide comprises a TGF-β1 or β3 polypeptide having an aa other than Val or Ile at position 92 (or an aa other than Ile, Val, or Leu at postion 92); and optionally comprises one or more independently selected MODs (e.g., one or more IL-2 MOD polypeptide or reduced affinity variant thereof). In another instance, the masked TGF-β construct or complex with a masking TβRII polypeptide comprises a TGF-β2 polypeptide having an aa other than Arg or Lys; and optionally comprises one or more independently selected MODs (e.g., one or more IL-2 MOD polypeptide or reduced affinity variant thereof). In one specific instance, a masked TGF-β construct or complex with a masking TβRII polypeptide comprises a TGF-β1 or β3 polypeptide comprising a substitution at one or more, two or more or all three of Arg 25, Val 92, and/or Arg 94, and further comprises one or more independently selected MODs. In another specific instance, a masked TGF-β construct or complex with a masking TβRII polypeptide comprises a TGF-β1 or β3 polypeptide comprising a substitution at one or more, two or more or all three of Arg 25, Val 92, and/or Arg 94, and further comprises one or more independently selected IL-2 MODs, or reduced affinity variants thereof. G. TGF-β receptor polypeptides and other polypeptides that bind and mask TGF-β [00300] In any of the above-mentioned TGF-β polypeptides or polypeptide complexes the polypeptide that binds to and masks the TGF-β polypeptide (a “masking polypeptide”) can take a variety of forms, including fragments of TβRI, TβRII, TβRIII and anti TGF-β antibodies or fragments thereof (e.g., Fab., single chain antibodies, etc.). 1 TGF-β Receptor Polypeptides [00301] The masking of TGF-β in masked TGF-β constructs and complexes may be accomplished by utilizing a TGF-β receptor fragment (e.g., the ectodomain sequences of TβRI, TβRII or TβRIII) that comprises polypeptide sequences sufficient to bind a TGF-β polypeptide (e.g., TGF-β1, TGF-β2 or TGF- β3). In an embodiment, the masking sequence comprises all or part of the TβRI, TβRII, or TβRIII ectodomain. a. TGF-β Receptor I (TβRI) [00302] In an embodiment the polypeptide sequence masking TGF-β in a masked TGF-β construct or complexes may be derived from a TβRI (e.g., isoform 1 SEQ ID NO:114) and may comprises all or part of the TβRI ectodomain (aas 34-126) In some cases, a suitable TβRI polypeptide for masking TGF-β comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%, aa sequence identity to at least 70, at least 80, at least 90, at least 100, or 103 aas of the following TβRI ectodomain aa sequence: LQCFCHL CTKDNFTCVT DGLCFVSVTE TTDKVIHNSM CIAEIDLIPR DRPFVCAPSS KTGSVTTTYC CNQDHCNKIE LPTTVKSSPG LGPVEL (SEQ ID NO:115). b. TGF-β Receptor II (TβRII) [00303] In embodiments, the polypeptide sequence masking TGF-β in a masked TGF-β construct or complex may be derived from a TβRII (e.g., isoform A SEQ ID NO:116), and may comprises all or part of the TβRII ectodomain sequence (aas 24 to 177). In an embodiment, a suitable TβRII isoform A polypeptide for masking TGF-β may comprise an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%, aa sequence identity to at least 70, at least 80, at least 90, at least 100, at least 110, at least 120, at least 130, at least 140, at least 150 or at least 154 aas of the following TβRII isoform A ectodomain aa sequence: IPPHVQK SDVEMEAQKD EIICPSCNRT AHPLRHINND MIVTDNNGAV KFPQLCKFCD VRFSTCDNQK SCMSNCSITS ICEKPQEVCV AVWRKNDENI TLETVCHDPK LPYHDFILED AASPKCIMKE KKKPGETFFM CSCSSDECND NIIFSEE (SEQ ID NO:117). The location of the aspartic acid residue corresponding to D118 in the B isoform is bolded, underlined, and italicized. [00304] In an embodiment, the polypeptide sequence masking TGF-β in a masked TGF-β construct or complex may be derived from TβRII isoform B SEQ ID NO:118) and may comprises all or part of the TβRII ectodomain sequence (aas 24 to 166). In embodiment, a suitable TβRII isoform B polypeptide for masking TGF-β comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%, aa sequence identity to at least 70, at least 80, at least 90, at least 100, or 103 aas of the TβRII isoform B ectodomain aa sequence: IPPHVQKSVN NDMIVTDNNG AVKFPQLCKF CDVRFSTCDN QKSCMSNCSI TSICEKPQEV CVAVWRKNDE NITLETVCHD PKLPYHDFIL EDAASPKCIM KEKKKPGETF FMCSCSSDEC NDNIIFSEEY NTSNPDLLLV IFQ (SEQ ID NO:119). As discussed below, any one or more of F30, D32, S52, E55, or D118 (italicized and bolded) may be substituted by an amino acid other than the naturally occurring aa at those positions (e.g., alanine). A polypeptide sequence masking TGF-β may comprise the polypeptide of SEQ ID NO:119 bearing a D118A or D118R substitution. A sequence masking TGF-β may comprise the peptide of SEQ ID NO:119 bearing a D118A or D118R substitution and one or more of a F30A, D32N, S52L and/or E55A substitution. [00305] Although TβRII’s ectodomain may be utilized as a masking polypeptide, that region of the protein has charged and hydrophobic patches that can lead to an unfavorable pI nd can be toxic to cell expressing the polypeptide. In addition, combining a TβRII ectodomain with the an active TGF-β polypeptide can result in a complex that could combine with cell surface TβRI and cause activation of that signaling receptor (e.g., signaling through the Smad pathway). Modifying TβRII ectodomain sequences used to mask TGF-β by removing or altering sequences involved in TβRI association can avoid the unintentional stimulation of cells by the masked TGF-β except through their own cell surface heterodimeric TβRI /TβRII complex. Modifications of TβRII may also alter (e.g., reduce) the affinity of the TβRII for TGF-β (e.g., TGF-β3), thereby permitting control of TGF-β unmasking and its availability as a signaling molecule. Masked TGF-β construct or complexes comprising TβR (e.g., TβRII) peptides with the highest affinity for TGF-β (e.g., TGF-β3) most tightly mask the TGF-β sequence and require higher doses to achieve the same effect. In contrast, aa substitutions in TβRII that lower the affinity unmask the TGF-β polypeptide and are biologically effective at lower doses. See e.g., Example 3. [00306] Accordingly, where it is desirable to block/limit signaling by the masked TGF-β polypeptide through TβRI and/or modify (e.g., reduce) the affinity of a masking TβRII polypeptide for TGF-β a number of alterations to TβRII may be incorporated into the TβRII polypeptide sequence. Modifications that can be made include the above-mentioned deletions of N-terminal 25 amino acids from 1 to 25 aa in length (e.g. Δ14, Δ25) and/or substitutions at one or more of L27, F30, D32, S49, 150, T51, S52, I53, E55, V77, D118, and/or E119. Some specific modifications resulting in a reduction in TβRI association with TβRII and reduced affinity for TGF-β include any one or more of L27A, F30A, D32A, D32N, S49A, I50A, T51A, S52A, S52L, I53A, E55A, V77A, D118A, D118R, E119A, and/or E119Q based on SEQ ID NO:119. See e.g., J. Groppe et al. Mol Cell 29, 157-168, (2008) and De Crescenzo et al. JMB 355, 47-62 (2006). See FIG X for the effects of those substitutions on TGF-β3−TβRII and TβRI−TβRII complexes. Modifications of TβRII the including an N-terminal Δ25 deletion and/or substitutions at F24 (e.g., an F24A substitution) substantially or completely block signal through the canonical SMAD signaling pathway). In one aspect, the aspartic acid at position 118 (D118) of the mature TβRII B isoform(SEQ ID NO:119) is replaced by an amino acid other than Asp or Glu, such as Ala giving rise to a “D118A” substitution or by an Arg giving rise to a D118R substitution. The Asp residues corresponding D118 are indicated SEQ ID NOs.117-123 (with bold and underlining in FIG.5B). N-terminal deletions of from 1 to 25 aa in length (e.g., a Δ25 deletions) and/or substitutions at F24 (e.g., an F24A substitution) may be combined with D118 substitutions (e.g., D118A or D118R). N-terminal deletions of from 1 to 25 aa in length (e.g., a Δ25 deletions) and/or substitutions at F24 (e.g., an F24A substitution) may also be combined with substitutions at any of L27, F30, D32, S49, 150, T51, S52, I53, E55, V77, D118, and/or E119 (e.g., D118A) substitutions, and particularly any of the specific substitutions recited for those locations in SEQ ID NO:119 described above to alter the affinity. [00307] Deletions of the N-terminus of the TβRII polypeptides may also result in loss of TβRI interactions and prevent masked TGF-β constructs and complexes comprising a TβRII polypeptide from acting as a constitutively active complex that engages and activates TβRI signaling. A 14 aa deletion (Δ14) of the TβRII polypeptide substantively reduces the interaction of the protein with TβRI, and a Δ25 aa deletion of TβRII appears to completely abrogate the interaction with TβRI. N-terminal deletions also substantially alter the pI of the protein, with the Δ14 TβRII ectodomain mutant displaying a pI of about 4.5-5.0 (e.g., about 4.74). Accordingly, TGF-β constructs or complexes may comprise TβRII ectodomain polypeptides (e.g., polypeptides of SEQ ID NOs: 117 or 118) with N-terminal deletions, such as from 14 to 25 aas (e.g., 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, or 25 aa). Modified ectodomain sequences, including those that limit interactions with TβRI, that may be utilized to mask TGF-β polypeptides in a masked TGF-β construct or complex are described in the paragraphs that follow. [00308] In an embodiment, the sequence masking TGF-β in a masked TGF-β construct or complex comprises sequence having at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%, aa sequence identity to at least 70, at least 80, at least 90, at least 100, or 103 aas of the TβRII isoform B ectodomain sequence: IPPHVQKSVN NDMIVTDNNG AVKFPQLCKF CDVRFSTCDN QKSCMSNCSI TSICEKPQEV CVAVWRKNDE NITLETVCHD PKLPYHDFIL EDAASPKCIM KEKKKPGETF FMCSCSSDEC NDNIIFSEE(SEQ ID NO:120). Any one or more of F30, D32, S52, E55, or D118 (italicized and bolded) may be substituted by an amino acid other than the naturally occurring aa at those positions (e.g., alanine). In an embodiment, the sequence masking TGF-β comprises the peptide of SEQ ID NO:120 bearing a D118A substitution. In an embodiment, the sequence masking TGF-β comprises the polypeptide of SEQ ID NO:120 bearing a D118A substitution and one or more of a F30A, D32N, S52L and/or E55A substitution. [00309] Combinations of N-terminal deletions of TβRII, such as from 14 to 25 aas (e.g., 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, or 25 aa), that block inadvertent cell signaling due to the masked TGF- β/TβRII complex interacting with TβRI may be combined with other TβRII ectodomain substitutions, including those at any one or more of F30, D32, S52, E55, and/or D118. The combination of deletions and substitutions ensures the masked TGF-β construct or complex does not cause cell signaling except through the cell’s membrane bound TβRI & TβRII receptors. [00310] In an embodiment, the sequence masking TGF-β in a masked TGF-β construct or complex comprises sequence having at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%, aa sequence identity to at least 70, at least 80, at least 90, at least 100, or 103 aas of the TβRII isoform B ectodomain sequence: TDNNG AVKFPQLCKF CDVRFSTCDN QKSCMSNCSI TSICEKPQEV CVAVWRKNDE NITLETVCHD PKLPYHDFIL EDAASPKCIM KEKKKPGETF FMCSCSSDEC NDNIIFSEE(SEQ ID NO:121), which has aas 1-14 (Δ14) deleted. Any one or more of F30, D32, S52, E55, or D118 (italicized and bolded) may be substituted by an amino acid other than the naturally occurring aa at those positions (e.g., alanine). In an embodiment, the sequence masking TGF-β comprises the peptide of SEQ ID NO:120 bearing a D118A substitution. In an embodiment, the sequence masking TGF-β comprises the polypeptide of SEQ ID NO:121 bearing a D118A substitution and one or more of a F30A, D32N, S52L and/or E55A substitution. [00311] In an embodiment, the sequence masking TGF-β in a masked TGF-β construct or complex comprises sequence having at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%, aa sequence identity to at least 70, at least 80, at least 90, at least 100, or 103 aas of the sequence: QLCKF CDVRFSTCDN QKSCMSNCSI TSICEKPQEV CVAVWRKNDE NITLETVCHD PKLPYHDFIL EDAASPKCIM KEKKKPGETF FMCSCSSDEC NDNIIFSEE(SEQ ID NO:122), which has aas 1-25 (Δ25) deleted. Any one or more of F30, D32, S52, E55, or D118 (italicized and bolded) may be substituted by an amino acid other than the naturally occurring aa at those positions (e.g., alanine). In an embodiment, the sequence masking TGF-β comprises the polypeptide of SEQ ID NO:122 bearing a D118A substitution (shown as SEQ ID NO:123 in FIG. 5B). In an embodiment, the sequence masking TGF-β in a masked TGF-β construct or complex comprises the peptide of SEQ ID NO:122 bearing a D118A substitution and one or more of a F30A, D32N, S52L and/or E55A substitution. In an embodiment, the sequence masking TGF-β in a masked TGF-β construct or complex comprises the peptide of SEQ ID NO:122 (see FIG.5B) bearing D118A and F30A substitutions. In an embodiment, the sequence masking TGF-β in a masked TGF-β construct or complex comprises the peptide of SEQ ID NO:122 (see FIG.5B) bearing D118A and D32N substitutions. In an embodiment, the sequence masking TGF-β in a masked TGF-β construct or complex comprises the peptide of SEQ ID NO:122 (see FIG.5B) bearing D118A and S52L substitutions. In an embodiment, the sequence masking TGF-β in a masked TGF-β construct or complex comprises the peptide of SEQ ID NO:122 (see FIG.5B) bearing D118A and E55A. c. TGF-β Receptor III (TβRIII) [00312] In an embodiment, the polypeptide sequence masking TGF-β in a masked TGF-β construct or complexes may be derived from a TβRIII (e.g., isoform A SEQ ID NO:124 and isoform B 125), and may comprises all or part of a TβRIII ectodomain (aas 27-787 of the A isoform or 27-786 of the B isoform). In some cases, a suitable TβRIII polypeptide for masking TGF-β comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%, aa sequence identity to at least 70, at least 80, at least 90, at least 100, or 120 aas of a TβRIII A isoform or B isoform ectodomain sequences (e.g., provided in FIG.5C as SEQ ID NO:124 or SEQ ID NO:125). 2 Antibodies [00313] Although TGF-β receptor polypeptides (e.g., ectodomain sequences) can function to bind and mask TGF-β polypeptides in masked TGF-β constructs or complexes, other polypeptide sequences (protein sequences) that bind to TGF-β sequences can also be employed as masking polypeptides. Among the suitable polypeptide or protein sequences that can be used to mask TGF-β are antibodies with affinity for TGF-β (e.g., antibodies specific for an one or more of TGF-β1, TGF-β2, or TGF-β3) or their fragments, nanobodies with affinity for TGF-β polypeptides, and particularly single chain anti- TGF-β antibodies (e.g., any of which may be humanized). Some antibodies, including scFV antibodies, that bind and neutralize TGF-β have been described. See e.g., US 9,090,685. Throughout the embodiments and/or aspects of the invention described in this disclosure, TβR (e.g., TβRII) sequences used to mask TGF-β polypeptides may be replaced with masking antibody sequences (e.g., a scFV or a nanobody) with affinity for the TGF-β polypeptide. For instance, in each of the masked TGF-β constructs or complexes in FIG.1 where a TGF-β receptor sequence is used to mask a TGF-β polypeptide, the receptor polypeptide may be replaced with a masking antibody polypeptide (e.g., scFV or a nanobody) with affinity for the TGF-β polypeptide. [00314] One potential advantage of using an antibody (e.g., a single chain antibody) as a masking polypeptide is the ability to limit it to the isoform of the TGF-β polypeptide(s) to be masked. By way of example, single chain antibody sequences based on Metelimumab (CAT192) directed against TGF-β1 (e.g., Lord et al., mAbs 10(3): 444-452 (2018)) can be used to mask that TGF-β isoform when present in TGF-β constructs or complexes. In another embodiment, a single chain antibody sequence specific for TGF-β2 is used to mask that TGF-β isoform when present in TGF-β constructs or complexes. In another embodiment, a single chain antibody sequence specific for TGF-β3 is used to mask that TGF-β isoform when present in TGF-β constructs or complexes. Single chain antibodies can also be specific for a combination of TGF-β isoforms (e.g., ectodomain sequences appearing in masked TGF-β constructs or complexes selected from the group consisting of: TGF-β1 & TGF-β2; TGF-β1 & TGF-β3; and TGF-β2 & TGF-β3. The single chain antibodies may also be pan-specific for TGF-β1, TGF-β2, and TGF-β3 ectodomain sequences appearing in masked TGF-β constructs or complexes See e.g., WO 2014/164709. Antibodies and single chain antibodies that have the desired specificity and affinity for TGF-β isoforms can be prepared by a variety of methods, including screening hybridomas and/or modification (e.g., combinatorial modification) to the variable region sequence of antibodies that have affinity for a target TGF-β polypeptide sequence. [00315] In an embodiment, a masked TGF-β construct or complex comprises a single chain antibody to mask a TGF-β sequence (e.g., a TGF-β3 sequence). In one such embodiment the single chain amino acid sequence is specific for the TGF-β3 set forth in SEQ ID NO:111 comprising a C77S substitution (see SEQ ID NO:112). H. Linkers [00316] As noted above, a masked TGF-β construct or complex can include a linker peptide/polypeptide sequence interposed between any two elements of a masked TGF-β construct or complex. Although the term “linker” is employed, the same sequences described below as linkers may also be placed at the N- and/or C-terminus of a polypeptide of a masked TGF-β construct or complex for example as protection against proteolytic degradation. [00317] Suitable linkers (also referred to as “spacers”) can be readily selected and can be any of a number of suitable lengths, such as from 1 aa to 25 aa, from 3 aa to 20 aa, from 2 aa to 15 aa, from 3 aa to 12 aa, from 4 aa to 10 aa, from 5 aa to 9 aa, from 6 aa to 8 aa, or from 7 aa to 8 aa. A suitable linker can be 1, 2, 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 or 25 aa in length A suitable linker can be from 25 to 35 aa in length. A suitable linker can be 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, or 35 aa in length. A suitable linker can also be from 35 to 45 aa in length. A suitable linker can be 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, or 45 aa in length. A suitable linker can be from 45 to 50 aa in length. A suitable linker can be 45, 46, 47, 48, 49, or 50 aa in length. [00318] Exemplary linkers include those comprising glycine, or a polyglycine containing sequence from about 2 to about 50 (e.g., 2-4, 4-7, 7-10, 10-20, 20-35, or 35-50 ) contiguous glycine residues; glycine- serine polymers (including, for example, (GS) n , (GSGGS) n (SEQ ID NO:126) and (GGGS) n (SEQ ID NO:127), where n is an integer of at least one (e.g., 1-10, 10-20, or 20-30); glycine-alanine polymers or alanine-serine polymers (e.g., having a length of 1-10, 10-20, or 20-30aa); and other flexible linkers known in the art. Glycine and glycine-serine polymers can be used; both Gly and Ser are relatively unstructured, and therefore can serve as a neutral tether between components. Glycine polymers can be used; glycine assesses significantly more phi-psi space than even alanine, and is much less restricted than residues with longer side chains (see Scheraga, Rev. Computational Chem.11173-142 (1992)). Exemplary linkers can comprise amino acid sequences including, but not limited to, GGSG (SEQ ID NO:128), GGSGG (SEQ ID NO:129), GSGSG (SEQ ID NO:130), GSGGG (SEQ ID NO:131), GGGSG (SEQ ID NO:132), GSSSG (SEQ ID NO:133), and the like. Exemplary linkers can comprise, e.g., GGSG (SEQ ID NO:134) which may be repeated 2, 3, 4, 5, 6, 7, 8, 9, or 10 ten times. In some cases, a linker comprises the amino acid sequence (GSSSS) (SEQ ID NO:135) that may be repeated 2, 3, or 4 times. In some cases, a linker comprises the amino acid sequence (GSSSS) (SEQ ID NO:135) repeated four or five times. Exemplary linkers can include, e.g., (GGGGS) (SEQ ID NO:136), which can be repeated 2, 3, 4, 5, 6, 7, 8, 9, or 10 ten times. In some cases, a linker comprises the amino acid sequence (GGGGS) (SEQ ID NO:136) once or repeated 2 times. In some cases, a linker comprises the amino acid sequence (GGGGS) (SEQ ID NO:136) repeated 3 or 4 times. In some cases, a linker comprises the amino acid sequence (GGGGS) (SEQ ID NO:136) repeated 5, 6, or 7 times. In some cases, a linker comprises the amino acid sequence (GGGGS) (SEQ ID NO:136) repeated 8, 9, or 10 times. [00319] In some cases, a linker polypeptide present in a first polypeptide of a masked TGF-β complex includes a cysteine residue that can form a disulfide bond with a cysteine residue present in a second polypeptide of the masked TGF-β construct or complex. In some cases, for example, a suitable linker comprises the amino acid sequence GCGASGGGGSGGGGS (SEQ ID NO:137). I. Exemplary masked TGF-β constructs and complexes [00320] As discussed above, in any of the masked TGF-β constructs and complexes described in the present disclosure, the masking polypeptide that binds to and masks the TGF-β polypeptide sequences can take a variety of forms. The masking peptide may be an antibody, binding fragment of an antibody, a single chain antibody or portion thereof that binds TGF-β (e.g., an scFv), or nanobody; any of which may be humanized. The masking polypeptide may also be a TGF-β receptor fragment (e.g., the ectodomain sequences of TβRI, TβRII or TβRIII) that comprises polypeptide sequences sufficient to bind a TGF-β polypeptide (eg TGF β1 TGF β2 or TGF β3) [00321] In any of the above-mentioned masked TGF-β constructs and complexes, the TGF-β polypeptide sequence employed may be based upon TGF-β1, TGF-β2 or TGF-β3. In an embodiment the TGF-β polypeptide comprises a TGF-β3 sequence. Full length mature TGF-β protein sequence is not required in the masked TGF-β constructs and complexes, only the portion of TGF-β needed to interact with cell surface TβRII and permit the masked TGF-β complexes with cell surface TβRII to recruit TβRI and thereby initiate signaling (e.g. signaling through the Smad and non-Smad pathways). [00322] Although immunomodulatory polypeptide (MODs) are not required for the delivery of masked TGF-β or its ability to activate cells bearing TβRI and TβRII, as noted above, the presence of MODs can substantially affect the outcome of TGF-β cell activation. Consequently, the incorporation of MODs in any of the above-mentioned masked TGF-β constructs and complexes can be used to drive various outcomes, including therapeutic outcomes, from the use of the masked TGF-β constructs and complexes described herein. In an embodiment, the MODs present in a masked TGF-β construct or complex are selected from the group consisting of PD-L1, Fas-L, IL-2, IL-4, IL-6, IL-7, IL-21, IL-23, and variants of any thereof including those with reduced affinity for their co-MOD. [00323] While it may be desirable to incorporate MODs into masked TGF-β constructs and complexes, their presence is not necessary in all cases, particularly where the masked TGF-β constructs and complexes are administered along with other materials, including cytokines (e.g., one or more independently selected interleukin, lymphokine, interferon, chemokine, and/or tumor necrosis factor). For example, where it is desirable to support the development of conventional CD8+ T cells (or the survival of low affinity CD8+ T cells) by promoting thymocyte expression of the interleukin 7 receptor (e.g., IL-7Ra), masked TGF-β constructs and complexes without a MOD polypeptide (“MOD-less”) may be employed. Similarly, where it is desirable to promote the development of T-cell populations that are induced by strong agonist ligands, MOD-containing or MOD-less masked TGF-β constructs and complexes may be employed to support the survival of thymus-derived Treg (tTreg), invariant natural killer T (iNKT), and CD8αα+ T-cell precursors. [00324] The following are non-limiting examples of masked TGF-β constructs and complexes. 1 Masked TGF-β constructs [00325] In the case of masked TGF-β constructs, all of the components ( e.g., TGF-β, scaffold, a masking polypeptide such as a TβRII sequence, and optionally one or more MODs) are part of a single polypeptide chain (see, e.g., FIG 1, structure A). In such an embodiment, the scaffold polypeptide does not form a dimer or higher order structure with other scaffold polypeptides, and accordingly the masked TGF-β constructs are not in the form of homodimers, heterodimers or higher order multimer structures (trimers etc.). [00326] In the case of the masked TGF-β construct in FIG.1, Structure A the polypeptide may comprise, from N-terminus to C-terminus: optionally one or more MODs; a scaffold polypeptide (without an interspecific binding sequence); a polypeptide that binds to and masks the TGF-β polypeptide; and a TGF β polypeptide sequence Such masked TGF β constructs include those where: (i) the polypeptide comprises from N-terminus to C-terminus: optionally one or more independently selected wt. or reduced affinity variant MODs; a scaffold polypeptide (without an interspecific binding sequence); a TβR polypeptide that binds to and masks the TGF-β polypeptide; and a TGF-β polypeptide sequence; (ii) the polypeptide comprises from N-terminus to C-terminus: optionally one or more independently selected wt. or reduced affinity variant MODs; a scaffold polypeptide (without an interspecific binding sequence); a TβRII polypeptide that binds to and masks the TGF-β polypeptide; and a TGF-β polypeptide sequence; (iii) the polypeptide comprises from N-terminus to C-terminus: one or more independently selected wt. or reduced affinity variant MODs; a scaffold polypeptide (without an interspecific binding sequence); a TβR polypeptide that binds to and masks the TGF-β polypeptide; and a TGF-β polypeptide sequence; (iv) the polypeptide comprises from N-terminus to C-terminus: one or more independently selected wt. or reduced affinity variant IL-2 MODs; a scaffold polypeptide (without an interspecific binding sequence); a TβR polypeptide that binds to and masks the TGF-β polypeptide; and a TGF-β polypeptide sequence; (v) the polypeptide comprises from N-terminus to C-terminus: one or more independently selected wt. or reduced affinity variant MODs; a scaffold polypeptide (without an interspecific binding sequence); a TβR polypeptide that binds to and masks a TGF-β3 polypeptide; and a TGF-β3 polypeptide sequence; (vi) the polypeptide comprises from N-terminus to C-terminus: one or more independently selected wt. or reduced affinity variant MODs; a scaffold polypeptide (without an interspecific binding sequence); a TβRII polypeptide that binds to and masks a TGF-β3 polypeptide; and a TGF-β3 polypeptide sequence; and (vii) the polypeptide comprises from N-terminus to C-terminus: one or more independently selected wt. or reduced affinity variant IL-2 MODs; a scaffold polypeptide (without an interspecific binding sequence); a TβRII polypeptide that binds to and masks a TGF-β3 polypeptide; and a TGF-β3 polypeptide sequence. [00327] In any instance of the masked TGF-β constructs described herein, C77 of the TGF-β polypeptide sequence may be substituted to prevent dimerization (e.g., a C77S substitution), and the TGF-β polypeptide may further comprise variations to reduce their affinity for the masking TβR polypeptide (e.g., at one, two or all three of aas 25, 92 and/or 94), along with modifications in the MODs and the TβR polypeptide sequences. Exemplary TβR polypeptide sequences that may be incorporated into masked TGF-β constructs include Δ14 or Δ25 TβRII polypeptides optionally having a D118A or D118R substitution to attenuate TβRI engagement. MODs variants are described along with their polypeptide sequences and additional modifications of TβRI, TβRII, and TβRIII are described above. [00328] In an embodiment, a masked TGF-β construct has the sequence set forth in SEQ ID NO:146 (See FIG. 7A). In an embodiment, a masked TGF-β construct has the sequence set forth in SEQ ID NO:147 (See FIG.7B). In an embodiment, a masked TGF-β construct has the sequence set forth in SEQ ID NO157 (See FIG.7G). In an embodiment, a masked TGF-β construct has the sequence set forth in SEQ ID NO:158 (See FIG.7H). In an embodiment, a masked TGF-β construct has the sequence set forth in SEQ ID NO:159 (See FIG.7I). 2 Masked TGF-β complexes [00329] Masked TGF-β complexes comprise at least two polypeptides, a first and a second polypeptide, each of which contains a scaffold polypeptide that associates with another scaffold polypeptide, bringing the first and second polypeptides together into a complex. Consequently, TGF-β polypeptide complexes form homodimers, heterodimers, or higher order multimeric structures: (i) in a first instance, the masked TGF-β complex comprises at least one TGF-β polypeptide sequence, at least one polypeptide that binds to and masks the one or more TGF-β polypeptides (e.g., a masking sequence for each TGF-β polypeptide sequence), and optionally one or more immunomodulatory polypeptides (MODs) assembled on a scaffold structure that can dimerize to form a homodimer (e.g., a symmetrical dimer) as in FIG.1, structure B. In such homodimers, the Ig Fc polypeptides can permit the spontaneous formation of disulfide bonds between the Ig Fc polypetides in the scaffold of each construct, and may include mutations (e.g., the LALA mutations discussed herein) that substantially reduce or eliminate the ability of the Ig polypeptide to induce cell lysis, e.g., though complement-dependent cytotoxicity (CDC) and antibody- dependent cellular cytotoxicity (ADCC). (ii) in a second instance, a masked TGF-β complex comprises (a) a first polypeptide comprising at least one TGF-β polypeptide sequence, at least one polypeptide that binds to and masks the one or more TGF-β polypeptides (e.g., a masking sequence for each TGF-β polypeptide sequence), and optionally one or more immunomodulatory polypeptides (MODs) assembled on a scaffold structure comprising an interspecific dimerization sequence, and (b) a second polypeptide comprising at least one TGF-β polypeptide sequence, at least one polypeptide that binds to and masks the at least one TGF-β polypeptide, and optionally one or more immunomodulatory polypeptides (MODs) assembled on a scaffold structure comprising a counterpart to the interspecific dimerization sequence of the first polypeptide; where the first and second polypeptides form a heterodimer through interaction of the interspecific dimerization sequences as in FIG.1, structure C. (iii) in a third instance, a masked TGF-β complex comprises (a) a first polypeptide comprising at least one TGF-β polypeptide sequence, at least one polypeptide that binds to and masks the at least one or more TGF β polypeptides (eg a masking sequence for each TGF-β polypeptide sequence), and optionally one or more immunomodulatory polypeptides (MODs) assembled on a scaffold structure comprising an interspecific dimerization sequence, and (b) a second polypeptide comprising a scaffold structure comprising a counterpart to the interspecific dimerization sequence of the first polypeptide, and optionally one or more immunomodulatory polypeptides (MODs); where the first and second polypeptides form a heterodimer through interaction of the interspecific dimerization sequences as in FIG.1, structure F, and (iv) in a fourth instance, a masked TGF-β complex comprises (a) a first polypeptide comprising at least one TGF-β polypeptide sequence, and optionally one or more immunomodulatory polypeptides (MODs) assembled on a scaffold structure comprising an interspecific dimerization sequence, and (b) a second polypeptide comprising at least one polypeptide that binds to and masks the at least one or more TGF-β polypeptides, and optionally one or more immunomodulatory polypeptides (MODs) assembled on a scaffold structure comprising a counterpart to the interspecific dimerization sequence of the first polypeptide; where the first and second polypeptides form a heterodimer through interaction of the interspecific dimerization sequences as in FIG.1, structures D and E. [00330] In some instances, the masked TGF-β complexes (FIG.1, structures B, C and F), the sequence comprising the TGF-β polypeptide (the first polypeptide) may comprise, from N-terminus to C- terminus: optionally one or more MODs; a scaffold polypeptide (with or without an interspecific binding sequence); a polypeptide that binds to and masks the TGF-β polypeptide; and a TGF-β polypeptide sequence. The polypeptide not containing a TGF-β sequence in FIG.1, structure F, (the second polypeptide) comprises a scaffold polypeptide with an interspecific binding sequence and optionally comprises a MOD on the N-terminus, C-terminus, or both the N- and C-termini. [00331] In some instances, the masked TGF-β complexes in FIG.1, structures D and E, the TGF-β polypeptide sequence-containing polypeptide (the first polypeptide) may comprise, from N-terminus to C-terminus: one or more optional MODs; a scaffold polypeptide (with interspecific binding sequence); and a TGF-β polypeptide sequence. The polypeptide not containing a TGF-β sequence in FIG.1, structures D and E, (the second polypeptide) may comprise, from N-terminus to C-terminus: optionally one or more MODs, a scaffold polypeptide with an interspecific binding sequence, and a polypeptide that binds to and masks the TGF-β polypeptide. Although not illustrated in FIG. 1, the first polypeptide comprising the TGF-β polypeptide sequence may not comprise one or more MODs and the second poypeptide comprising the masking sequence may comprise one or more MODs. [00332] The above-described instances of masked TGF-β complexes include those where the first polypeptide comprises, from N-terminus to C-terminus: (i) optionally one or more MODs; a scaffold polypeptide (with an interspecific binding sequence); and a TGF-β polypeptide sequence; (ii) optionally one or more independently selected wt. or reduced affinity variant MODs; a scaffold polypeptide (with an interspecific binding sequence); and a TGF-β polypeptide sequence; (iii) one or more independently selected wt. or reduced affinity variant MODs; a scaffold polypeptide (with an interspecific binding sequence); and a TGF-β1 or 2 polypeptide sequence; (iv) one or more independently selected wt. or reduced affinity variant IL-2 MODs; a scaffold polypeptide (without an interspecific binding sequence); and a TGF-β polypeptide sequence; (v) one or more independently selected wt. or reduced affinity variant MODs; a scaffold polypeptide (with an interspecific binding sequence); and a TGF-β3 polypeptide sequence; (vi) one or more independently selected wt. or reduced affinity variant MODs; a scaffold polypeptide (with an interspecific binding sequence); and a TGF-β3 polypeptide sequence; or (vii) one or more independently selected wt. or reduced affinity variant IL-2 MODs; a scaffold polypeptide (with an interspecific binding sequence); and a TGF-β3 polypeptide sequence. In each instance, the second polypeptide comprises from N-terminus to C-terminus a scaffold polypeptide comprising the counterpart to the interspecific binding (dimerization sequence) of the first polypeptide followed by a TβR (e.g., a TβRII) polypeptide that binds to and masks the TGF-β polypeptide of the first polypeptide. In the case of a masked TGF-β complex as in FIG.1, structure F, a TβR (e.g., a TβRII) polypeptide may be interposed between the N-terminal MOD (if present) and the scaffold of the first polypeptide and the second polypeptide comprises the counterpart to the interspecific binding (dimerization sequence) of the first polypeptide to which one or more independently selected wt. or reduced affinity variant MODs (e.g., wt. or variant IL-2 MODs) may be attached at the N- or C-termini. [00333] In any instance of the masked TGF-β complexes described herein, C77 of the TGF-β polypeptide sequence may be substituted to prevent dimerization (e.g., a C77S substitution), and the TGF-β polypeptide may further comprise variations to reduce their affinity for the masking TβR polypeptide (e.g., at one, two or all three of aas 25, 92 and/or 94), along with modifications in the MODs and the TβR polypeptide sequences. Exemplary TβR polypeptide sequences that may be incorporated into masked TGF-β constructs include Δ14 or Δ25 TβRII polypeptides optionally having a D118A substitution. MODs variants are described along with their polypeptide sequences and additional modifications of TβRI, TβRII, and TβRIII are described above. [00334] In an embodiment, a masked TGF-β complex comprise polypeptides having the sequences set forth in SEQ ID NO:148 and 149 (See FIG.7C). In an embodiment, a masked TGF-β complex comprise polypeptides having the sequences set forth in SEQ ID NO:150 and 151 (See FIG.7D). In an embodiment, a masked TGF-β complex comprise polypeptides having the sequences set forth in SEQ ID NO:152 and 153 (See FIG.7E). In an embodiment, a masked TGF-β complex comprise polypeptides having the sequences set forth in SEQ ID NO:155 and 156 (See FIG.7F). In an embodiment, a masked TGF-β complex comprise polypeptides having the sequences set forth in SEQ ID NO:148 and 160 (See FIG.7J). J. Nucleic ACIDS [00335] The present disclosure provides a nucleic acid comprising a nucleotide sequence encoding masked TGF-β constructs and complexes. In some cases, the nucleic acid is a recombinant expression vector; thus, the present disclosure provides a recombinant expression vector comprising a nucleotide sequence encoding a masked TGF-β construct or complex. In some cases, the nucleic acid is a recombinant expression vector; thus, the present disclosure provides a recombinant expression vector comprising a nucleotide sequence encoding masked TGF-β constructs and complexes. The discussion, of nucleic acids that follows refers to nucleic acids encoding masked TGF-β constructs and complexes of the present disclosure. Nucleic acids encoding single-chain antigen-presenting polypeptides [00336] As described above, a masked TGF-β construct comprises a single polypeptide chain. Thus, the present disclosure provides a nucleic acid comprising a nucleotide sequence encoding a single-chain masked TGF-β construct. A nucleic acid comprising a nucleotide sequence encoding a single-chain masked TGF-β construct can be operably linked to a transcription control element(s), e.g., a promoter. Nucleic acid(s) encoding masked TGF-β complexes [00337] As noted above, in some cases, a masked TGF-β complex comprises at least two separate polypeptide chains (a first polypeptide chain and a second polypeptide chain). The present disclosure provides nucleic acids comprising nucleotide sequences encoding a masked TGF-β complex. In some cases, the individual polypeptide chains of a masked TGF-β complex are encoded in separate nucleic acids. In some cases, all polypeptide chains of a masked TGF-β construct or complex are encoded in a single nucleic acid. In some cases, a first nucleic acid comprises a nucleotide sequence encoding the first polypeptide of a masked TGF-β complex; and a second nucleic acid comprises a nucleotide sequence encoding the second polypeptide of a masked TGF-β complex. In some cases, single nucleic acid comprises a nucleotide sequence encoding the first and the second polypeptide of a masked TGF-β complex, which may be operably linked and under the transcriptional control of a single promoter or two independently selected promoters. Separate nucleic acids encoding individual polypeptide chains of a masked TGF-β construct or complex [00338] As noted above, in some cases, the individual polypeptide chains of a masked TGF-β complex are encoded by separate nucleic acids. In some cases, nucleotide sequences encoding the separate polypeptide chains of a masked TGF-β complex are operably linked to transcriptional control elements, e.g., promoters, such as promoters that are functional in a eukaryotic cell, where the promoter can be a constitutive promoter or an inducible promoter. [00339] For example, the present disclosure provides a first nucleic acid and a second nucleic acid, where the first nucleic acid comprises a nucleotide sequence encoding the first polypeptide of a masked TGF-β complex, and where the second nucleic acid comprises a nucleotide sequence encoding the second polypeptide of the masked TGF-β complex. In some cases, the nucleotide sequences encoding the first and the second polypeptides are operably linked to transcriptional control elements. In some cases, the transcriptional control element is a promoter that is functional in a eukaryotic cell. In some cases, the nucleic acids are present in separate expression vectors. [00340] In some cases, the nucleotide sequences encoding the first and the second polypeptides are operably linked to transcriptional control elements. In some cases, the transcriptional control element is a promoter that is functional in a eukaryotic cell. In some cases, the nucleic acids are present in separate expression vectors. Nucleic acid encoding two or more polypeptides present in a masked TGF-β complex [00341] The present disclosure provides a nucleic acid comprising nucleotide sequences encoding at least the first polypeptide and the second polypeptide of a masked TGF-β complex. In some cases, where a masked TGF-β complex includes a first, second, and third polypeptide, the nucleic acid includes a nucleotide sequence encoding the first, second, and third polypeptides. In some cases, the nucleotide sequences encoding the first polypeptide and the second polypeptide of a masked TGF-β complex encode a proteolytically cleavable site or linker interposed between the encoded first polypeptide and second polypeptide. In some cases, the nucleotide sequences encoding the first polypeptide and the second polypeptide of a masked TGF-β complex includes a nucleotide encoding an internal ribosome entry site (IRES) interposed between the encoded the first polypeptide and second polypeptides. In some cases, the nucleotide sequences encoding the first polypeptide and the second polypeptide of a masked TGF-β complex includes a sequence encoding a ribosome skipping signal (or cis-acting hydrolase element, CHYSEL) interposed between the nucleotide sequence encoding the first polypeptide and the nucleotide sequence encoding the second polypeptide. [00342] In some cases, the first nucleic acid (e.g., a recombinant expression vector, an mRNA, a viral RNA, etc.) comprises a nucleotide sequence encoding a first polypeptide chain of a masked TGF-β complex; and a second nucleic acid (e.g., a recombinant expression vector, an mRNA, a viral RNA, etc.) comprises a nucleotide sequence encoding a second polypeptide chain of a masked TGF-β complex. In some cases, the nucleotide sequence encoding the first polypeptide, and the second nucleotide sequence encoding the second polypeptide, are each operably linked to independently selected transcriptional control elements, e.g., promoters, such as promoters that are functional in a eukaryotic cell, where the promoter can be a constitutive promoter or an inducible promoter. Recombinant expression vectors [00343] The present disclosure provides recombinant expression vectors comprising nucleic acids. In some cases, the recombinant expression vector is a non-viral vector. In some cases, the recombinant expression vector is a viral construct, e.g., a recombinant adeno-associated virus construct (see, e.g., U.S. Patent No.7,078,387), a recombinant adenoviral construct, a recombinant lentiviral construct, a recombinant retroviral construct, a non-integrating viral vector, etc. [00344] Suitable expression vectors include, but are not limited to, viral vectors (e.g. viral vectors based on vaccinia virus; poliovirus; adenovirus (see, e.g., Li et al., Invest Opthalmol Vis Sci 35:25432549, 1994; Borras et al., Gene Ther 6:515524, 1999; Li and Davidson, PNAS 92:77007704, 1995; Sakamoto et al., H Gene Ther 5:10881097, 1999; WO 94/12649, WO 93/03769; WO 93/19191; WO 94/28938; WO 95/11984 and WO 95/00655); adeno-associated virus (see, e.g., Ali et al., Hum Gene Ther 9:8186, 1998, Flannery et al., PNAS 94:69166921, 1997; Bennett et al., Invest Opthalmol Vis Sci 38:28572863, 1997; Jomary et al., Gene Ther 4:683690, 1997, Rolling et al., Hum Gene Ther 10:641648, 1999; Ali et al., Hum Mol Genet 5:591594, 1996; Srivastava in WO 93/09239, Samulski et al., J. Vir. (1989) 63:3822-3828; Mendelson et al., Virol. (1988) 166:154-165; and Flotte et al., PNAS (1993) 90:10613-10617); SV40; herpes simplex virus; human immunodeficiency virus (see, e.g., Miyoshi et al., PNAS 94:1031923, 1997; Takahashi et al., J Virol 73:78127816, 1999); a retroviral vector (e.g., Murine Leukemia Virus, spleen necrosis virus, and vectors derived from retroviruses such as Rous Sarcoma Virus, Harvey Sarcoma Virus, avian leukosis virus, a lentivirus, human immunodeficiency virus, myeloproliferative sarcoma virus, and mammary tumor virus); and the like. Numerous suitable expression vectors are known to those of skill in the art, and many are commercially available. [00345] Depending on the host/vector system utilized, any of a number of suitable transcription and translation control elements, including constitutive and inducible promoters, transcription enhancer elements, transcription terminators, etc. may be used in the expression vector (see e.g., Bitter et al. (1987) Methods in Enzymology, 153:516-544). [00346] In some cases, a nucleotide sequence encoding the polypeptides of masked TGF-β constructs and complexes are operably linked to a control element, e.g., a transcriptional control element, such as a promoter. The transcriptional control element may be functional in either a eukaryotic cell, e.g., a mammalian cell; or a prokaryotic cell (e.g., bacterial or archaeal cell). In some cases, a nucleotide sequence encoding a DNA-targeting RNA and/or a site-directed modifying polypeptide is operably linked to multiple control elements that allow expression of the nucleotide sequence encoding a DNA- targeting RNA and/or a site-directed modifying polypeptide in both prokaryotic and eukaryotic cells. [00347] Non-limiting examples of suitable eukaryotic promoters (promoters functional in a eukaryotic cell) include those from cytomegalovirus (CMV) immediate early, herpes simplex virus (HSV) thymidine kinase, early and late SV40, long terminal repeats (LTRs) from retrovirus, and mouse metallothionein-I. Selection of the appropriate vector and promoter is well within the level of ordinary skill in the art. The expression vector may also contain a ribosome binding site for translation initiation and a transcription terminator. The expression vector may also include appropriate sequences for amplifying expression. Preparation of genetically modified host cells expressing masked TGF-β constructs and complexes and purification of masked TGF-β constructs and complexes [00348] The present disclosure provides a genetically modified host cell, where the host cell is genetically modified with one or more nucleic acid(s) encoding a masked TGF-β construct or complex. [00349] Suitable host cells include eukaryotic cells, such as yeast cells, insect cells, and mammalian cells. In some cases, the host cell is a cell of a mammalian cell line. Suitable mammalian cell lines include human cell lines, non-human primate cell lines, rodent (e.g., mouse, rat) cell lines, and the like. Suitable mammalian cell lines include, but are not limited to, HeLa cells (e.g., American Type Culture Collection (ATCC) No. CCL-2), CHO cells (e.g., ATCC Nos. CRL9618, CCL61, CRL9096), 293 cells (e.g., ATCC No. CRL-1573), Vero cells, NIH 3T3 cells (e.g., ATCC No. CRL-1658), Huh-7 cells, BHK cells (e.g., ATCC No. CCL10), PC12 cells (ATCC No. CRL1721), COS cells, COS-7 cells (ATCC No. CRL1651), RAT1 cells, mouse L cells (ATCC No. CCLI.3), human embryonic kidney (HEK) cells (ATCC No. CRL1573), HLHepG2 cells, and the like. [00350] Genetically modified host cells can be used to produce a masked TGF-β construct or complex. For example, a genetically modified host cell can be used to produce a masked TGF-β complex, or a single-chain masked TGF-β construct by introducing expression vector(s), such as those described above, comprising nucleotide sequences encoding the polypeptide(s) into a host cell, generating thereby producing a genetically modified host cell. The host cell may constitutively express the masked TGF-β construct or complex, or express it in response to exposure to an inducer where the promoters driving expression are inducible (e.g., a CMV promoter and a tetracycline resistance operon induced by exposure to tetracycline). [00351] The masked TGF-β construct or complex is obtained from the cells, or if the polypeptide(s) are targeted to the secretory pathway by incorporation of signal sequences, from the cell culture media. The protein may be purified by any means known in the art including, for example, one or more of precipitation (e.g., ammonium sulfate or ethanol), isoelectric focusing, and one or more types of chromatography. Suitable chromatographic methods include, but are not limited to, size-based chromatographic separation (e.g., size exclusion or gel permeation), hydrophobic interaction chromatography, ion-exchange chromatography, and affinity chromatography. Where the masked TGF- β construct or complex comprises an immunoglobulin polypeptide sequence (e.g., as a scaffold) the protein A or protein G may be used to affinity purify the masked TGF-β construct or complex. In the absence of an immunoglobulin polypeptide, the complex may be affinity purified using an antibody directed a polypeptide present in the masked TGF-β construct or complex; or alternatively, by incorporation of an affinity tag such as a myc epitope (CEQKLISEEDL SEQ ID NO:154), “HIS” tag (for divalent metal ion resin binding), or a “FLAG” tag. A purification and/or concentration step that may be combined with any of the foregoing methods employs size limited semipermeable membrane (e.g., a dialysis membrane or pressure cell), which may be used to remove contaminants having a substantially different molecular weight and/or to concentrate the purified protein. [00352] In an embodiment, a masked TGF-β construct or complex is expressed from a nucleic acid sequence introduced into a mammalian cell (e.g., a CHO cell) and targeted to the secretory pathway such that it is excreted from the cell into its culture media (e.g., a serum free media). The masked TGF- β construct or complex is purified from the cell culture media using affinity chromatography alone or in combination with sized-based separation (e.g., size-based chromatographic or membrane separation). In a specific example of such an embodiment, the masked TGF-β construct or complex comprises an immunoglobulin scaffold (e.g., an IgG polypeptide sequence), and purification is accomplished by affinity chromatography (e.g., protein A or G) alone or in combination with sized based separation (size- based chromatography). K. Compositions [00353] The present disclosure provides compositions, including pharmaceutical compositions, comprising a masked TGF-β construct or complex. The present disclosure also provides compositions, including pharmaceutical compositions, comprising a nucleic acid or a recombinant expression vector. 1 Compositions comprising a masked TGF-β construct or complex [00354] A composition of the present disclosure can comprise, in addition to a masked TGF-β construct or complex, one or more of: a salt, e.g., NaCl, MgCl 2 , KCl, MgSO 4 , etc.; a buffering agent, e.g., a Tris buffer, N-(2-hydroxyethyl)piperazine-N'-(2-ethanesulfonic acid) (HEPES), 2-(N-morpholino) ethanesulfonic acid (MES), 2-(N-Morpholino)ethanesulfonic acid sodium salt (MES), 3-(N-morpholino) propanesulfonic acid (MOPS), N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid (TAPS), etc.; a solubilizing agent; a detergent, e.g., a non-ionic detergent such as Tween-20, etc.; a protease inhibitor; glycerol; and the like. [00355] The composition may comprise a pharmaceutically acceptable excipient, a variety of which are known in the art and need not be discussed in detail herein. Pharmaceutically acceptable excipients have `been amply described in a variety of publications, including, for example, “Remington: The Science and Practice of Pharmacy”, 19 th Ed. (1995), or latest edition, Mack Publishing Co; A. Gennaro (2000) "Remington: The Science and Practice of Pharmacy", 20th edition, Lippincott, Williams, & Wilkins; Pharmaceutical Dosage Forms and Drug Delivery Systems (1999) H.C. Ansel et al., eds 7 th ed., Lippincott, Williams, & Wilkins; and Handbook of Pharmaceutical Excipients (2000) A.H. Kibbe et al., eds., 3 rd ed. Amer. Pharmaceutical Assoc. [00356] A pharmaceutical composition can comprise: i) a masked TGF-β construct or complex; and ii) a pharmaceutically acceptable excipient. In some cases, a subject pharmaceutical composition will be suitable for administration to a subject, e.g., will be sterile. For example, in some embodiments, a subject pharmaceutical composition will be suitable for administration to a human subject, e.g., where the composition is sterile and is substantially free of detectable pyrogens and/or other toxins, or where such detectable pyrogens and/or other toxins are present at a level within acceptable limits set by an applicable regulatory agency, e.g., the USF&DA. [00357] The protein compositions may comprise other components, such as pharmaceutical grades of mannitol, lactose, starch, magnesium stearate, sodium saccharin, talcum, cellulose, glucose, sucrose, magnesium, carbonate, and the like. The compositions may contain pharmaceutically acceptable auxiliary substances as required to approximate physiological conditions such as pH adjusting and buffering agents, toxicity adjusting agents and the like, for example, sodium acetate, sodium chloride, potassium chloride, calcium chloride, sodium lactate, hydrochloride, sulfate salts, solvates (e.g., mixed ionic salts, water, organics), hydrates (e.g., water), and the like. [00358] For example, compositions may include aqueous solution, powder form, granules, tablets, pills, suppositories, capsules, suspensions, sprays, and the like. The composition may be formulated according to the various routes of administration described below. [00359] Where a masked TGF-β construct or complex is utilized (e.g., introduced into a cell culture system) or administered (e.g., subcutaneously, intraperitoneally, intramuscularly, intralymphatically, and/or intravenously) as an injectable directly into a tissue, a formulation can be provided as a ready-to- use dosage form, or as non-aqueous form (e.g. a storage-stable powder that can be reconstituted) or aqueous form, such as liquid composed of pharmaceutically acceptable carriers and excipients. The protein-containing formulations may also be provided in a form that enhances serum half-life of the subject protein following administration. For example, the protein may be provided in a liposome formulation, prepared as a colloid, or other conventional techniques for extending serum half-life. A variety of methods are available for preparing liposomes, as described in, e.g., Szoka et al.1980 Ann. Rev. Biophys. Bioeng.9:467, U.S. Pat. Nos.4,235,871, 4,501,728 and 4,837,028. The preparations may also be provided in controlled release or slow-release forms. [00360] In some cases, a composition comprises: a) a masked TGF-β construct or complex; and b) saline (e.g., 0.9% NaCl). In some cases, the composition is sterile. In some cases, the composition is suitable for administration to a human subject, e.g., where the composition is sterile and is substantially free of detectable pyrogens and/or other toxins, or where such detectable pyrogens and/or other toxins are present in an amount within acceptable limits. Thus, the present disclosure provides a composition comprising: a) a masked TGF-β construct or complex; and b) saline (e.g., 0.9% NaCl), where the composition is sterile and is substantially free of detectable pyrogens and/or other toxins, or where such detectable pyrogens and/or other toxins are present in an amount within acceptable limits. [00361] Other examples of formulations suitable for parenteral administration include isotonic sterile injection solutions, anti-oxidants, bacteriostats, and solutes that render the formulation isotonic with the blood of the intended recipient, suspending agents, solubilizers, thickening agents, stabilizers, and preservatives. For example, a subject pharmaceutical composition can be present in a container, e.g., a sterile container, such as a syringe. The formulations can be presented in unit-dose or multi-dose sealed containers, such as ampules and vials, and can be stored in a freeze-dried (lyophilized) condition requiring only the addition of the sterile liquid excipient, for example, water, for injections, immediately prior to use. Extemporaneous injection solutions and suspensions can be prepared from sterile powders, granules, and tablets. [00362] The concentration of a masked TGF-β construct or complex in a formulation can vary widely such as from less than about 0.1% (usually at or at least about 2%) to as much as 20% to 50% or more by weight (e.g., from 0.1% to 1%, 1% to 5%.5% to 10%, 10% to 20%, or 20% to 50% by weight) and will usually be selected primarily based on fluid volumes, viscosities, and patient-based factors in accordance with the particular mode of administration selected and the patient's needs. [00363] The present disclosure provides a container comprising a composition, e.g., a liquid composition. The container can be, e.g., a syringe, an ampoule, and the like. In some cases, the container is sterile. In some cases, both the container and the composition are sterile. 2 Compositions comprising a nucleic acid or a recombinant expression vector [00364] The present disclosure provides compositions, e.g., pharmaceutical compositions, comprising a nucleic acid or a recombinant expression vector of the present disclosure. A wide variety of pharma- ceutically acceptable excipients is known in the art and need not be discussed in detail herein. Pharma- ceutically acceptable excipients have been amply described in a variety of publications, including, for example, A. Gennaro (2000) "Remington: The Science and Practice of Pharmacy", 20th edition, Lippincott, Williams, & Wilkins; Pharmaceutical Dosage Forms and Drug Delivery Systems (1999) H. C. Ansel et al., eds 7th ed., Lippincott, Williams, & Wilkins; and Handbook of Pharmaceutical Excipients (2000) A. H. Kibbe et al., eds., 3rd ed. Amer. Pharmaceutical Assoc. [00365] A composition of the present disclosure can include: a) one or more nucleic acids or one or more recombinant expression vectors comprising nucleotide sequences encoding a masked TGF-β construct or complex; and b) one or more of: a buffer, a surfactant, an antioxidant, a hydrophilic polymer, a dextrin, a chelating agent, a suspending agent, a solubilizer, a thickening agent, a stabilizer, a bacteriostatic agent, a wetting agent, and a preservative. Suitable buffers include, but are not limited to, (such as N,N-bis(2-hydroxyethyl)-2-aminoethanesulfonic acid (BES), bis(2-hydroxyethyl)amino- tris(hydroxymethyl)methane (BIS-Tris), N-(2-hydroxyethyl)piperazine-N'3-propanesulfonic acid (EPPS or HEPPS), glycylglycine, N-2-hydroxyehtylpiperazine-N'-2-ethanesulfonic acid (HEPES), 3-(N- morpholino)propane sulfonic acid (MOPS), piperazine-N,N'-bis(2-ethane-sulfonic acid) (PIPES), sodium bicarbonate, 3-(N-tris(hydroxymethyl)-methyl-amino)-2-hydroxy-propanesulf onic acid) TAPSO, (N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid (TES), N- tris(hydroxymethyl)methyl-glycine (Tricine), tris(hydroxymethyl)-aminomethane (Tris), etc.). Suitable salts include, e.g., NaCl, MgCl2, KCl, MgSO4, etc. [00366] A pharmaceutical formulation can include a nucleic acid or recombinant expression vector in an amount of from about 0.001% to about 99% (w/w ) (e.g., 0.001-0.1, 0.1-1.0, 1.0-10, 10-20, 20-40, 40- 80, or 80-100 percent w/w). In the description of formulations, below, “subject nucleic acid or recombinant expression vector” will be understood to include a nucleic acid or recombinant expression vector. For example, in some cases, a subject formulation comprises a nucleic acid or recombinant expression vector. [00367] A subject nucleic acid or recombinant expression vector can be admixed, encapsulated, conjugated or otherwise associated with other compounds or mixtures of compounds; such compounds can include, e.g., liposomes or receptor-targeted molecules. A subject nucleic acid or recombinant expression vector can be combined in a formulation with one or more components that assist in uptake, distribution and/or absorption. [00368] A subject nucleic acid or recombinant expression vector composition can be formulated into any of many possible dosage forms such as, but not limited to, tablets, capsules, gel capsules, liquid syrups, soft gels, suppositories, and enemas. A subject nucleic acid or recombinant expression vector composition can also be formulated as suspensions in aqueous, non-aqueous or mixed media. Aqueous suspensions may further contain substances which increase the viscosity of the suspension including, for example, sodium carboxymethylcellulose, sorbitol and/or dextran. The suspension may also contain stabilizers. [00369] A formulation comprising a subject nucleic acid or recombinant expression vector can be a liposomal formulation. As used herein, the term "liposome" means a vesicle composed of amphiphilic lipids arranged in a spherical bilayer or bilayers. Liposomes are unilamellar or multilamellar vesicles which have a membrane formed from a lipophilic material and an aqueous interior that contains the composition to be delivered. Cationic liposomes are positively charged liposomes that can interact with negatively charged DNA molecules to form a stable complex. Liposomes that are pH sensitive or negatively charged are believed to entrap DNA rather than complex with it. Both cationic and noncationic liposomes can be used to deliver a subject nucleic acid or recombinant expression vector. [00370] Liposomes also include "sterically stabilized" liposomes, a term which, as used herein, refers to liposomes comprising one or more specialized lipids that, when incorporated into liposomes, result in enhanced circulation lifetimes relative to liposomes lacking such specialized lipids. Examples of sterically stabilized liposomes are those in which part of the vesicle-forming lipid portion of the liposome comprises one or more glycolipids or is derivatized with one or more hydrophilic polymers, such as a polyethylene glycol (PEG) moiety. Liposomes and their uses are further described in U.S. Pat. No.6,287,860, which is incorporated herein by reference in its entirety. [00371] The formulations and compositions may also include surfactants. The use of surfactants in drug products, formulations and in emulsions is well known in the art. Surfactants and their uses are further described in U.S. Pat. No.6,287,860. [00372] In one embodiment, various penetration enhancers are included, to effect the efficient delivery of nucleic acids. In addition to aiding the diffusion of non-lipophilic drugs across cell membranes, penetration enhancers also enhance the permeability of lipophilic drugs. Penetration enhancers may be classified as belonging to one of five broad categories, i.e., surfactants, fatty acids, bile salts, chelating agents, and non-chelating non-surfactants. Penetration enhancers and their uses are further described in U.S. Pat. No.6,287,860, which is incorporated herein by reference in its entirety. [00373] Compositions and formulations for oral administration include powders or granules, microparticulates, nanoparticulates, suspensions or solutions in water or non-aqueous media, capsules, gel capsules, sachets, tablets, or minitablets. Thickeners, flavoring agents, diluents, emulsifiers, dispersing aids or binders may be desirable. Suitable oral formulations include those in which a subject antisense nucleic acid is administered in conjunction with one or more penetration enhancers surfactants and chelators. Suitable surfactants include, but are not limited to, fatty acids and/or esters or salts thereof, bile acids and/or salts thereof. Suitable bile acids/salts and fatty acids and their uses are further described in U.S. Pat. No.6,287,860. Also suitable are combinations of penetration enhancers, for example, fatty acids/salts in combination with bile acids/salts. An exemplary suitable combination is the sodium salt of lauric acid, capric acid, and UDCA. Further penetration enhancers include, but are not limited to, polyoxyethylene-9-lauryl ether, and polyoxyethylene-20-cetyl ether. Suitable penetration enhancers also include propylene glycol, dimethylsulfoxide, triethanolamine, N,N-dimethylacetamide, N,N-dimethylformamide, 2-pyrrolidone and derivatives thereof, tetrahydrofurfuryl alcohol, and AZONE™. L. Formulations [00374] Suitable formulations are described above, where the compositions are of pharmaceutically acceptable grade (e.g., the compositions include a pharmaceutically acceptable excipient(s) and active molecules). In some cases, a suitable formulation comprises: a) a masked TGF-β construct or complex; and b) a pharmaceutically acceptable excipient. In some cases, a suitable formulation comprises: a) a nucleic acid comprising a nucleotide sequence encoding a masked TGF-β construct or complex; and b) a pharmaceutically acceptable excipient; in some instances, the nucleic acid is an mRNA. In some cases, a suitable formulation comprises: a) a first nucleic acid comprising a nucleotide sequence encoding the first polypeptide of a masked TGF-β construct or complex; b) a second nucleic acid comprising a nucleotide sequence encoding the second polypeptide of a masked TGF-β construct or complex; and c) a pharmaceutically acceptable excipient. In some cases, a suitable formulation comprises: a) a recombinant expression vector comprising a nucleotide sequence encoding a masked TGF-β construct or complex; and b) a pharmaceutically acceptable excipient. In some cases, a suitable formulation comprises: a) a first recombinant expression vector comprising a nucleotide sequence encoding the first polypeptide of a masked TGF-β construct or complex; b) a second recombinant expression vector comprising a nucleotide sequence encoding the second polypeptide of a masked TGF-β construct or complex; and c) a pharmaceutically acceptable excipient. Suitable pharmaceutically acceptable excipients are described above. M. Methods [00375] A masked TGF-β construct or complex is useful for modulating an activity of a T cell. Thus, the present disclosure provides methods of modulating an activity of a T cell, the methods generally involving contacting a target T cell with a masked TGF-β construct or complex. 1 Methods of modulating immune cell activity including generating, stimulating or inhibiting specific immune cell types. [00376] The present disclosure provides a method of selectively modulating the activity of cells that express TβRI and TβRII, the method comprising contacting the cell (e.g., T cells, B cells, and innate cells, including natural killer (NK) cells, macrophages, dendritic cells, and granulocytes) with a masked TGF-β construct or complex, where contacting the T cell with a masked TGF-β construct or complex selectively modulates the activity of the epitope-specific T cell. In some cases, the contacting occurs in vitro. In some cases, the contacting occurs in vivo. Wherein the activity of the cells (e.g., signaling through canonical pathway, non-canonical pathways, and/or downstream gene expression) subject to a masked TGF-β construct or complex may be assessed relative to treatment groups (e.g., cells subjects) that have not been exposed to TGF-β or a masked TGF-β construct or complex. [00377] The present disclosure provides a method of reducing the number and/or activity of T cells or B cells (e.g., pathogenic autoreactive T cells and/or pathogenic autoreactive B cells); the method comprising administering (e.g., to a subject in need thereof) one or more masked TGF-β constructs or complexes. In some cases, the method increases the number and/or activity of a regulatory T cell (Treg), resulting in reduced number and/or activity of T cells or B cells (e.g., one or more autoreactive T cells and/or one or more autoreactive B cells), wherein the reduction in the number and/or activity of T cells or B cells subjected to one or more masked TGF-β constructs or complexes is assessed relative to treatment groups (e.g., cells subjects) that have not been exposed to TGF-β or one or more masked TGF- β constructs or complexes. [00378] Administration of one or more masked TGF-β constructs or complexes, optionally comprising one or more (e.g., one, two or more or three or more) independently selected wildtype or variant MODs may directly or indirectly effect various cell populations. By way of example, administration of masked TGF-β constructs or complexes, optionally comprising one or more wild type or variant IL-2 MODs may directly stimulate the development and/or survival of FoxP3+ Treg cells (in vivo or in vitro). In addition to any direct action that a TGF-β/IL-2 complex has on various immune cells, the resultant Treg cells can suppress immune responses by, for example, blocking induction of T cell activation and/or the effector phase of T cell responses, suppressing B cell activation, and/or inhibiting the differentiation and/or proliferation of natural killer cells. a. Tregs (i) tTregs, pTregs, iTregs and TGF-β constructs or complexes comprising IL-2 [00379] The present disclosure provides a method of promoting the development (e.g. expansion) and/or survival of thymus-derived Treg (tTreg) and/or peripheral Treg (pTreg) (Tregs are CD4 + , FoxP3 + , and CD25 + cells that can suppress autoreactive T cells and B cells); the method comprising administering (e.g., to one or more subjects in need thereof), or contacting CD4+ T cells (e.g., naïve CD4+ T cells) with, one or more masked TGF-β constructs or complexes; (e.g., in tissue culture, blood, or in a specific tissue location such as a wound). The one or more masked TGF-β constructs or complexes administered or contacted in the method may comprise one or more (e.g., one, two or three) independently selected IL-2 MOD polypeptide sequences and/or variant IL-2 MOD polypeptide sequences. Administration or contacting may be conducted in conjunction with the administration or contacting of the cells with vitamin D (e.g., Vitamin D3 or an analog thereof), retinoic acid (e.g., all trans retinoic acid), and /or an inhibitor of the mammalian target of rapamycin (mTOR) (e.g., rapamycin or a functional analog thereof such as sirolimus, everolimus or temsirolimus). Accordingly, the present disclosure provides a method of promoting the development and/or survival of induced regulatory T cells (iTregs), which are FoxpP3+, FoxP3+ thymus derived Treg (tTreg) and/or FoxP3+ peripheral Treg (pTreg), the method comprising administering (e.g., to a subject in need thereof), or contacting CD4+ T cells (e.g., naïve CD4+ T cells) with, one or more masked TGF-β constructs or complexes that comprises one or more IL- 2 MOD polypeptide sequences and/or variant IL-2 MOD polypeptide sequences, optionally in the presence of vitamin D or an analog thereof, retinoic acid (e.g., all trans retinoic acid) or an analog thereof, and /or rapamycin or an analog thereof. The effects of administration or treatment with one or more masked TGF-β constructs or complexes may be assessed relative the baseline value (e.g., number of cells prior to treatment) or relative to a treatment group (e.g., cells or subjects) that are matched with a test group (e.g., otherwise identical to), but that have not been exposed to TGF-β or one or more masked TGF-β constructs or complexes. [00380] The present disclosure provides a method of increasing the induction/proliferation of Tregs, maintaining Tregs and/or sustaining their function, the method comprising contacting T cells (e.g., CD4+ T cell in vivo or in vitro) with one or more masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected IL-2 MOD polypeptide sequences and/or variant IL-2 MOD polypeptide sequences. The contacting increases the induction/proliferation of Tregs, maintains the Tregs, and/or sustains their function either relative to a baseline value determined prior to the contacting or relative to a control group of otherwise identical cells that have not been contacted with the one or more masked TGF-β constructs or complexes. The disclosure includes and provides for masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected IL-2 MOD polypeptide sequences and/or variant IL-2 MOD polypeptide sequences for use in the method. In an embodiment, the masked TGF-β constructs or complexes comprising one or more ( t th ) i d d tl l t d IL 2 MOD l tid d/ i t IL 2 MOD polypeptide sequences has the structural organization described in FIG.1 strucures A, B or C. In an embodiment, the masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected IL-2 MOD polypeptide sequences and/or variant IL-2 MOD polypeptide sequences has the structural organization described in FIG.1 strucures D or E. In an embodiment, the masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected IL-2 MOD polypeptide sequences and/or variant IL-2 MOD polypeptide sequences has the structural organization described in FIG.1 strucure F. [00381] The present disclosure provides a method of increasing the induction/proliferation of Tregs, maintaining Tregs and/or sustaining their function, the method comprising contacting T cells (e.g., CD4+ T cell in vivo or in vitro) with one or more masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected PD-L1 or PD-L2 MOD polypeptide sequences and/or variant PD-L1or PD-L2 MOD polypeptide sequences. The contacting increases the induction/proliferation of Tregs, maintains the Tregs, and/or sustains their function either relative to a baseline value determined prior to the contacting or relative to a control group of otherwise identical cells that have not been contacted with the one or more masked TGF-β constructs or complexes. The disclosure includes and provides for masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected PD-L1 or PD-L2 MOD polypeptide sequences and/or variant PD-L1 or PD-L2 MOD polypeptide sequences for use in the method. In an embodiment, the masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected PD-L1 or PD-L2 MOD polypeptide sequences and/or variant PD-L1 or PD-L2 MOD polypeptide sequences has the structural organization described in FIG.1 strucures A, B or C. In an embodiment, the masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected PD-L1 MOD polypeptide sequences and/or variant PD-L1 or PD-L2 MOD polypeptide sequences has the structural organization described in FIG.1 strucures D or E. In an embodiment, the masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected PD-L1 or PD-L2 MOD polypeptide sequences and/or variant PD-L1 or PD-L2 MOD polypeptide sequences has the structural organization described in FIG.1 strucure F. Masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected PD-L1 or PD-L2 MOD polypeptide sequences and/or variant PD-L1 or PD-L2 MOD polypeptide sequences may be administered wth IL-2 (e.g. recombinanat IL-2 such as Proleukin (aldesleukin)) for the induction/proliferation of Tregs (e.g., Tbet+ FoxP3+ iTreg cells), maintaining Tregs, and/or sustaining their function. [00382] The present disclosure provides a method for increasing the induction/proliferation of Tregs, maintaining Tregs (e.g. Treg numbers), and/or sustaining their function, the method comprising contacting T cells(e.g., CD4+ cells in vivo or in vitro) with one or more masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected IL-2 and/or variant IL-2 MOD polypeptide sequences, and one or more independently selected wt. or variant PD-L1 and/or PD-L2 MOD polypeptide sequences. The contacting increases the induction/proliferation of Tregs, maintains the Tregs, and/or sustains their function either relative to a baseline value determined prior to the contacting or relative to a control group of otherwise identical cells that have not been contacted with the one or more masked TGF-β constructs or complexes. The disclosure includes and provides for masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected IL-2 MOD and/or variant IL-2 MOD polypeptide sequences and one or more independently selected wt. or variant PD-L1 and/or PD-L2 polypeptide sequences for use in the method. In an embodiment, the masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected IL-2 MOD and/or variant IL-2 MOD polypeptide sequences and one or more independently selected wt. or variant PD-L1 and/or PD-L2 polypeptide sequences has the structural organization described in FIG.1 strucures A, B or C. In an embodiment, the masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected IL-2 MOD and/or variant IL-2 MOD polypeptide sequences and one or more independently selected wt. or variant PD-L1 and/or PD-L2 polypeptide sequences has the structural organization described in FIG.1 strucures D or E. In an embodiment, the masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected IL-2 MOD and/or variant IL-2 MOD polypeptide sequences and one or more independently selected wt. or variant PD-L1 and/or PD-L2 polypeptide sequences has the structural organization described in FIG.1 structure F. [00383] Contacting T cells (e.g., naieve CD4+ cells) with masked TGF-β constructs or complexes (e.g., in vivo or in vitro) comprising one or more (e.g., one, two or three) independently selected IL-2 MOD and/or variant IL-2 MOD polypeptide sequences, alone or in combination with one or more independently selected wt. or variant PD-L1 and/or PD-L2 MOD polypeptide sequences can increase the expression of FoxP3 and Treg cell induction (e.g., Tbet+ FoxP3+ iTreg cells). Similarly, contacting T cells (e.g., naieve CD4+ cells) with masked TGF-β constructs or complexes (e.g., in vitro or in vivo) comprising one or more (e.g., one, two or three) independently selected PD-L1 or PDL2 and/or variant PD-L1 or PD-L2 MOD polypeptide sequences, alone or in combination with IL-2 (e.g., recombinant human IL-2) can increase the expression of FoxP3 and Treg cell induction (e.g., Tbet+ FoxP3+ iTreg cells). Where both IL-2 and either PD-L1 or PD-L2 are provided to the cells the contacting may reduce T reg endolysosomal asparaginyl endopeptidase. Reduction in endolysosomal asparaginyl endopeptidase, which is responsible for destabilizing Foxp3 in Tregs, results in maintenance of Tregs (e.g., iTregs) and sustains their function. See, e.g., Francsisco et al., J Exp. Med., 206(13) 3015-3029 (2018) and Stathopoulou et al. Immunity 49(2): 247–263 (2018). Accordingly, where the masked TGF- β constructs or complexes comprise both IL-2 and either PD-L1 or PD-L2, contacting the T-cells may result not only in increased numbers of Treg, but also increased stability and function of those cells. [00384] Where contacting of masked TGF-β constructs or complexes comprising IL-2 MOD (wt. and/or variant) and/or PD-L1 and/or PD-L2 (wt. and/or variant) polypeptide sequences occurs in vivo (or in vitro with the treated cells administered to patient), the contacting may constitute treatment. Such treatments result in increased Treg cell levels (e.g., total number of iTregs or their fraction in a tissue or circulating in blood) in an individual or population of individuals. The treatment may also result in elevated levels of FoxP3 in Tregs. [00385] Where the masked TGF-β constructs or complexes comprise wt. and/or variant IL-2 MOD polypeptide sequence(s) in combination with wt. or variant PD-L1 and/or PD-L2 MOD polypeptide sequence(s) the increased Treg cell levels (e.g., total number of iTregs or their fraction in a tissue or circulating in blood) in an individual or population of individuals persists for a longer period of time than is observed when treating an individual or population of individuals (e.g., matched for age, gender, weight, and/or disease status) with an otherwise identical masked TGF-β construct or complex lacking the PD-L1 sequence(s). Treatment with masked TGF-β constructs or complexes comprising wt. and/or variant IL-2 MOD polypeptide sequences in combination with wt. or variant PD-L1 and/or PD-L2 MOD polypeptide sequences may also result in persistantly elevated levels of FoxP3 in Tregs relative to the levels observed when the treatment is conducted with an otherwise identical masked masked TGF-β construct or complex that lacks PD-L1 polypeptide sequences. Treatment with masked TGF-β constructs or complexes comprising wt. and/or variant IL-2 MOD polypeptide sequences in combination with wt. or variant PD-L1 and/or PD-L2 MOD polypeptide sequences may also result in reduced activity of endolysosomal asparaginyl endopeptidase in Treg cells relative to the activity of that enzyme in T- cells of an individual (or group of individuals on average) that have been treated with an otherwise identical masked masked TGF-β construct or complex that lacks PD-L1 MOD polypeptide sequences. [00386] The process of contacting T-cells, with masked TGF-β constructs or complexes comprising wt. and/or variant IL-2 MOD polypeptide sequences alone or in combination with wt. or variant PD-L1 and/or PD-L2 MOD polypeptide sequences (e.g., in vitro, ex vivio or in vivo such as in a process of treating an individual), may further comprise contacting the T cells presence of vitamin D or an analog thereof, retinoic acid (e.g., all trans retinoic acid) or an analog thereof, and/or an mTOR inhibitor such as rapamycin or an analog thereof). Contacting in the presences of those agents may increase level of Tregs (e.g., number or relative number of Tregs in an individual or tissue due to proliferation or maintence of cells with the Treg phenotype) either relative to a baseline value determined prior to the contacting or relative to a the value determine in a control group (e.g., a group of individuals) that have not been contacted with the one or more masked TGF-β constructs or complexes. Where control groups of individuals are employed the individual may be matched for one or more of age, sex, and weight. The individuals may also be matched for ethnicity, alcohol consumption, and/or smoking status. [00387] The present disclosure provides a method of increasing the number of Tregs in one or more subjects (e.g., indivuals or patients), the method comprising administering to the one or more subjects one or more masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected IL-2 MOD polypeptide sequences and/or variant IL-2 MOD polypeptide sequences and optionally comprising one or more independently slected wt. or variant PD-L1 or PD-L2 MOD polypeptide sequences, where the administering results in an increase in the number of Tregs in the one or more subjects. For example, the average number of Tregs (e.g., in blood or a tissue or a location such as a wound) can be increased by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 2-fold, at least 2.5-fold, at least 5-fold, at least 10-fold, or more than 10-fold relative to the number of Tregs in the individual prior to administration of the one or more masked TGF-β constructs or complexes or relative to a control group that did not receive the one or more masked TGF-β constructs or complexes. [00388] The present disclosure provides a method of increasing the number of Tregs in one or more subjects (e.g., indivuals or patients), the method comprising administering to the one or more subjects one or more masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected wt. or variant PD-L1 and/or PD-L2 polypeptide sequences optionally in combination with IL-2 (e.g., recombinanat IL-2 such as Proleukin (aldesleukin)), where the administering results in an increase in the number of Tregs in the one or more subjects. For example, the average number of Tregs (e.g., in blood or a tissue or a location such as a wound) can be increased by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 2-fold, at least 2.5-fold, at least 5-fold, at least 10-fold, or more than 10-fold relative to the number of Tregs in the individual prior to administration of the one or more masked TGF-β constructs or complexes or relative to a control group that did not receive the one or more masked TGF-β constructs or complexes b. T helper cells (i) Th9 cells and masked TGF-β constructs or complexes comprising IL-4 [00389] The present disclosure provides a method of promoting the development and/or survival of thymus-derived Th9 cells (CD4+ cells characterized by expression of CD4 and CCR6 and the lack of CCR4); the method comprising administering (e.g., to a subject in need thereof), or contacting CD4+ T cells (e.g., naïve CD4+ T cells or Th2 cells ) with, one or more masked TGF-β constructs or complexes. The one or more masked TGF-β constructs or complexes administered or contacted in the method may comprise one or more (e.g., one, two or three) independently selected IL-4 MOD polypeptide sequences and/or variant IL-4 MOD polypeptide sequences. Accordingly, the present disclosure provides a method of promoting the development and/or survival of Th9 cells comprising administering (e.g., to a subject in need thereof), or contacting naïve T cells with, one or more masked TGF-β constructs or complexes that comprises one or more IL-4 MOD polypeptide sequences and/or variant IL-4 MOD polypeptide sequences, where the administering results in an increase in the number of Th9 cells in the individual. For example, the number of Th9 cells (e.g., in tissue culture, blood, or in a specific tissue location) can be increased by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 2-fold, at least 2.5-fold, at least 5-fold, at least 10-fold, or more than 10-fold. (ii) Th17 cells and TGF-β constructs or complexes comprising IL-17 [00390] The present disclosure provides a method of stimulating the production of Th17 cells (T cells defined by their production of IL-17), the method comprising administering (e.g., to a subject in need thereof), or contacting CD4+ T cells (e.g., naïve CD4+ T cells) with one or more masked TGF-β constructs or complexes comprising at least one IL-6 or variant IL-6 MOD polypeptide (e.g., one, two or three IL-6 and/or variant IL-6 MOD polypeptides). For example, the number of Th17 cells (e.g., in tissue culture, blood, or in a specific tissue location) can be increased by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 2-fold, at least 2.5-fold, at least 5-fold, at least 10-fold, or more than 10-fold relative to either the number present prior to administration of the one or more masked TGF-β constructs or complexes, or relative to a control group that did not receive the one or more masked TGF- β constructs or complexes. The method may be useful for maintaining the gut mucosal barrier function and may be needed for protection against pathogenic bacteria (e.g., against Citrobacter) and for recruiting neutrophils and monocytes and neutrophils to attack and destroy extracellular fungi (e.g., mucocutaneous Candida). (iii) Tfh cells and masked TGF-β constructs or complexes comprising IL-21 and IL-23 [00391] The present disclosure provides a method of stimulating the production of T follicular helper (Tfh) cells (T cells which are defined by CXCR5 expression), the method comprising administering (e.g., to a subject in need thereof), or contacting macrophages with, one or more masked TGF-β constructs or complexes comprising at least one MOD polypeptide (e.g., one, two or three) independently selected from an IL-21 MOD polypeptide, an IL-23 MOD polypeptide, a variant of an IL- 21 or a variant of an IL-23 MOD polypeptide. For example, the number of Tfh cells (e.g., in tissue culture, blood, or in a specific tissue location such as a lymphoid follicle) can be increased by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 2-fold, at least 2.5-fold, at least 5-fold, at least 10-fold, or more than 10-fold relative to either the number present prior to administration of the one or more masked TGF-β constructs or complexes, or relative to a control group that did not receive the one or more masked TGF-β constructs or complexes. The method may be useful in supporting the development of antigen-specific antibody responses. c. T effector cells and masked TGF-β constructs or complexes comprising IL-7 (i) IL-7 and CD8+ T cells [00392] The present disclosure provides a method of promoting the development (lineage commitment) and/or survival of CD4+ and/or CD8+ T-cell (e.g., by promoting thymocyte expression of the IL-7R (e.g., IL-7Rα); the method comprising administering (e.g., to a subject in need thereof), or contacting precursor CD4+CD8+ T-cells with, one or more masked TGF-β constructs or complexes. The one or more masked TGF-β constructs or complexes administered or contacted in the method may comprise one or more (e.g., one, two or three) independently selected IL-7 MOD polypeptide sequences and/or variant IL-7 MOD polypeptide sequences. Accordingly, the present disclosure provides a method of promoting the development of cells committed to CD4+ or CD8+ lineages (e.g., by promoting thymocyte expression of interleukin (IL)-7Rα), the method comprising administering (e.g., to a subject in need thereof), or contacting CD 4+ and or CD8+ cell precursors (e.g., CD4+8+ T-cells) with one or more masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected IL-7 MOD polypeptide sequences and/or variant IL-7 MOD polypeptide sequences; wherein the development and/or survival of CD4+ and/or CD8+ cells is assessed by monitor peripheral blood or specific tissue (e.g., thymus) CD4+ and/or CD8+ cell numbers. (i) IL-7 and low affinity T-cells [00393] The present disclosure provides a method of regulating peripheral T-cell homeostasis by promoting IL-7-dependent survival of CD4+ T cells and CD8+ T cells with T-cell receptors having low affinity for peptides being presented by MHC proteins. See e.g., Cold Spring Harbor Perspect. Biol. 2017;9:a022236 and citations therein. The method may operate by controlling thymocyte IL-7Rα expression. The method promoting IL-7-dependent survival comprises administering (e.g., to a subject in need thereof) one or more masked TGF-β constructs or complexes. The one or more masked TGF-β constructs or complexes administered may comprise one or more (e.g., one, two or three) independently selected IL-7 MOD polypeptide sequences and/or variant IL-7 MOD polypeptide sequences. Accordingly, the present disclosure provides a method of regulating peripheral T-cell homeostasis; the method comprising administering (e.g., to a subject in need thereof) one or more masked TGF-β constructs or complexes comprising one or more (e.g., one, two or three) independently selected IL-7 MOD polypeptide sequences and/or variant IL-7 MOD polypeptide sequences, wherein administration of the TGF-β construct or complex increases the number of peripheral CD4+ T cells and CD8+ T cells in a subject, or group of subjects, relative to the number of those cells prior to administration. d. Masked TGF-β constructs or complexes and IL-10 [00394] The present disclosure provides a method of inhibiting type 2 innate lymphoid cells (ILC2 cells) (e.g., to suppress asthma and allergic inflammation, see e.g., Rajas et al., J Allergy Clin Immunol, 139(5):1468 (2017); and Ogasawara, et al., J Allergy Clin Immunol, 141(3): 1147–1151 (2018)), using one or more masked TGF-β constructs or complexes comprising at least one (e.g. at least two) independently selecte4d wild type or variant IL-10 MOD polypeptide (e.g., one, two or three independently selected MODs). Variant IL-10 MOD polypeptides may include all or part of a monomeric IL-10 polypeptide (e.g., all or part of SEQ ID NO:50 or 51 substituted with a 5-7 aa insertion in the hinge region between helices D and E mentioned above). See e.g., Josephson et al., J. Biol. Chem. 275:13552-13557 (2000). The method of inhibiting type II innate lymphoid cells comprising administering (e.g., to a subject in need thereof), or contacting type II innate lymphoid cells with, one or more masked TGF-β constructs or complexes optionally comprising one or more (e.g., one, two or more or three or more) independently selected wild type or variant IL-10 MODs. The inhibition of ILC2 cells is assessed by suppression of type 2 cytokine (e.g., IL-3 and/or IL-13) expression by ILC2 cells relative to either the amount if type 2 cytokines prior to administration of the one or more masked TGF-β constructs or complexes, or relative to the amount of type 2 cytokines in a control group (e.g., in cells, tissue, or bodily fluid from a subject) that have not been exposed to TGF-β or the one or more masked TGF-β constructs or complexes. [00395] TGF-β and IL-10 have nonredundant roles in maintaining gastrointestinal homeostasis, with IL- 10 functioning both upstream and downstream of TGF-β. For example, IL-10 can induce TGF-β expression and secretion by lamina propria T cells and it acts cooperatively with TGF-b to promote differentiation of Treg cells. Accordingly, the present disclosure provides methods of maintaining intestinal homeostasis and differentiation of Treg cells in a subject comprising administering one or more masked TGF-β constructs or complexes comprising a wt. or variant IL-10 sequence or both an IL- 2 and IL-10 aa sequence, either or both of which may be an independently selected wt. or a variant sequence. See e.g., Cold Spring Harbor Perspect. Biol.2017;9:a022236 and citations therein. [00396] In some case, such as where it is desirable to induce tolerance, at least one MOD polypeptide (e.g., one, two or three independently selected MODs) present in one or more masked TGF-β constructs or complexes comprising at least one (e.g. at least two) independently selected wild type or variant IL- 10 MOD polypeptides. See e.g., Am J Physiol Gastrointest Liver Physiol 306: G575–G581 (2014), and Levings et al. Int Arch Allergy Immunol.129(4):263-76 (2002). The variant IL-10 MOD polypeptides may include all or part of a monomeric IL-10 polypeptide (e.g., all or part of SEQ ID NO:50 or 51 substituted with a 5-7 aa insertion in the hinge region between helices D and E to form an active monomeric IL-10 as mentioned above. Accordingly, the present disclosure provides methods of inducing tolerance in a subject comprising administering one or more masked TGF-β constructs or complexes comprising a wt. or variant IL-10 sequence or both an IL-2 and IL-10 polypeptide sequence. Alternatively, one or more masked TGF-β constructs or complexes comprising a wt. or variant IL-10 (e.g., monomeric IL-10) sequence may be administered with (concurrently or combined) one or more masked TGF-β constructs or complexes comprising a wt. or variant IL-2 polypeptide sequence. e. Masked TGF-β constructs or complexes and FasL [00397] In some case, such as where it is desirable to induce tolerance or suppress T-effector cells, at least one MOD polypeptide (e.g., one, two or three independently selected MODs) present in one or more masked TGF-β constructs or complexes may comprise a Fas ligand (FasL) polypeptide, or a variant of a Fas ligand polypeptide. (see e.g., Qiu et. al. J Surg Res.218:180-193 (2017). As discussed above, IL-10 or variant IL-10 polypeptides may also be utilized to induce tolerance. [00398] Accordingly, the present disclosure provides methods of inducing tolerance or suppressing T- effector cells in a subject comprising administering one or more masked TGF-β constructs or complexes comprising a wt. or variant FasL polypeptide sequence or both an IL-2 and a FasL polypeptide sequence. The present disclosure also provides for induction of tolerance Alternatively one or more masked TGF β constructs or complexes comprising a wt. or variant FasL sequence may be administered with (concurrently or combined) one or more masked TGF-β constructs or complexes comprising a wt. or variant IL-2 polypeptide sequence. f. Methods of modulating other cells [00399] The present disclosure provides a method of supporting the development and/or survival of invariant natural killer T (iNKT) cells; the method comprising administering (e.g., to a subject in need thereof), or contacting iNKT cell precursor cells with a masked TGF-β construct or complex, optionally comprising one or more (e.g., one, two or more or three or more) independently selected wild type or variant MODs. Where the development and/or survival is assessed relative to treatment groups (e.g., cells or subjects) that have not been exposed to TGF-β or a masked TGF-β construct or complex. [00400] The present disclosure provides a method of inhibiting macrophages (e.g., macrophages activated by a Toll Like Receptor Ligand or cytokine stimulation); the method comprising administering (e.g., to a subject in need thereof), or contacting macrophages with, one or more masked TGF-β constructs or complexes optionally comprising one or more (e.g., one, two or more or three or more) independently selected wildtype or variant MODs; wherein the inhibition is assessed relative to treatment groups (e.g., cells or subjects) that have not been exposed to TGF-β and/or a one or more masked TGF-β constructs or complexes. Activation, and inhibition of macrophage activation is assessed by methods known in the art, such as nitric oxide production by activated macrophages. [00401] TGF-β inhibits H 2 O 2 production by monocytes, and is a chemoattractant for monocytes that inhibits fibronectin adherence. See e.g.,Warwick Davies and Cole, J Immunol.155(6): 3186-3193 (1995). Accordingly, the present disclosure provides a method of stimulating monocytes (e.g., resting monocytes) to undergo migration; the method comprising administering (e.g., to a subject in need thereof), or contacting monocytes with one or more masked TGF-β constructs or complexes optionally comprising one or more (e.g., one, two or more or three or more) independently selected wildtype or variant MODs; wherein the stimulation is assessed relative to treatment groups (e.g., cells or subjects) that have not been exposed to TGF-β and/or one or more masked TGF-β constructs or complexes. Activation, and inhibition of monocytes activation is assessed by methods known in the art, including measurement of H 2 O 2 production and fibronectin adherence. H 2 O 2 production (e.g., in response to a monocyte stimulus) may be decreased by at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, 10-fold, 20-fold, 30-fold, or more). [00402] The present disclosure provides a method of altering peripheral blood monocyte and/or macrophage migration (e.g., assessed by time-lapse microscopy or Boyden chamber assay) into tissues (e.g., injured or inflamed tissue), and/or to enhance macrophage and/or monocyte adherent properties; the method comprising administering (e.g., to a subject in need thereof), or contacting myeloid cells with a masked TGF-β construct or complex, optionally comprising one or more (e.g., one, two or more or three or more) independently selected wildtype or variant MODs; wherein the migration and/or adherent properties are assessed relative to treatment groups (e.g., cells or subjects) that have not been exposed to TGF-β or a masked TGF-β construct or complex. For example, some instances short term interaction of cells or tissue with TGF-β (e.g., TGF-β1) stimulated the migration of macrophages or monocytes, whereas long-term exposure decreased their migration. See, e.g., Kim et al., Blood 108:1821-1829 (2006), and Xu et al Bone Research, 6 (Article No.2) (2018). [00403] The present disclosure provides a method of inducing chemotaxis (e.g., assessed by time-lapse microscopy or Boyden chamber assay) and/or enhancing the adherent properties of mast cells; the method comprising administering (e.g., to a subject in need thereof), or contacting mast cells with, a masked TGF-β construct or complex, optionally comprising one or more (e.g., one, two or more or three or more) independently selected wildtype or variant MODs; wherein the chemotaxis and/or adherent properties are assessed relative to treatment groups (e.g., cells or subjects) that have not been exposed to TGF-β or a masked TGF-β construct or complex. [00404] The present disclosure includes and provides methods of modulating auto reactive and/or inflammatory T cells (e.g., Th1, Th2, Th17 and/or Th22 cells). The methods comprise administering (e.g., to a subject in need thereof), or contacting the T cells (e.g., in vivo or in vitro) with, one or more masked TGF-β constructs or complexes, optionally comprising one or more (e.g., one, two or more or three or more) independently selected wildtype and/or variant MODs. The TGF-β constructs or complexes that optionally comprise one or more wildtype and/or variant MODs may directly interact with such inflammatory T cells, and/or indirectly affect such cells through released molecules (e.g., cytokines/interleukins) or through other cell populations. By way of example, administration of masked TGF-β constructs or complexes optionally comprising one or more wild type and/or variant IL-2 MODs (a TGF-β/IL-2 complex) may directly stimulate the development and/or survival of FoxP3+ T reg cells (in vitro or in vivo). In addition to the direct interactions of a TGF-β/IL-2 complexs with cells resulting in FoxP3 + T reg cells, the resultant T regs may influence other cells such as by, for example, blocking induction of T cell activation and/or the effector phase of T cell responses, suppressing B cell activation, and inhibiting the differentiation and/or proliferation of natural killer cells. Such actions by T regs may be carried out through various means including, but not limited to, production of IL-10, TGF-β, and/or the binding of CTLA-4 on the T reg to B7 (B7-1 or CD80 / B7-2 or CD86) on antigen presenting cells thereby competing with CD28 costimulation of those cells. Accordingly, this disclosure includes and provides for methods of modulating autoreactive T cells and inflammatory T cells belonging to lineages such as Th1, Th2, Th17, Th22 etc. The autoreactive cells may be a population of bystander T cells (e.g., bystander Th1, Th2, and/or Th17 cells). For example, in celiac disease the T cells that are modulated may include Th17 cells found in the intestinal mucosa resulting in reduced expression, secretion, and/or mucosal tissue levels of IL-17A, IL-17F, IL-21, and/or IL-22. [00405] The present disclosure includes and provides a method of inhibiting the action of CD4+ Th1 cells (e.g., reduce their secretion of interferon γ and/or TNF) and thereby activation of macrophages (e.g., phagocytosis and the macrophage involvement in delayed type hypersensitivity or “DTH” that is a component of inflammatory disease including granulomatous inflammation). The method comprising administering (e.g., to a subject in need thereof), or contacting CD4+ Th1 cells with, a one or more masked TGF-β constructs or complexes, optionally comprising one or more (e.g., one, two or more or three or more) independently selected wildtype or variant MODs; wherein the inhibition of Th1 cell action is assessed by the production of interferon γ and/or TNF relative to a treatment group (e.g., cells or subjects) that have not been exposed to TGF-β and/or one or more masked TGF-β constructs or complexes. [00406] The present disclosure includes and provides a method of inhibiting the action (activation) of CD4+ Th2 cells (e.g., reduced IgE, mast cell, and eosinophil mediated reactions); the method comprising administering (e.g., to a subject in need thereof), or contacting CD4+ Th2 cells with, one or more masked TGF-β constructs or complexes, optionally comprising one or more (e.g., one, two or more or three or more) independently selected wildtype or variant MODs; wherein the inhibition of Th2 cell action (the degree of Th2 cell activation) is assessed by the production of IL-4, IL-5, and/or IL-13 relative to a treatment group (e.g., cells or subjects) that have not been exposed to TGF-β and/or one or more masked TGF-β constructs or complexes. 2 Methods of Selectively Delivering a Costimulatory Polypeptide [00407] The present disclosure provides a method of delivering TGF-β in a masked form along with one or more (e.g., one, two or more, three or more, or four or more) independently selected MODs and/or variant MODs using one or more masked TGF-β constructs or complexes. Delivery of MODs to cells comprising TβRs can be complicated due to the interact actions of MODs with their receptors (co- MODs) on cells that contain or do not contain TβRs. Masked TGF-β constructs or complexes may be targeted to cells by varying the number MODs and the affinity for their corresponding co-MODs relative to the effective affinity of the masked TGF-β polypeptide for the TβR. Incorporating variant MODs with reduced affinity into masked TGF-β constructs or complexes allows the TGF-β polypeptide to more strongly influence, or even dominate, the binding interactions. Incorporating a combination of variant MODs with reduced affinity (provided they can still stimulate their co-MODs) and TGF-β polypeptides with relatively strong affinity for the TβR permits the masked TGF-β constructs and complexes comprising one or more MOD(s) to be biased (or even selective) in their binding to cells with both TβRs and the corresponding co-MOD(s). Such a combination also avoids the off-target stimulation of cell bearing the co-MODs without TβR. [00408] The present disclosure provides for the selective delivery of both a TGF-β polypeptide and at least one variant MOD selectively to target cells (e.g., in vitro or in vivo) expressing on their surface membrane a TβR (e.g., TβRII and/or TβRI) and co-MODs corresponding to the at least one variant MOD. When used in this context, “selective delivery” means that the MOD of the masked TGF-β construct or complex is delivered to a co-MOD on a higher number of cells that express a TβR (e.g., TβRII and/or TβRI), i.e., the “target cells”, than to cells that do not comprise a TβR, i.e., “non-target cells” [00409] In view of the foregoing, the present disclosure provides for the delivery of both a TGF-β polypeptide and at least one variant MOD selectively to target cells (e.g., in vitro or in vivo) expressing on their surface membrane a TβR (e.g., TβRII and/or TβRI) and co-MODs corresponding to the at least one variant MOD; the method comprising: contacting a population of cells with an amount of a masked TGF-β construct or complex comprising at least one reduced affinity variant MOD that is insufficient to saturate the TβRs present on the cells (e.g., occupy less than 70%, 60%, 50%, 40% or 30% of the TβRs present on the cells); and permitting the masked TGF-β construct or complex comprising at least one reduced affinity variant MOD to interact with the cells (e.g., for a time sufficient to bind). In such a method the ratio of (i) number of cells expressing both the TβR and a co-MOD bound by the masked TGF-β construct or complex comprising at least one reduced affinity variant MOD divided by the number of cells expressing the co-MOD bound by the masked TGF-β construct or complex comprising at least one reduced affinity variant MOD is greater than (ii) the ratio of number of cells expressing both the TβR and a co-MOD bound by the masked TGF-β construct or complex comprising the wt. MOD divided by the number of cells expressing the co-MOD bound by the masked TGF-β construct or complex comprising the wt. MOD. [00410] The present disclosure provides for the delivery to target cells (e.g., in vitro or in vivo) of both a masked TGF-β polypeptide and at least one wt. and/or variant IL-2 MOD polypeptide, comprising contacting the target cell with a masked TGF-β construct or complex comprising at least one wt. and/or variant IL-2 MOD polypeptide optionally in the presence of vitamin D, retinoic acid (e.g., all trans retinoic acid), and/or rapamycin. In one case masked TGF-β polypeptide comprising at least one wt. or variant IL-2 MOD polypeptide are delivered in the presence of any one, any two, or all three of vitamin D, retinoic acid (e.g., all trans retinoic acid), and/or rapamycin. [00411] The present disclosure provides for the delivery and optionally the selective delivery to target cells (e.g., in vitro or in vivo) of a masked TGF-β construct or complex comprising at least one wild type and/or variant IL-6 MOD polypeptide. [00412] The present disclosure provides for the delivery and optionally the selective delivery to target cells (e.g., in vitro or in vivo) of both a masked TGF-β construct or complex comprising at least one wild type and/or variant IL-7 MOD polypeptide. [00413] The present disclosure provides for the delivery and optionally the selective delivery to target cells (e.g., in vitro or in vivo) of both a masked TGF-β construct or complex comprising at least one wild type and/or variant IL-10 MOD polypeptide. [00414] The present disclosure provides for the delivery and optionally the selective delivery to target cells (e.g., in vitro or in vivo) of both a masked TGF-β construct or complex comprising at least one wild type and/or variant IL-15 MOD polypeptide. [00415] The present disclosure provides for the delivery and optionally the selective delivery to target cells (e.g., in vitro or in vivo) of both a masked TGF-β construct or complex comprising at least one wild type and/or variant IL-21 MOD polypeptide. [00416] The present disclosure provides for the delivery and optionally the selective delivery to target cells (e.g., in vitro or in vivo) of both a masked TGF-β construct or complex comprising at least one wild type and/or variant IL-23 MOD polypeptide. [00417] The present disclosure provides for the delivery and optionally the selective delivery to target cells (e.g., in vitro or in vivo) of both a masked TGF-β construct or complex comprising at least one wild type and/ variant PD-L1 MOD polypeptide. [00418] The present disclosure provides for the delivery and optionally the selective delivery to target cells (e.g., in vitro or in vivo) of both a masked TGF-β construct or complex comprising at least one wild type and/or variant FasL MOD polypeptide. 3 Methods of treatment or prophylaxis [00419] The present disclosure provides treatment and prophylaxis methods, the methods may comprise contacting a target population of cells from an individual (e.g., in vitro or in vivo) and/or administering to the individual, an effective amount of a masked TGF-β construct or complex (e.g., PSM-4033-4039), or one or more nucleic acids or expression vectors encoding the masked TGF-β construct or complex, effective to selectively modulate the activity of the target cell population of cells and/or to treat the individual. Where target cells are treated separately from the individual (i.e., in vitro), all or a portion of the cells or their progeny may be administered to individual. In some cases, a method of treatment or prophylaxis comprises administering to an individual in need thereof an effective amount of one or more recombinant expression vectors comprising nucleotide sequences encoding a masked TGF-β construct or complex. In some cases, a method of treatment or prophylaxis comprises administering to an individual in need thereof one or more mRNA molecules comprising nucleotide sequences encoding a masked TGF-β construct or complex. In some cases, a method of treatment or prophylaxis comprises contacting a target population of cells from an individual (i.e., in vitro) in need thereof with an effective amount of a masked TGF-β construct or complex (e.g., PSM-4033-4039) and thereby forming a contacted target population of cells, the method further comprising administering all or part of the contacted target population of cells (and/or their progeny) to the individual. In some cases, a method of treatment or prophylaxis comprises administering to an individual in need thereof an effective amount of a masked TGF-β construct or complex (e.g., PSM-4033-4039), or a pharmaceutically acceptible composition comprising an effective amount of a masked TGF-β construct or complex (e.g., PSM-4033- 4039). Conditions that can be treated (e.g., to cure and/or ameliorate symptoms) with a composition comprising an effective amount of a masked TGF-β construct or complex (e.g., PSM-4033-4039) include: conditions associated with an insufficient number of Treg cells or insufficiently active Treg cells, autoimmune diseases or disorders, allergic reaction(s), wounds (e.g., dermal and/or mucosal wounds), and/or burns. In addition, individuals undergoing organ transplantation may also benefit from treatment. [00420] A method of treatment or prophylaxis comprising administering to an individual with an insufficient number of FoxP3+ Treg cells or insufficiently active FoxP3+ Treg cells an effective amount of a masked TGF-β construct or complex (e.g., PSM-4033-4039) and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. In one instance, the masked TGF-β construct or complex comprises PSM-4033-4039. In one instance, the masked TGF-β construct or complex comprises one or more (e.g., one, two or three) independently selected IL-2 or variant IL-2 MOD polypeptide sequences. The masked TGF-β construct or complex and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex, with or without an IL-2 or variant IL-2 MOD, may be administered before, during (concurrent or combined administration) or after administration of any one or more of vitamin D (e.g., 1α,25- dihydroxyvitamin D3 or 1α,25-Dihydroxycholecalciferol) or a vitamin D analog, rapamycin, and/or a retinoic acid (e.g., all trans retinoic acid). [00421] A method of treatment or prophylaxis may comprise administering to an individual with an autoimmune disease or disorder which is in need thereof an effective amount of a masked TGF-β construct or complex and/or one or more nucleic acids (e.g., recombinant expression vectors) comprising nucleotide sequences encoding a masked TGF-β construct or complex. In one instance, the masked TGF-β construct or complex comprise one or more (e.g., one, two or three) independently selected IL-2 or variant IL-2 MOD polypeptide sequences (e.g., PSM-4033-4039). In a second instance, the masked TGF-β construct or complex comprise one or more (e.g., one, two or three) independently selected IL-10 or variant IL-10 MOD polypeptide sequences. In one instance, the masked TGF-β construct or complex comprises at least one independently selected IL-2 or variant IL-2 MOD polypeptide sequence and at least one independently selected IL-10 or variant IL-10 MOD polypeptide sequence. In a second instance, the masked TGF-β construct or complex comprise one or more (e.g., one, two or three) independently selected IL-10 or variant IL-10 MOD polypeptide sequences. Autoimmune diseases that can be treated with a method of the present disclosure include, but are not limited to, Addison's disease, alopecia areata, ankylosing spondylitis, autoimmune encephalomyelitis, autoimmune hemolytic anemia, autoimmune hepatitis, autoimmune-associated infertility, autoimmune thrombocytopenic purpura, bullous pemphigoid, Crohn's disease, Goodpasture's syndrome, glomerulonephritis (e.g., crescentic glomerulonephritis, proliferative glomerulonephritis), Grave's disease, Hashimoto's thyroiditis, mixed connective tissue disease, multiple sclerosis, myasthenia gravis (MG), pemphigus (e.g., pemphigus vulgaris), pernicious anemia, polymyositis, psoriasis, psoriatic arthritis, rheumatoid arthritis, scleroderma, Sjögren's syndrome, systemic lupus erythematosus (SLE), vasculitis, and vitiligo. In an embodiment, the autoimmune disease that can be treated with a method of the present disclosure is T1D. In an embodiment, the autoimmune disease that can be treated with a method of the present disclosure is celiac disease. T1D and/or celiac disease also may be excluded from the autoimmune diseases subject to treatment with a method of the present disclosure. [00422] A method of treatment or prophylaxis comprising administering to an individual with a deficiency in Th17 cells (e.g., individuals unable to sufficiently respond to bacterial and/or fungal infections in the gut) an effective amount of a masked TGF-β construct or complex and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. In one instance, the masked TGF-β construct or complex comprises one or more (e.g., one, two or three) independently selected IL-6 or variant IL-6 MOD polypeptide sequences. A method of treatment or prophylaxis may comprise administering to an individual unable to sufficiently respond to bacterial and/or fungal infections in the gut an effective amount of a masked TGF-β construct or complex comprising one or more independently selected IL-6 and/or variant IL-6 polypeptides, or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex comprising one or more independently selected IL-6 and/or variant IL-6 polypeptides. [00423] A method of treatment or prophylaxis comprising administering to an individual with a deficiency in Th9 cells (e.g., individuals unable to sufficiently respond to helminth infections) an effective amount of a masked TGF-β construct or complex and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex sufficient to respond to helminth infection. In one instance, the masked TGF-β construct or complex comprise one or more (e.g., one, two or three) independently selected IL-4 or variant IL-4 MOD polypeptide sequences. A method of treatment or prophylaxis may comprise administering to an individual unable to sufficiently respond to sufficiently respond to helminth infections an effective amount of a masked TGF-β construct or complex comprising one or more independently selected IL-4 and/or variant IL-4 polypeptides, or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex comprising one or more independently selected IL-4 and/or variant IL-4 polypeptides. [00424] A method of treatment or prophylaxis comprising administering to an individual with a deficiency in Tfh cells (e.g., individuals unable to produce high affinity antibodies or sufficient amounts of high affinity antibodies) an effective amount of a masked TGF-β construct or complex and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex sufficient to increase the production of high affinity antibodies. In one instance, the masked TGF-β construct or complex comprises one or more (e.g., one, two or three) independently selected IL- 21, IL-23, variant IL-21 or variant IL-23 MOD polypeptide sequences. A method of treatment or prophylaxis may comprise administering to an individual unable to produce high affinity antibodies or insufficient amounts of high affinity antibodies an effective amount of a masked TGF-β construct or complex comprising one or more independently selected IL-21, IL-23, variant IL-21 or variant IL-23 MOD polypeptide sequences, or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex comprising one or more independently selected IL- 21, IL-23, variant IL-21 or variant IL-23 MOD polypeptide sequences. [00425] A method of treatment or prophylaxis comprising administering to an individual having excess Th1 cell activity relative to a control group (e.g., and individual with elevated levels of activated macrophages and/or elevated levels of interferon gamma “IFN-γ” in a target tissue or circulating ) an effective amount of a masked TGF-β construct or complex and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. A method of treatment or prophylaxis may comprise administering to an individual with elevated levels of activated macrophages and/or elevated levels of interferon gamma “IFN-γ” (e.g., circulating or in a target tissue) an effective amount of a masked TGF-β construct or complex, or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. [00426] A method of treatment or prophylaxis comprising administering to an individual having excess Th2 cell activity relative to a control group (e.g., an individual with elevated levels of activated MAST cells and/or with elevated levels of IgE that circulating or tissue localize) an effective amount of a masked TGF-β construct or complex and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. A method of treatment or prophylaxis may comprise administering to an individual with elevated levels of activated MAST cells and/or with elevated levels of IgE (circulating or tissue localize) an effective amount of a masked TGF-β construct or complex, or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. [00427] A method of treatment or prophylaxis comprising administering to an individual having T-cell receptor-driven activation of autoreactive T cells (or high affinity T-cells) an effective amount of a masked TGF-β construct or complex (e.g., PSM-4033-4039) and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. A method of treatment or prophylaxis may comprise administering to an individual with autoreactive T-cells an effective amount of a masked TGF-β construct or complex (e.g., PSM-4033-4039), or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. [00428] A method of treatment or prophylaxis comprising administering to an individual in which it is desirable to promote IL-7-dependent survival of low-affinity CD4+ and /or CD8+ T cells (e.g., by control of thymocyte IL-7Ra expression) an effective amount of a masked TGF-β construct or complex and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. In one instance, the masked TGF-β construct or complex comprise one or more (e.g., one, two or three) independently selected IL-7 or variant IL-7 MOD polypeptide sequences. A method of treatment or prophylaxis may comprise administering to an individual unable to sufficiently maintain levels of low-affinity CD4+ and /or CD8+ T cells an effective amount of a masked TGF-β construct or complex comprising one or more independently selected IL-7 and/or variant IL-7 polypeptides, or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex comprising one or more independently selected IL-7 and/or variant IL-7 polypeptides. [00429] A method of treatment or prophylaxis comprising administering to an individual in which it is desirable to promote apoptosis of specific cells (e.g., cancer cells or cancer cells bearing a specific marker such as cancer antigens 15-3, 27-29, 125, carcinoembryonic antigen, Alpha-fetoprotein and/or Beta 2-microglobulin) an effective amount of a masked TGF-β construct or complex and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex (e.g., PSM-4033-4039). In one instance, the masked TGF-β construct or complex comprise one or more (e.g., one, two or three) independently selected wt. Fas ligand or variant Fas ligand MOD polypeptide sequences. [00430] A method of treatment or prophylaxis comprising administering to an individual in which it is desirable to induce iTreg (CD4+ FoxP3+) cells (e.g., individuals in which it is desirable to induce peripheral tolerance to actively suppress effector T (T eff) cells and/or inhibit immune-mediated tissue damage) an effective amount of a masked TGF-β construct or complex (e.g., PSM-4033-4039) and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. In one instance, the masked TGF-β construct or complex comprise one or more (e.g., one, two or three) independently selected wt. or variant PD-L1 MOD polypeptide sequences. In another instance, the masked TGF-β construct or complex comprise one or more (e.g., one, two or three) independently selected wt. and/or variant PD-L1 MOD polypeptide sequences and one or more wt. and/or variant IL-2 MOD polypeptide sequences. In an embodiment the masked TGF-β construct or complex comprise (i) one independently selected wt. or variant PD-L1 MOD polypeptide sequence and (ii) one wt. or variant IL-2 MOD sequence. See, e.g., Francisco et al., J. Exp. Med., 206(13): 3015-3029 (2009). [00431] A method of treatment or prophylaxis comprising administering to an individual in which it is desirable to inhibit type II innate lymphoid cells (ILC2 cells) (e.g., to suppress asthma, allergic reaction, and/or allergic inflammation) an effective amount of a masked TGF-β construct or complex (e.g., PSM- 4033-4039) and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. In one instance, the masked TGF-β construct or complex comprise one or more (e.g., one, two or three) independently selected IL-10 or variant IL-10 MOD polypeptide sequences. The masked TGF-β construct or complex and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex, with or without an IL-10 or variant IL-10 MOD, may be administered before, during (concurrent or combined administration) or after administration of a glucocorticoid (e.g., dexamethasone, prednisone, etc.), antihistamine (e.g., diphenhydramine, chlorpheniramine, etc.), and/or epinephrine. [00432] A method of treatment or prophylaxis comprising administering to an individual having an allergy, allergic inflammation, and/or elevated levels of IgE (circulating or tissue localized) an effective amount of a masked TGF-β construct or complex comprising at least one (e.g., one, two or three) independently selected IL-10 or variant IL-10 MOD polypeptides and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. A method of treatment or prophylaxis may comprise administering to an individual with elevated levels of IgE (circulating or tissue localize) an effective amount a masked TGF-β construct or complex comprising at least one (e.g., one, two or three) independently selected IL-10 or variant IL-10 MOD polypeptides and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. The masked TGF-β construct or complex and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex, with or without an IL-10 or variant IL-10 MOD, may be administered before, during (concurrent or combined administration) or after administration of a glucocorticoid (e.g., dexamethasone, prednisone, etc.), antihistamine (e.g., diphenhydramine, chlorpheniramine, etc.), and/or epinephrine. The TGF-β and IL-10 act to suppress expression of the high-affinity IgE receptor (Fc1RI) that activates MAST cells and IL-10 additionally acts to prevent excessive MAST cell activation and the development of chronic inflammation. See e.g., Kennedy et al. Journal of Immunology, 180(5) 2848-2854 (2008). [00433] A method of or prophylaxis comprising administering to an individual diagnosed with or having multiple sclerosis, an effective amount of a masked TGF-β construct or complex (e.g., PSM-4033-4039) and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. In one instance, the masked TGF-β construct or complex comprise one or more (e.g., one, two or three) independently selected IL-10 or variant IL-10 MOD polypeptide sequences. [00434] A method of treatment an individual having at least one cutaneous or mucosal burn, the method comprising administering the individual an effective amount of a masked TGF-β construct or complex (e.g., PSM-4033-4039) and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. In an instance the method may comprise administering an effective amount of a masked TGF-β construct or complex comprising at least one (e.g., one, two or three) independently selected IL-10 or variant IL-10 MOD polypeptides and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. The burns may be first, second, or third-degree burns. [00435] A method of treatment an individual having at least one cutaneous or mucosal wound (an abrasion, avulsion, incision, laceration, or puncture of the epidermis or mucosa), the method comprising administering the individual an effective amount of a masked TGF-β construct or complex (e.g., PSM- 4033-4039) and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex to speed wound closure (reduce time until closure), reduce healing time, or to reduce scar formation relative to an untreated wound. In an instance, the method may comprise administering an effective amount of a masked TGF-β construct or complex comprising at least one (e.g., one, two or three) independently selected IL-10 or variant IL-10 MOD polypeptides and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. When the masked TGF-β construct or complex, either with or without an IL-10 MOD polypeptide, comprises TGF-β1 polypeptide, the method may further comprise one or more of: the recruitment of inflammatory cells into the injury site; expression of extracellular matrix proteins such as fibronectin, collagen (e.g., types I and/or III), and/or VEGF; stimulation fibroblasts contraction to enable wound closure; wound site expression of integrins, such as β1, α5, αv, and β5; and keratinocyte migration. When the masked TGF-β construct or complex, either with or without an IL-10 MOD polypeptide, comprises TGF-β2 polypeptide, the method may further comprise one or more of: the recruitment of both fibroblasts and immune cells from circulation and the wound edges into the wounded area; expression of collagen (e.g., types I and/or III); and expression of fibronectin. See, e.g., Pakyari et al Adv Wound Care, 2(5): 215–224 (2013). In such methods the masked TGF-β construct or complex may be applied directly to or injected into the wound. [00436] A method of treatment an individual having at least one cutaneous or mucosal wound (an abrasion, avulsion, incision, laceration, or puncture of the epidermis or mucosa), the method comprising administering to the individual an effective amount of a masked TGF-β (e.g., TGF-β3) construct or complex (e.g., PSM-4033-4039) and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β3 construct or complex to reduce scar formation relative to an untreated wound. In an instance, the method may comprise administering an effective amount of a masked TGF-β (e.g., TGF-β3) construct or complex comprising at least one (e.g., one, two or three) independently selected IL-10 or variant IL-10 MOD polypeptides and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β (e.g., TGF-β3) construct or complex. In such methods the masked TGF-β (e.g., TGF-β3) construct or complex may be applied directly to or injected into the wound. Without being bound by theory, it may be understood that TGF-β3 reduces type 1collagen deposition while promoting collagen degradation by MMP-9, leading to decreased scar formation. See. e.g., Pakyari et al Adv Wound Care, 2(5): 215–224 (2013). [00437] A method of facilitating organ transplant in an individual, the method comprising administering the individual an effective amount of a masked TGF-β construct or complex (e.g., PSM-4033-4039) and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex to speed incision closure (reduce time until closure), reduce recovery time, or to reduce scar formation relative to the average time to closure, recovery time or scar formation in untreated individuals matched for the type of organ transplantation, age, sex, smoking habits, and/or body mass index. In an instance, the method may comprise administering an effective amount of a masked TGF-β construct or complex comprising at least one (e.g., one, two or three) independently selected IL-10 or variant IL-10 MOD polypeptides and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex. [00438] A method of treating an individual with graft vs. host disease (GVHD, including acute GVHD), the method comprising administering the individual an effective amount of a masked TGF-β construct or complex (e.g., PSM-4033-4039) and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex [00439] In any of the foregoing methods, unless specified otherwise, the TGF-β polypeptide of a masked TGF-β construct or complex can be a TGF-β1, TGF-β2, or TGF-β3 polypeptide or a variant thereof as discussed in the preceding section (e.g., a TGF-β3 C77S variant or a TGF-β1 or TGF-β2 variant with a corresponding mutation limiting TGF-β polypeptide dimerization). Similarly, the polypeptide masking the TGF-β polypeptide can be selected from those described above (e.g., antibodies or fragments thereof, single chain antibodies, or TβRI or TβRII ectodomain fragments that bind to TGF-β). [00440] As noted above, in some cases, in carrying out a subject method of treatment or prophylaxis, a masked TGF-β construct or complex is administered to an individual in need thereof, as the polypeptide per se. In other instances, in carrying out a subject method of treatment or prophylaxis, one or more nucleic acids comprising nucleotide sequences encoding a masked TGF-β construct or complex is/are administering to an individual in need thereof. Thus, in other instances, one or more nucleic acids, e.g., one or more recombinant expression vectors, is/are administered to an individual in need thereof. N. Dosages [00441] A suitable dosage can be determined by an attending physician or other qualified medical personnel, based on various clinical factors. As is well known in the medical arts, dosages for any one patient depend upon many factors, including the patient's size, body surface area, age, the particular polypeptide or nucleic acid to be administered, sex of the patient, time, and route of administration, general health, and other drugs being administered concurrently. A masked TGF-β construct or complex may be administered in amounts between 1 ng/kg body weight and 20 mg/kg body weight per dose, e.g. between 0.1 mg/kg body weight to 10 mg/kg body weight, e.g. between 0.5 mg/kg body weight to 5 mg/kg body weight; however, doses below or above this exemplary range are envisioned, especially considering the aforementioned factors. If the regimen is a continuous infusion, it can also be in the range of 1 μg to 10 mg per kilogram of body weight per minute. A masked TGF-β construct or complex can be administered in an amount of from about 1 mg/kg body weight to 50 mg/kg body weight, e.g., from about 1 mg/kg body weight to about 5 mg/kg body weight, from about 5 mg/kg body weight to about 10 mg/kg body weight, from about 10 mg/kg body weight to about 15 mg/kg body weight, from about 15 mg/kg body weight to about 20 mg/kg body weight, from about 20 mg/kg body weight to about 25 mg/kg body weight, from about 25 mg/kg body weight to about 30 mg/kg body weight, from about 30 mg/kg body weight to about 35 mg/kg body weight, from about 35 mg/kg body weight to about 40 mg/kg body weight, or from about 40 mg/kg body weight to about 50 mg/kg body weight. [00442] In some cases, a suitable dose of a masked TGF-β construct or complex is from 0.01 μg to 100 g per kg of body weight, from 0.1 μg to 10 g per kg of body weight, from 1 μg to 1 g per kg of body weight, from 10 μg to 100 mg per kg of body weight, from 100 μg to 10 mg per kg of body weight, or from 100 μg to 1 mg per kg of body weight. Persons of ordinary skill in the art can easily estimate repetition rates for dosing based on measured residence times and concentrations of the administered agent in bodily fluids or tissues. Following successful treatment, it may be desirable to have the patient undergo maintenance therapy to prevent the recurrence of the disease state, wherein a masked TGF-β construct or complex or a single-chain masked TGF-β construct or complex) is administered in maintenance doses, ranging from 0.01 μg to 100 g per kg of body weight, from 0.1 μg to 10 g per kg of body weight, from 1 μg to 1 g per kg of body weight, from 10 μg to 100 mg per kg of body weight, from 100 μg to 10 mg per kg of body weight, or from 100 μg to 1 mg per kg of body weight. [00443] Those of skill will readily appreciate that dose levels can vary as a function of the specific masked TGF β construct or complex the severity of the symptoms and the susceptibility of the subject to side effects. Preferred dosages for a given compound are readily determinable by those of skill in the art by a variety of means. [00444] In some cases, multiple doses of a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector are administered. The frequency of administration of a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector can vary depending on any of a variety of factors, e.g., severity of the symptoms, etc. For example, in some cases, a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vectors administered once per month, twice per month, three times per month, every other week (qow), once per week (qw), twice per week (biw), three times per week (tiw), four times per week, five times per week, six times per week, every other day (qod), daily (qd), twice a day (qid), or three times a day (tid). [00445] The duration of administration of a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector, e.g., the period of time over which a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector is administered, can vary, depending on any of a variety of factors, e.g., patient response, etc. For example, a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector can be administered over a period of time ranging from about one day to about one week, from about two weeks to about four weeks, from about one month to about two months, from about two months to about four months, from about four months to about six months, from about six months to about eight months, from about eight months to about 1 year, from about 1 year to about 2 years, or from about 2 years to about 4 years, or more. O. Routes of administration [00446] An active agent (a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector) is administered to an individual using any available method and route suitable for drug delivery, including in vivo and in vitro methods, as well as systemic and localized routes of administration. [00447] Conventional and pharmaceutically acceptable routes of administration include intratumoral, peritumoral, intramuscular, intratracheal, intralymphatic, intracranial, cutaneous, subcutaneous, intradermal, topical application, intravenous, intraarterial, rectal, nasal, oral, and other enteral and parenteral routes of administration. Routes of administration may be combined, if desired, or adjusted depending upon the masked TGF-β construct or complex and/or the desired effect. A masked TGF-β construct or complex, or a nucleic acid or recombinant expression vector, can be administered in a single dose or in multiple doses. [00448] In some cases, a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector is administered intravenously. In some cases, a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector is administered intramuscularly. In some cases, a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector is administered intralymphatically. In some cases, a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector is administered locally In some cases a masked TGF β construct or complex, a nucleic acid, or a recombinant expression vector is administered intratumorally. In some cases, a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector is administered peritumorally. In some cases, a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector is administered intracranially. In some cases, a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector is administered cutaneously. In some cases, a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector is administered subcutaneously. In some cases, a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector is administered to a wound (e.g., a dermal or mucosal wound). In some cases, a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector is administered to burned tissue (e.g., a dermal burns). [00449] In some cases, a masked TGF-β construct or complex is administered intravenously. In some cases, a masked TGF-β construct or complex is administered intramuscularly. In some cases, a masked TGF-β construct or complex is administered locally. In some cases, a masked TGF-β construct or complex is administered intratumorally. In some cases, a masked TGF-β construct or complex is administered peritumorally. In some cases, a masked TGF-β construct or complex is administered intracranially. In some cases, a masked TGF-β construct or complex is administered cutaneously. In some cases, a masked TGF-β construct or complex is administered subcutaneously. In some cases, a masked TGF-β construct or complex is administered intralymphatically. In some cases, a masked TGF-β construct or complex is administered to a wound (e.g., a dermal or mucosal wound). In some cases, a masked TGF-β construct or complex is administered to burned tissue (e.g., a dermal burns). [00450] A masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector can be administered to a host using any available conventional methods and routes suitable for delivery of conventional drugs, including systemic or localized routes. In general, routes of administration contemplated for use in a method include, but are not necessarily limited to, enteral, parenteral, cutaneous, and inhalational routes. [00451] Parenteral routes of administration other than inhalation administration include, but are not necessarily limited to, topical, transdermal, subcutaneous, intramuscular, intraorbital, intracapsular, intraspinal, intrasternal, intratumoral, intralymphatic, peritumoral, and intravenous routes, i.e., any route of administration other than through the alimentary canal. Parenteral administration can be carried to effect systemic or local delivery of a masked TGF-β construct or complex, a nucleic acid, or a recombinant expression vector. Where systemic delivery is desired, administration typically involves invasive or systemically absorbed topical or mucosal administration of pharmaceutical preparations. P. Subjects suitable for treatment [00452] Subjects suitable for treatment with a masked TGF-β construct or complex e.g., PSM-4033- 4039), such as by a method described herein, include individuals (e.g., humans) with an autoimmune disease, allergic reaction(s), wounds (e.g., dermal and/or mucosal wounds), and/or burns. Subjects additionally include individuals undergoing organ transplantation In addition to humans subjects include non-human mammals including, but not limited to, bovine canine, caprine, cercopithecine, feline, lapine, lapine, murine, ovine, porcine, or simian subjects or patients in need of treatment. [00453] Subjects ( individuals) who have an autoimmune disease or conditions and are suitable for treatment with a masked TGF-β construct or complex (e.g., PSM-4033-4039), including individuals those who have been diagnosed as having an autoimmune disease or condition, and individuals who have been treated for an autoimmune disease or condition but who failed to respond to the treatment. Autoimmune diseases and conditions that can be treated with a method of the present disclosure include, but are not limited to, Addison's disease, alopecia areata, ankylosing spondylitis, autoimmune encephalomyelitis, , autoimmune colitis, autoimmune gastritis, autoimmune hemolytic anemia, autoimmune hepatitis, autoimmune-associated infertility, autoimmune pancreatitis, autoimmune retinopathy, autoimmune thrombocytopenic purpura, autoimmune urticaria, bullous pemphigoid, celiac disease, Crohn's disease, Goodpasture's syndrome, glomerulonephritis (e.g., crescentic glomerulonephritis, proliferative glomerulonephritis), graft vs. host disease (GVHD, including acute GVHD), Grave's disease, Hashimoto's thyroiditis, inflammatory bowel disease, mixed connective tissue disease, multiple sclerosis, myasthenia gravis (MG), pemphigus (e.g., pemphigus vulgaris), pernicious anemia, polymyositis, psoriasis, psoriatic arthritis, rheumatoid arthritis, scleroderma, Sjögren's syndrome, systemic lupus erythematosus (SLE), transplant rejection, type-1 diabetes (T1D) vasculitis, and vitiligo. In an embodiment, the autoimmune disease is T1D. In an embodiment, the autoimmune disease is celiac disease. Individuals with T1D and/or celiac disease may be excluded from the subjects suitable for treatment. Similarly, T1D and/or celiac disease may be excluded from the autoimmune disease subject to treatment. [00454] In an embodiment, the autoimmune diseases and conditions that can be treated with a method of the present disclosure include, but are not limited to, rheumatoid arthritis (RA), psoriasis/psoriatic arthritis, multiple sclerosis, inflammatory bowel disease, Addison’s disease, Graves’ disease, Sjögren’s syndrome, Hashimoto’s thyroiditis, myasthenia gravis, autoimmune vasculitis, and pernicious anemia. [00455] Subjects that have allergic reactions cannot easily categorized by the allergens because allergens are too numerous to recite. By way of example, however, subjects (e.g., individuals previously treated for their allergies or who have never been treated) who have an allergic reaction(s) include those with reactions to: peanuts and tree nuts, plant pollens, latex, and the like. For example, subjects with allergic reactions to peanut allergens include those with reactions to Ara h 1 to 13 proteins that come from seven protein families, include those in Ara h 1 (e.g., PGQFEDFF (SEQ ID NO:161), YLQGFSRN (SEQ ID NO:162), FNAEFNEIRR (SEQ ID NO:163), QEERGQRR (SEQ ID NO:164), DITNPINLRE (SEQ ID NO:165), NNFGKLFEVK (SEQ ID NO:166), GNLELV (SEQ ID NO:167), RRYTARLKEG (SEQ ID NO:168), ELHLLGFGIN (SEQ ID NO:169), HRIFLAGDKD (SEQ ID NO:170), IDQIEKQAKD (SEQ ID NO:171), KDLAFPGSGE (SEQ ID NO:172), KESHFVSARP (SEQ ID NO:173), NEGVIVKVSKEHVEELTKHAKSVSK (SEQ ID NO:174), Ara h 2 (e.g., HASARQQWEL (SEQ ID NO:175), QWELQGDRRC (SEQ ID NO:176), DRRCQSQLER (SEQ ID NO:177), LRPCEQHLMQ (SEQ ID NO:178), KIQRDEDSYE (SEQ ID NO:179), YERDPYSPSQ (SEQ ID NO:180), SQDPYSPSPY (SEQ ID NO:181), DRLQGRQQEQ (SEQ ID NO:182), KRELRNLPQQ (SEQ ID NO:183), QRCDLDVESG (SEQ ID NO:184), and Ara h 3 (e.g., IETWNPNNQEFECAG (SEQ ID NO:185), GNIFSGFTPEFLAQA (SEQ ID NO:186), VTVRGGLRILSPDRK (SEQ ID NO:187), DEDEYEYDEEDRRRG (SEQ ID NO:188). See, e.g., Zhou et al, (2013) Intl. J. of Food Sci.2013: 8 pages article ID 909140. Subjects with allergic reactions also include those with reactions to hymenoptera proteins (e.g., allergens in bee and wasp venoms such as phospholipase A2, melittin, “antigen 5” found in wasp venom, and hyaluronidases). [00456] Subjects that have wounds include individuals with abrasion, avulsion, incision, laceration, and puncture of skin or mucosa. It may be understood that subjects that have organ transplantation, will, by their nature have one or more of those wound types. V. CERTAIN ASPECTS [00457] Certain aspects including aspects of the subject matter directed to the TGF-β constructs or complexes described above, may be beneficial alone or in combination, with one or more other aspects, such as those recited below directed to TGF-β constructs and complexes, their method of manufacture, and their methods of use (e.g., as therapeutics). 1. A construct comprising as a first polypeptide: i) a scaffold polypeptide sequence; ii) a TGF-β polypeptide sequence; iii) a masking polypeptide sequence (e.g., a TGF-β receptor polypeptide sequence or anti-TGF-β polypeptide sequence); iv) optionally, one or more (e.g., one, two or more) independently selected MOD polypeptide sequences; and v) optionally one or more independently selected linker polypeptide sequences (e.g., between any of the foregoing polypeptide sequences); a construct comprising these elements being collectively referred to as a “masked TGF-β construct,” wherein the masking polypeptide sequence (e.g., TGF-β receptor polypeptide sequence or anti-TGF-β polypeptide sequence) and the TGF-β polypeptide sequence bind to each other (interact with each other to mask the TGF-β polypeptide sequence). See e.g., FIG 1, structure A. 2. The masked TGF-β construct of aspect 1, wherein the first polypeptide comprises, in order from N- terminus to C-terminus: i) the scaffold polypeptide sequence, the masking polypeptide sequence (e.g., TGF-β receptor polypeptide sequence), and the TGF-β polypeptide sequence; or ii) a first MOD polypeptide sequence, the scaffold polypeptide sequence, the masking polypeptide sequence (e.g., TGF-β receptor polypeptide sequence), and the TGF-β polypeptide sequence; or iii) a first independently selected MOD polypeptide sequence, a second independently selected MOD polypeptide sequence (MODs in tandem), the scaffold polypeptide sequence, the masking polypeptide sequence (e.g., TGF-β receptor polypeptide sequence), and the TGF-β polypeptide sequence; wherein masked TGF-β construct optionally comprise one or more independently selected linker polypeptide sequences (e.g. between any of the foregoing polypeptide sequences). 3. The masked TGF-β construct of aspect 1 or aspect 2, wherein the scaffold polypeptide comprises a dimerization (or multimeriation) sequence. 4. The masked TGF-β construct of aspect 3, in the form of a masked TGF-β complex homodimer wherein the scaffold polypeptide sequences optionally have one or more (e.g., one, two or more) covalent attachments (e.g., disulfide bonds) to each other (e.g., wherein a first molecule of the masked TGF-β construct as the first polypeptide is dimerized with a second molecule of the masked TGF-β construct as a second polypeptide through covalent or non-covalent interactions of their scaffold polypeptide sequences to form a homodimer), optionally wherein , the scaffolds comprise Ig Fc polypeptides that include mutations (e.g., the LALA mutations) that substantially reduce or eliminate the ability of the Ig polypeptide to induce cell lysis, e.g., though complement-dependent cytotoxicity (CDC) and/or antibody-dependent cellular cytotoxicity (ADCC). See e.g., FIG 1, structure B. 5. The masked TGF-β construct of any of aspects 1-3, wherein the scaffold polypeptide comprises an interspecific dimerization sequence (e.g., a dimerization sequence that preferentially dimerizes with its counterpart interspecific binding sequence as opposed to homodimerizing). See e.g., FIG 1, structures C and F. 6. The masked TGF-β construct of aspect 5, further comprising a second polypeptide dimerized with the first polypeptide to form a masked TGF-β complex heterodimer; wherein the second polypeptide comprises a scaffold polypeptide sequence that comprises a counterpart interspecific dimerization sequence to the interspecific binding sequence of the first polypeptide; and wherein the interspecific binding sequence and the counterpart interspecific binding sequence interact with each other in the heterodimer. 7. The masked TGF-β complex of aspect 6, wherein the second polypeptide comprises: (i) a scaffold polypeptide sequence comprising the counterpart interspecific dimerization sequence; (ii) one or two (or more) independently selected MOD sequences (e.g., in tandem) and a scaffold polypeptide sequence comprising the counterpart interspecific dimerization sequence; (iii) a scaffold polypeptide sequence comprising the counterpart interspecific dimerization sequence, and an independently selected MOD sequence; or (iv) one or two (or more) independently selected MOD sequences (e.g., in tandem) and a scaffold polypeptide sequence comprising the counterpart interspecific dimerization sequence; wherein the first and or second polypeptides optionally comprise one or more independently selected linker polypeptide sequences (e.g. between any of the foregoing polypeptide sequences). See e.g., FIG 1, structure F. 8. The masked TGF-β complex of aspect 6 or 7, wherein the second polypeptide comprises, from N- terminus to C-terminus: i) a scaffold polypeptide sequence comprising the counterpart interspecific dimerization sequence; (ii) one or two (or more) independently selected MOD sequences (e.g., in tandem) and a scaffold polypeptide sequence comprising the counterpart interspecific dimerization sequence; (iii) a scaffold polypeptide sequence comprising the counterpart interspecific dimerization sequence, and one or two (or more) independently selected MOD sequences; or (iv) one or two (or more) independently selected MOD sequences (e.g., in tandem) and a scaffold polypeptide sequence comprising the counterpart interspecific dimerization sequence wherein first and/or second polypeptides optionally comprises one or more independently selected linker polypeptide sequences (e.g., between any of the foregoing polypeptide sequences). See e.g., FIG 1, structure F. 9. The masked TGF-β complex of aspect 6, wherein the second polypeptide comprises: i) optionally, one or more (e.g., one, two or more) independently selected MOD polypeptide sequences; ii) a scaffold polypeptide sequence comprising the counterpart interspecific dimerization sequence; iii) a TGF-β polypeptide sequence; iv) a masking polypeptide sequence (e.g., a TGF-β receptor polypeptide sequence or anti-TGF-β polypeptide sequence); and v) optionally one or more independently selected linker polypeptide sequences (e.g., between any of the foregoing polypeptide sequences of the second polypeptide); wherein the masking polypeptide sequence (e.g., TGF-β receptor polypeptide sequence or anti-TGF-β polypeptide sequence) and the TGF-β polypeptide sequence bind to each other (interact with each to mask the TGF-β polypeptide sequence). See e.g., FIG 1, structure C. 10. The masked TGF-β complex heterodimer of aspect 9, wherein the second polypeptide comprises in order from N-terminus to C-terminus: i) the scaffold polypeptide sequence comprising the counterpart interspecific dimerization sequence, the masking polypeptide sequence (e.g., TGF-β receptor polypeptide sequence), and the TGF-β polypeptide sequence; ii) a first MOD polypeptide sequence, the scaffold polypeptide sequence comprising the counterpart interspecific dimerization sequence, the masking polypeptide sequence (e.g., TGF-β receptor polypeptide sequence), and the TGF-β polypeptide sequence; or iii) a first independently selected MOD polypeptide sequence, a second independently selected MOD polypeptide sequence, the scaffold polypeptide sequence comprising the counterpart interspecific dimerization sequence, the masking polypeptide sequence (e.g., TGF-β receptor polypeptide sequence), and the TGF-β polypeptide sequence. See e.g., FIG 1, structure C. 11. A complex comprising a first polypeptide and a second polypeptide as a heterodimer (or multimer), wherein: (i) the first polypeptide comprises a) a scaffold polypeptide sequence comprising an interspecific dimerization sequence, b) a masking polypeptide sequence (e.g., a TGF-β receptor polypeptide sequence or anti-TGF-β polypeptide sequence), c) optionally, one or more (e.g., one, two or more) independently selected MOD polypeptide sequences, and d) optionally one or more independently selected linker polypeptide sequences (e.g., between any of the foregoing polypeptide sequences of the first polypeptide); (ii) the second polypeptide comprises a) a scaffold polypeptide sequence comprising a counterpart interspecific dimerization sequence to the interspecific dimerization sequence in the first polypeptide, b) a TGF-β polypeptide sequence, c) optionally, one or more (e.g., one, two or more) independently selected MOD polypeptide sequences, and d) optionally one or more independently selected linker polypeptide sequences (e.g., between any of the foregoing polypeptide sequences of the second polypeptide); a complex comprising these elements being collectively referred to as a “masked TGF-β complex,” wherein the masking polypeptide sequence (e.g., TGF-β receptor polypeptide sequence or anti-TGF-β polypeptide sequence) and the TGF-β polypeptide sequence bind to each other (interact with each other to mask the TGF-β polypeptide sequence); wherein the interspecific binding sequence and the counterpart interspecific binding sequence interact with each other (e.g., bind non-covalently) in the heterodimer; and wherein masked TGF-β first polypeptide and/or the second polypeptide optionally comprise one or more independently selected linker polypeptide sequences (e.g., between any of their polypeptide sequences). See e.g., FIG 1, structures D and E. 12. The masked TGF-β complex heterodimer of aspect 11, wherein the first polypeptide comprises, from N-terminus to C-terminus: a) one or two (or more) independently a) one or two (or more) independently selected MOD sequences, a scaffold polypeptide sequence comprising an interspecific dimerization sequence, and the masking polypeptide sequence (e.g., TGF-β receptor polypeptide sequence), or b) a scaffold polypeptide sequence comprising an interspecific dimerization sequence, and the masking polypeptide sequence (e.g., TGF-β receptor polypeptide sequence); and the second polypeptide comprises, from N-terminus to C-terminus one or two (or more) independently selected MOD sequences, a scaffold polypeptide sequence comprising the counterpart interspecific dimerization sequence, and the TGF-β polypeptide sequence. 13. The masked TGF-β construct or complex of any of aspects 1-12, wherein the scaffold polypeptide sequence(s) are selected from the group consisting of Ig Fc polypeptide sequences (e.g., CH2-CH3 region sequences); Ig heavy chain region 1 (CH1) domains; light chain constant regions (“CL”) (e.g. an Ig κ chain (kappa chain) constant region or an Ig λ chain (lambda chain)); leucine zipper polypeptide sequences; Fos or Jun binding pair sequences; collectin polypeptides (e.g., ACRP30 or ACRP30-like proteins); coiled-coil domains; and variants of any of the foregoing (e.g., knob-in-hole and other interspecific sequences in Table 1). 14. The masked TGF-β construct or complex of any of aspects 1-13, wherein the scaffold polypeptide sequence is selected from the group consisting of Ig Fc polypeptide sequences (immunoglobulin sequences); Ig heavy chain sequences (e.g., CH2-CH3 region sequences); Ig heavy chain region 1 (CH1) domains; light chain constant regions (“CL”) (e.g. an Ig κ chain (kappa chain) and variants of any of the foregoing. In one embodiment, the scaffold polypeptide are selected from an Ig CH1 domain bearing MD13 substitutions or Ig κ chain sequence bearing MD13 substitutions. 15. The masked TGF-β construct or complex of aspect 14, where the immunoglobulin sequences comprise a sequence having at least about 70%, at least about 80%, at least about 90%, at least about 95%, at least about 98%, at least about 99%, or 100% aa sequence identity to any of SEQ ID NOs: 68 to 83 or 85-87. See, e.g., FIGs.2A-2H, and 2J-2K. (Immunoblobulin sequence can form dimers and in the case of IgM sequence, such as in FIG.2H, multimers). 16. The masked TGF-β construct or complex of 15, where the immunoglobulin sequences comprise an immunoglobulin heavy chain sequence having at least about 70%, at least about 80%, at least about 90%, at least about 95%, at least about 98%, at least about 99%, or 100% aa sequence identity to any of SEQ ID NOs: 68 to 83. See, e.g., FIGs.2A-2H. (Immunoblobulin sequence can form dimers and in the case of IgM sequence, such as in FIG.2H, multimers). 17. The masked TGF-β construct or complex of any one of aspects 4 and 6-16, wherein the scaffold polypeptide sequences have one or more (e.g., one, two or more) covalent attachments to each other. 18. The masked TGF-β construct or complex of aspect 17, where at least one (e.g., one, two or more) of the one or more covalent attachments is a disulfide bond between the scaffold polypeptide sequence of the first polypeptide and the scaffold polypeptide sequence of the second polypeptide. 19. The masked TGF-β construct or complex of any of aspects 14-18, wherein the scaffold sequences are immunoglobulin heavy chain constant region (Ig Fc) polypeptide sequences comprising CH2-CH3 immunoglobulin regions that are optionally covalently linked by one or more (e.g., one, two or more) disulfide bonds. 20. The masked TGF-β construct of aspects 5, wherein the scaffold polypeptide comprises an interspecific dimerization sequence selected from the group consisting of: i) an interspecific immunoglobulin (Ig) heavy chain sequence; ii) an Ig CH1 domain; iii) an Ig light chain constant region (“CL”) (e.g. an Ig κ chain (kappa chain) or an Ig λ chain (lambda chain) constant region); and (iv) a polypeptide of a Fos/Jun binding pair. In one embodiment the scaffold polypeptide comprises an interspecific dimerization sequence selected from an Ig CH1 domain bearing MD13 substitutions or an Ig κ chain sequence bearing MD13 substitutions. 21. The masked TGF-β construct of aspect 20, wherein the interspecific binding sequence comprises a sequence having at least about 70%, at least about 80%, at least about 90%, at least about 95%, at least about 98%, at least about 99%, or 100% aa sequence identity to any of SEQ ID NOs: 68 to 82 or 85-87. See, e.g., FIGs.2A-2G, and 2J-2K. 22. The masked TGF-β complex of any of aspects 4 and 6-12, wherein the scaffold polypeptide of the first polypeptide and the second polypeptide comprise an interspecific dimerization sequence and a counterpart interspecific dimerization sequence pair selected from the group consisting of: (i) interspecific immunoglobulin (Ig) heavy chain sequences (e.g., heavy chain CH1-CH2 regions); (ii) an Ig CH1 domain and one of its counterpart interspecific light chain constant region (“CL”) (e.g. an Ig κ chain (kappa chain) constant region or an Ig λ chain (lambda chain) constant region); (iii) Fos/Jun binding pairs; and (iv) Ig heavy chain region 1 (CH1) and light chain constant region (“CL”) sequences (CH1/CL pairs such as a CH1 sequence paired with a κ or λ Ig light chain constant region sequence). In one embodiment, the scaffold polypeptide of the first polypeptide and the second polypeptide comprise an interspecific dimerization sequence and a counterpart interspecific dimerization sequence pair that comprise an Ig CH1 domain bearing MD13 substitutions and an Ig κ chain sequence bearing MD13 substitutions. 23. The masked TGF-β complex of aspect 22, wherein the scaffold polypeptide sequences have one or more (e.g., one, two or more) covalent attachments to each other. 24. The masked TGF-β complex of aspect 22, where at least one (e.g., one, two or more) of the one or more covalent attachments is a disulfide bond between the scaffold sequence of the first polypeptide and the scaffold sequence of the second polypeptide. 25. The masked TGF-β complex of any of aspects 22-24, wherein the scaffold sequences are immunoglobulin heavy chain constant region (Ig Fc) polypeptide sequences comprising CH2-CH3 immunoglobulin regions that are optionally covalently linked by one or more (e.g., one, two or more) disulfide bonds (between the first and second polypeptides). 26. The masked TGF-β complex of any of aspects 22-25, wherein the interspecific binding sequence and/or the counterpart interspecific binding sequence comprise a sequence having at least about 70%, at least about 80%, at least about 90%, at least about 95%, at least about 98%, at least about 99%, or 100% aa sequence identity to any of SEQ ID NOs: 68 to 82 or 85-87. See, e.g., FIGs.2A-2G, and 2J-2K. 27. The masked TGF-β complex of 26, where the immunoglobulin sequences comprise an immunoglobulin heavy chain sequence having at least about 70%, at least about 80%, at least about 90%, at least about 95%, at least about 98%, at least about 99%, or 100% aa sequence identity to any of SEQ ID NOs: 68 to 83. See, e.g., FIGs.2A-2H. (Immunoblobulin sequence can form dimers and in the case of IgM sequence, such as in FIG.2H, multimers). 27. The masked TGF-β construct or complex of any of aspects 1-27, comprising a scaffold polypeptide sequence, optionally comprising an interspecific dimerization sequence and/or a counterpart interspecific dimerization sequence, wherein the scaffold polypeptide sequence has at least about 70% (e.g., at least about 80%, at least about 90%, at least about 95%, at least about 98%, at least about 99%, or 100%) aa sequence identity to at least 150 contiguous aas (at least 175, at least 200, at least 225, at least 250, at least 275, at least 300, at least 325, or at least 350 contiguous aas), or all aas, of the IgA Fc sequence depicted in FIG.2A (SEQ ID NO:68). 28. The masked TGF-β construct or complex of any of aspects 1-27, comprising a scaffold polypeptide sequence, optionally comprising an interspecific dimerization sequence and/or a counterpart interspecific dimerization sequence, wherein the scaffold polypeptide sequence has at least about 70% (e.g., at least about 80%, at least about 90%, at least about 95%, at least about 98%, at least about 99%, or 100%) aa sequence identity to at least 150 contiguous aas (at least 175, at least 200, at least 225, at least 250, at least 275, at least 300, at least 325, or at least 350 contiguous aas), or all aas, of the IgD Fc sequence depicted in FIG.2B (SEQ ID NO:69). 29. The masked TGF-β construct or complex of any of aspects 1-27, comprising a scaffold polypeptide sequence, optionally comprising an interspecific dimerization sequence and/or a counterpart interspecific dimerization sequence, wherein the scaffold polypeptide sequence has at least about 70% (e.g., at least about 80%, at least about 90%, at least about 95%, at least about 98%, at least about 99%, or 100%) aa sequence identity to least 125 contiguous aas (at least 150, at least 175, or at least 200 contiguous aas), or all aas, of the IgE Fc sequence depicted in FIG.2C (SEQ ID NO:70). 30. The masked TGF-β construct or complex of any of aspects 1-27, comprising a scaffold polypeptide sequence, optionally comprising an interspecific dimerization sequence and/or a counterpart interspecific dimerization sequence, wherein the scaffold polypeptide sequence has at least about 70% (e.g., at least about 80%, at least about 90%, at least about 95%, at least about 98%, at least about 99%, or 100%) aa sequence identity to least 125 contiguous aas (at least 150, at least 175, or at least 200 contiguous aas), or all aas, of the wt. IgG Fc polypeptide sequence, such as the IgG1 Fc sequence depicted in FIG.2D (SEQ ID NOs: 71-78). 31. The masked TGF-β construct or complex of any of aspects 1-27, comprising a scaffold polypeptide sequence, optionally comprising an interspecific dimerization sequence and/or a counterpart interspecific dimerization sequence, wherein the scaffold polypeptide sequence has at least about 70% (e.g., at least about 80%, at least about 90%, at least about 95%, at least about 98%, at least about 99%, or 100%) aa sequence identity to at least 125 contiguous aas (at least 150, at least 175, at least 200, at least 225, at least 250, at least 275, or at least 300), or all aas, of the IgG2 Fc polypeptide sequence depicted in FIG.2E (SEQ ID NO:79). 32. The masked TGF-β construct or complex of any of aspects 1-27, comprising a scaffold polypeptide sequence, optionally comprising an interspecific dimerization sequence and/or a counterpart interspecific dimerization sequence, wherein the scaffold polypeptide sequence has at least about 70% (e.g., at least about 80%, at least about 90%, at least about 95%, at least about 98%, at least about 99%, or 100%) aa sequence identity to at least 125 contiguous aas (at least 150, at least 175, at least 200, or at least 225), or all aas, of the IgG3 Fc sequence depicted in FIG.2F (SEQ ID NO:80). 33. The masked TGF-β construct or complex of any of aspects 1-27, comprising a scaffold polypeptide sequence, optionally comprising an interspecific dimerization sequence and/or a counterpart interspecific dimerization sequence, wherein the scaffold polypeptide sequence has at least about 70% (e.g., at least about 80%, at least about 90%, at least about 95%, at least about 98%, at least about 99%, or 100%) aa sequence identity to at least 125 contiguous aas (at least 150, at least 175, at least 200, at least 225, or at least 250,), or all aas, of the IgG4 Fc sequence depicted in FIG.2G (SEQ ID NO:81 or 82). 34. The masked TGF-β complex of any of aspects 27-33, comprising one or two interchain disulfide bonds between the first and second polypeptides (e.g., between cystines adjacent to their hinge regions of the IgA, IgD, IgE, IgG1, IgG2, IgG3 or IgG4 sequences). 35. The masked TGF-β construct or complex of any of aspects 1-34, wherein one or more scaffold polypeptides comprise an immunoglobulin (Ig) polypeptide sequence bearing one or more substitutions that limits (e.g., reduces) binding of the polypeptide to complement component 1q (C1q) and/or Fc lambda receptor (FcλR) and/or that substantially reduces or eliminates the ability of the Ig polypeptide to induce cell lysis though complement-dependent cytotoxicity (CDC) and/or antibody-dependent cellular cytotoxicity (ADCC). 36. The masked TGF-β construct or complex of aspect 35, wherein each scaffold polypeptide comprises an immunoglobulin (Ig) polypeptide sequence comprising a polypeptide having at least about 70% (e.g., at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 98%, at least about 99%, or 100%) aa sequence identity to least 125 contiguous aas (at least 150, at least 175, at least 200, or at least 220 contiguous aas) of wt. IgG1 Fc Sequence (SEQ ID NO:71). 37. The masked TGF-β construct or complex of aspect 36, wherein the immunoglobulin polypeptide sequence comprises a substitution of any one, two, or more of aas 234, 235, 236, 237, 238, and 239 (234-LLGGPS-239). 38. The masked TGF-β construct or complex of aspect 36 or 37, wherein the immunoglobulin polypeptide sequence comprises a substitution at any one, two or more of N297, P331, D270, K322, and/or P329. 39. The masked TGF-β construct or complex of any of aspects 36-38 wherein the immunoglobulin polypeptide sequence comprises an N297 substitution (N77 of SEQ ID NO:71) with an aa other than asparagine (e.g., alanine to give aN297A such as in SEQ ID NO:74). 40. The masked TGF-β construct or complex of any of aspects 36-38 wherein the immunoglobulin polypeptide sequence comprises an L234 and/or L235 (L14 and L15 in SEQ ID NO:71) substitution with an aa other than leucine (e.g., alanine, L234A and/or L235A). 41. The masked TGF-β construct or complex of 39, wherein the immunoglobulin polypeptide sequence comprises an L234A and/or L235A substitutions (see e.g., SEQ ID NO:75). 42. The masked TGF-β construct or complex of any of aspects 36-41 wherein the immunoglobulin polypeptide sequence comprises P331 (P111 of SEQ ID NO:71)) substituted with an aa other than proline (e.g., serine for a P331S substitution). 43. The masked TGF-β construct or complex of any of aspects 36-38, wherein the immunoglobulin polypeptide sequence comprises substitutions at L234 and/or L235, and a substitution of P331. 44. The masked TGF-β construct or complex of aspect 43 wherein the immunoglobulin polypeptide sequence comprises (i) L234F, L235E, and P331S or (ii) L234A, L235A, and P331S substitutions. 45. The masked TGF-β construct or complex of any of aspects 20-44, comprising an interspecific dimerization sequence of an interspecific dimerization pair selected from the group consisting of KiH, KiHs-s, HA-TF, ZW-1, 7.8.60, DD-KK, EW-RVT, EW-RVTs-s, and A107 sequences (see, e.g., Table 1). 46. The masked TGF-β complex of any of aspects 4 and 22-44, wherein interspecific dimerization sequence and a counterpart interspecific dimerization sequence are a pair of sequences is selected from the group consisting of KiH, KiHs-s, HA-TF, ZW-1, 7.8.60, DD-KK, EW-RVT, EW-RVTs-s, and A107 sequence pairs (see, e.g., Table 1). 47. The masked TGF-β complex of aspect 46, wherein one of the first polypeptide and the second polypeptides comprise an interspecific IgG1polypeptide sequence (e.g., a sequence of SEQ ID NO:71) comprising a T366Y substitution and the other a Y407T substitution, or corresponding substitutions in other interspecific immunoglobulin heavy chain sequences (e.g., interspecific sequences comprising IgA, IgD, IgE, IgG2, IgG3 or IgG4 heavy chain sequences). 48. The masked TGF-β complex of aspect 46, wherein one of the first polypeptide and the second polypeptides comprise an interspecific IgG1polypeptide sequence (e.g., a sequence of SEQ ID NO:71) comprising a T366W substitution and the other T366S, L368A and Y407V substitutions, or corresponding substitutions in other interspecific immunoglobulin heavy chain sequences (e.g., interspecific sequences comprising IgA, IgD, IgE, IgG2, IgG3 or IgG4 heavy chain sequences). 49. The masked TGF-β complex of aspect 46, wherein one of the first polypeptide and the second polypeptides comprise an interspecific IgG1polypeptide sequence (e.g., a sequence of SEQ ID NO:71) comprising Y349C, T366S, L368A, and Y407V substitutions and the other S354C, and T366W substitutions, or corresponding substitutions in other interspecific immunoglobulin heavy chain sequences (e.g., interspecific sequences comprising IgA, IgD, IgE, IgG2, IgG3 or IgG4 heavy chain sequences). 50. The masked TGF-β complex of aspect 46, wherein the first polypeptide comprises an IgG1 scaffold having a T146W KiH sequence substitution, and the second polypeptide comprises an IgG1 scaffold having T146W, L148A, and Y187V KiH sequence substitutions, where the scaffolds comprises a sequence having at least 80%, 90%. 95%, 98%, 99%, or 100% sequence identity to at least 170 (e.g., at least 180, at least 190, at least 200, at least 210, at least 220, or all 227) contiguous aas of the IgG1 of SEQ ID NO:71, and optionally comprises substitutions at one of more of: L14 and L15 (e.g., L14A/L15A “LALA” or L14F/L15E); N77 (e.g., N77A); P111 (e.g. P111S); L131 (e.g., L131K); T146 (e.g., T146S); P175 (e.g., P175V); F185 (e.g., F185R); Y187 (e.g., Y187A); and K189 (e.g., K189Y) as numbered in SEQ ID NO:71. 51. The masked TGF-β complex of aspect 46, wherein the first polypeptide comprises an IgG1 scaffold having a T146W KiH sequence substitution, and the second polypeptide comprises an IgG1 scaffold having T146S, L148A, and Y187V KiH sequence substitutions, where the scaffolds comprises a sequence having at least 80%, 90%. 95%, 98%, 99%, or 100% sequence identity to at least 170 (e.g., at least 180, at least 190, at least 200, at least 210, at least 220, or all 227) contiguous aas of the IgG1 of SEQ ID NO:71; with none, one, or both of the scaffold aa sequences comprising L14 and L15 substitutions (e.g., L234A and L235A “LALA” in Kabat numbering), and/or N77 substitution to remove effector function by blocking interactions with Fcγ receptors (N297 e.g., N297A or N297G in Kabat numbering). See e.g., FIG 2D SEQ ID NOs: 77 and 78, 52. The masked TGF-β complex of aspect 46, wherein the first polypeptide comprises an IgG1 scaffold having T146W and S134C KiHs-s substitutions, and the second polypeptide comprises an IgG1 scaffold having T146S, L148A, Y187V and Y129C KiHs-s substitutions, where the scaffolds comprise a sequence having at least 80%, 90%. 95%, 98%, 99%, or 100% sequence identity to at least 170 (e.g., at least 180, at least 190, at least 200, at least 210, at least 220, or all 227) contiguous aas of the IgG1 of SEQ ID NO:71; with none, one, or both of the scaffold aa sequences of the first and second polypeptide comprising L14 and L15 substitutions (e.g., L234A and L235A “LALA” in Kabat numbering), and/or N77 (N297 in Kabat numbering) substitution to remove effector function by blocking interactions with Fcγ receptors (e.g., N297A or N297G substitutions in Kabat numbering). 53. The masked TGF-β complex of aspect 46, wherein the first and second polypeptide are selected from: a first polypeptide comprising an IgG1 scaffold having S144H and F185A substitutions, and a second polypeptide comprising an IgG1 scaffold having Y129T and T174F substitutions; a first polypeptide comprising an IgG1 scaffold having T130V, L131Y, F185A, and Y187V substitutions, and a second polypeptide comprising an IgG1 scaffold having 130V, T146L, K172L, and T174W substitutions; a first polypeptide comprising an IgG1 scaffold having K140D, D179M, and Y187A substitutions, and a second polypeptide comprising an IgG1 scaffold having E125R, Q127R, T146V, and K189V substitutions; a first polypeptide comprising an IgG1 scaffold having K189D, and K172D substitutions, and a second polypeptide comprising an IgG1 scaffold having D179K and E136K substitutions; a first polypeptide comprising an IgG1 scaffold having K140E and K189W substitutions, and a second polypeptide comprising an IgG1 scaffold having Q127R, D179V, and F185T substitutions; a first polypeptide comprising an IgG1 scaffold having K140E, K189W, and Y129C substitutions, and a second polypeptide comprising an IgG1 scaffold having Q127R, D179V, F185T, and S134C substitutions; and a first polypeptide comprising an IgG1 scaffold having K150E and K189W substitutions, and a second polypeptide comprising an IgG1 scaffold having E137N, D179V, and F185T substitutions; wherein the scaffolds comprise a sequence having at least 80%, 90%.95%, 98%, 99%, or 100% sequence identity to at least 170 (e.g., at least 180, at least 190, at least 200, at least 210, at least 220, or all 227) contiguous aas of the IgG1 of SEQ ID NO:71; and wherein none, one, or both of the scaffold aa sequences of the first and second polypeptide comprising L14 and L15 substitutions (e.g., L234A and L235A “LALA” in Kabat numbering), and/or N77 (N297 in Kabat numbering) substitution to remove effector function by blocking interactions with Fcγ receptors (e.g., N297A or N297G substitutions in Kabat numbering). 54. The masked TGF-β construct of aspects 20, wherein the wherein the scaffold polypeptide comprises an interspecific dimerization sequence selected from the group consisting of: (i) an Ig heavy chain CH1 domain (e.g., the polypeptide of SEQ ID NO:85); (ii) an Ig κ chain constant region sequence (e.g., SEQ ID NO:86); and (iii) an Ig λ chain constant region sequence (e.g., SEQ ID NO:87); where the scaffold comprises a sequence having at least 80% (85%, 90%. 95%, 98%, 99%, or 100%) sequence identity to at least 70, at least 80, at least 90, or at least 100 contiguous aas of SEQ ID NOs: 85, 86, or 87 respectively. See FIGs.2J and 2K. The Ig CH1 domain and/or the Ig κ chain sequence optionally comprise their respective MD13 substitutions. 55. The masked TGF-β complex of aspect 22, wherein the scaffold polypeptide of one of the first and second polypeptides comprises an Ig heavy chain CH1 domain (e.g., the polypeptide of SEQ ID NO:85); and the other of the first and second polypeptides comprise either an Ig κ chain constant region sequence (e.g., SEQ ID NO:86 optionally comprising MD13 substitutions) or an Ig λ chain constant region sequence (e.g., SEQ ID NO:87); wherein the scaffolds comprise a sequence having at least 80% (85%, 90%. 95%, 98%, 99%, or 100%) sequence identity to at least 70, at least 80, at least 90, or at least 100) contiguous aas of SEQ ID NOs: 85, 86, or 87 respectively). See FIGs.2J and 2K. 56. The masked TGF-β construct or complex of any of aspects 1-56, wherein the masked TGF-β construct or complex comprises at least one (e.g., at least two, or at least three) independently selected linker polypeptide sequences. 57. The masked TGF-β construct or complex of aspect 56, wherein the independently selected linkers have a length from about 1 aa to about 25 aa, (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, or 25 aa in length). 58. The masked TGF-β construct or complex of aspect 56, wherein the independently selected linkers have a length from about 25 to about 35 aa in length (e.g., 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, or 35 aa in length). 59. The masked TGF-β construct or complex of aspect 56, wherein the independently selected linkers have a length from about 35 to about 50 aa in length (e.g., 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, or 45, 46, 47, 48, 49, or 50, aa in length). 60. The masked TGF-β construct or complex of any of aspects 56 to 59, wherein at least one (e.g., at least two, or at least three) of the independently selected linkers comprises a (i) glycine or a polyglycine containing sequence having from about 2 to about 50 contiguous glycine residues; (ii) glycine-serine polymer (e.g., (GS)n, (GSGGS)n (SEQ ID NO:126), (GGGGS)n SEQ ID NO:136, and (GGGS)n (SEQ ID NO:127), where n is an integer of at least one (e.g., 1-10, 10-20, or 20-30); or (iii) glycine-alanine polymer or alanine-serine polymer (e.g., having a length of 1-10, 10-20, or 20-30 aa). 61. The masked TGF-β construct or complex of any of aspects 56 to 59, wherein at least one (e.g., at least two, or at least three) of the independently selected linkers comprises an aa sequence selected from the group consisting of: GGSG (SEQ ID NO:128), GGSGG (SEQ ID NO:129), GSGSG (SEQ ID NO:130), GSGGG (SEQ ID NO:131), GGGSG (SEQ ID NO:132), GSSSG (SEQ ID NO:133), GSGS (SEQ ID NO:134), GSSSSS (SEQ ID NO:135), GGGGS SEQ ID NO:136, and the like. 62. The masked TGF-β construct or complex of any of aspects 56 to 59, wherein at least one of the independently selected linkers comprises a cysteine residue(e.g., a GCGASGGGGSGGGGS linker aa sequence SEQ ID NO:137) that can or does form a disulfide bond with a cysteine residue present in a second polypeptide (e.g., in a linker of the second polypeptide) of the masked TGF-β construct or complex. 63. The masked TGF-β construct or complex of any of aspects 1 to 62, wherein the one or more (e.g., one, two or more) independently selected MOD polypeptide sequences are selected from the group consisting of: PD-L1, FAS-L, IL-1, IL-2, IL-4, IL-6, IL-7, IL-10, IL-15, IL-21, IL-23 MOD polypeptide sequences, and variants of any thereof (e.g., variants having reduced affinity for their receptor relative to the corresponding wt. MOD polypeptide sequence). 64. The masked TGF-β construct or complex of any of aspects 1 to 62, wherein the one or more (e.g., one, two or more) independently selected MOD polypeptide sequences are selected from the group consisting of: PD-L1, FAS-L, IL-2, IL-4, IL-6, IL-7, IL-10, IL-21, IL-23 MOD polypeptide sequences, and variants of any thereof (e.g., variants having reduced affinity for their receptor relative to the corresponding wt. MOD polypeptide sequence). 65. The masked TGF-β construct or complex of any of aspects 1 to 62, wherein the one or more (e.g., one, two or more) independently selected MOD polypeptide sequences are selected from the group consisting of: PD-L1, FAS-L, IL-2, IL-10 MOD polypeptide sequences, and variants of any thereof (e.g., variants having reduced affinity for their receptor relative to the corresponding wt. MOD polypeptide sequence). 66. The masked TGF-β construct or complex of any of aspects 1 to 62, wherein at least one (e.g., at least two) of the MOD polypeptide sequences is an IL-2 MOD polypeptide sequence or variant IL-2 MOD polypeptide sequence: (i) having at least 80% (e.g., at least 85%, at least 90%, at least 95%, at least 98%, or at least 99%) aa sequence identity to at least 80 (e.g., 90, 100, 110, 120, 130 or 133) contiguous aas of SEQ ID NO:9; or (ii) having at least 80% (e.g., at least 85%, at least 90%, at least 95%, at least 98%, or at least 99%) aa sequence identity to at least 80 (e.g., 90, 100, 110, 120, 130 or 133) contiguous aas of SEQ ID NO:13-27. 67. The masked TGF-β construct or complex of any of aspects 1 to 62, wherein the one or more (e.g., one, two or more) independently selected MOD polypeptide sequences comprise: (i) at least one (e.g., at least two) IL-2 MOD polypeptide sequence or variant IL-2 MOD polypeptide sequence (e.g., variant IL-2 MOD polypeptide sequence of aspect 66); and (ii) at least one (e.g., at least two) MOD polypeptide sequence selected from the group consisting of PD-L1, FAS-L, IL-1, IL-4, IL-6, IL-7, IL-10, IL-15, IL-21, IL-23 MOD polypeptide sequences, and variants of any thereof (e.g., variants having reduced affinity for their receptor relative to the corresponding wt. MOD polypeptide sequence). 68. The masked TGF-β construct or complex of any of aspects 1 to 62, wherein the one or more (e.g., one, two or more) independently selected MOD polypeptide sequences comprise: (i) at least one (e.g., at least two) wt. IL-2 MOD polypeptide sequence or variant IL-2 MOD polypeptide sequence (e.g., variant IL-2 MOD polypeptide sequence of aspect 66); and (ii) at least one (e.g., at least two) PD-L1 or PD-L2 MOD polypeptide sequence or variant PD-L1 or PD-L2 MOD polypeptide sequence (e.g., with reduced affinity for the PD1 receptor relative to the corresponding wt. sequence). 69. The masked TGF-β construct or complex of any of aspects 1 to 62, wherein the one or more (e.g., one, two or more) independently selected MOD polypeptide sequences comprise: (i) at least one (e.g., at least two) wt. IL-2 MOD polypeptide sequence or variant IL-2 MOD polypeptide sequence (e.g., variant IL-2 MOD polypeptide sequence of aspect 66); and (ii) at least one (e.g., at least two) FAS-L MOD polypeptide sequence or variant FAS-L MOD polypeptide sequence (e.g., with reduced affinity for the Fas receptor relative to the corresponding wt. sequence). 70. The masked TGF-β construct or complex of any of aspects 1 to 62, wherein the one or more (e.g., one, two or more) independently selected MOD polypeptide sequences comprise: (i) at least one (e.g., at least two) wt. IL-2 MOD polypeptide sequence or variant IL-2 MOD polypeptide sequence (e.g., variant IL-2 MOD polypeptide sequence of aspect 66); and (ii) at least one (e.g., at least two) IL-1 MOD polypeptide sequence or variant IL-1 MOD polypeptide sequence (e.g., with reduced affinity for the IL-1 receptor relative to the corresponding wt. sequence). 71. The masked TGF-β construct or complex of any of aspects 1 to 62, wherein the one or more (e.g., one, two or more) independently selected MOD polypeptide sequences comprise: (i) at least one (e.g., at least two) IL-2 MOD polypeptide sequence or variant IL-2 MOD polypeptide sequence (e.g., variant IL-2 MOD polypeptide sequence of aspect 66); and (ii) at least one (e.g., at least two), IL-4 MOD polypeptide sequence or variant,IL-4 MOD polypeptide sequence (e.g., with reduced affinity for the IL-4 receptor relative to the corresponding wt. sequence). 72. The masked TGF-β construct or complex of any of aspects 1 to 62, wherein the one or more (e.g., one, two or more) independently selected MOD polypeptide sequences comprise: (i) at least one (e.g., at least two) IL-2 MOD polypeptide sequence or variant IL-2 MOD polypeptide sequence (e.g., variant IL-2 MOD polypeptide sequence of aspect 66); and (ii) at least one (e.g., at least two) IL-6 MOD polypeptide sequence or variant IL-6 MOD polypeptide sequence (e.g., with reduced affinity for the IL-6 receptor relative to the corresponding wt. sequence). 73. The masked TGF-β construct or complex of any of aspects 1 to 62, wherein the one or more (e.g., one, two or more) independently selected MOD polypeptide sequences comprise: (i) at least one (e.g., at least two) IL-2 MOD polypeptide sequence or variant IL-2 MOD polypeptide sequence (e.g., variant IL-2 MOD polypeptide sequence of aspect 66); and (ii) at least one (e.g., at least two) IL-7 MOD polypeptide sequence or variant IL-7 MOD polypeptide sequence (e.g., with reduced affinity for the IL-7 receptor relative to the corresponding wt. sequence). 74. The masked TGF-β construct or complex of any of aspects 1 to 62, wherein the one or more (e.g., one, two or more) independently selected MOD polypeptide sequences comprise: (i) at least one (e.g., at least two) IL-2 MOD polypeptide sequence or variant IL-2 MOD polypeptide sequence (e.g., variant IL-2 MOD polypeptide sequence of aspect 66); and (ii) at least one (e.g., at least two) IL-10 MOD polypeptide sequence or variant IL-10 MOD polypeptide sequence (e.g., with reduced affinity for the IL-10 receptor relative to the corresponding wt. sequence). 75. The masked TGF-β construct or complex of any of aspects 1 to 62, wherein the one or more (e.g., one, two or more) independently selected MOD polypeptide sequences comprise: (i) at least one (e.g., at least two) IL-2 MOD polypeptide sequence or variant IL-2 MOD polypeptide sequence (e.g., variant IL-2 MOD polypeptide sequence of aspect 66); and (ii) at least one (e.g., at least two) IL-15 MOD polypeptide sequence or variant IL-15 MOD polypeptide sequence (e.g., with reduced affinity for the IL-15 receptor relative to the corresponding wt. sequence). 76. The masked TGF-β construct or complex of any of aspects 1 to 62, wherein the one or more (e.g., one, two or more) independently selected MOD polypeptide sequences comprise: (i) at least one (e.g., at least two) IL-2 MOD polypeptide sequence or variant IL-2 MOD polypeptide sequence (e.g., variant IL-2 MOD polypeptide sequence of aspect 66); and (ii) at least one (e.g., at least two) IL-21 MOD polypeptide sequence (e.g., a sequence of SEQ ID NO:58 or 60) or variant IL-21 (e.g., with reduced affinity for the IL-21 receptor relative to the corresponding wt. sequence) MOD polypeptide sequence. 77. The masked TGF-β construct or complex of any of aspects 1 to 62, wherein the one or more (e.g., one, two or more) independently selected MOD polypeptide sequences comprise: (i) at least one (e.g., at least two) wt. IL-2 MOD polypeptide sequence (e.g., comprising the sequence of SEQ ID NO:9) or variant IL-2 MOD polypeptide sequence (e.g., variant IL-2 MOD polypeptide sequence of aspect 66); and (ii) at least one (e.g., at least two) IL-23 MOD polypeptide sequence (e.g., of SEQ ID NO:63 or 65) or variant IL-23 (e.g., with reduced affinity for the IL-23 receptor relative to the corresponding wt. sequence) MOD polypeptide sequence. 78. The masked TGF-β construct or complex of any of aspects 63 to 77, wherein when the TGF-β polypeptide/polypeptide complex comprises a variant IL-2 MOD polypeptide sequence, the variant IL- MOD polypeptide (e.g., a variant of SEQ ID NO:9) comprises a substitution at any one of, two of, or all of N88, F42 and/or H16. 79. The masked TGF-β construct or complex of aspect 78, wherein at least one variant IL-2 MOD polypeptide sequence comprises an F42A, F42T, H16A, or H16T substitution. 80. The masked TGF-β construct or complex of aspect 78, wherein at least one variant IL-2 MOD polypeptide sequence comprises: (i) F42A and H16A; (ii) F42T and H16A; (iii) F42A and H16T; or (iv) F42T and H16T substitutions. 81. The masked TGF-β construct or complex of aspect 78, wherein at least one variant IL-2 MOD polypeptide sequence comprises: (i) N88R, F42A, and H16A; (ii) N88R, F42T, and H16A; (iii) N88R, F42A, and H16T; or (iv) N88R, F42T, and H16T substitutions. 82. The masked TGF-β construct or complex of any of aspects 1 to 81, wherein the masking polypeptide sequence is a TGF-β receptor (“TβR”) polypeptide sequence that comprises an ectodomain fragment of a type I (TβRI), type II (TβRII) or type III (TβRIII) TβR. 83. The masked TGF-β construct or complex of aspect 82, wherein the TβRII ectodomain sequence comprises an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 90 (e.g., at least 100, at least 110, at least 120, at least 130, at least 140, at least 150, or 154) contiguous aas of the TβRII isoform A ectodomain set forth in SEQ ID NO:117. 84. The masked TGF-β construct or complex of aspect 82, wherein the TβRII ectodomain sequence comprises an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 90 (e.g., at least 100, at least 110, at least 120, at least 130, at least 140, or 143) contiguous aas of the TβRII isoform B ectodomain set forth in SEQ ID NO:119. 85. The masked TGF-β construct or complex of aspect 82, wherein the TβRII ectodomain sequence comprises an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 90 (e.g., at least 100, at least 110, at least 120, at least 130, at least 140, or 143) contiguous aas of the TβRII isoform B ectodomain set forth in SEQ ID NO:120. 86. The masked TGF-β construct or complex of aspect 82, wherein the TβRII ectodomain sequence comprises an amino acid sequence selected from a TβRII isoform B polypeptide sequence that comprises: the ectodomain fragment of SEQ ID NO:120; the TβRII ectodomain N-terminal Δ14 (delta 14) aa deletion sequence in SEQ ID NO:121; the N-terminal Δ25(delta 25) aa deletion sequence set forth in SEQ ID NO:122; or a sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 70, at least 80, at least 90, at least 100, at least 110, or 118) contiguous aas of any of those TβRII isoform B polypeptide sequence. 87. The masked TGF-β construct or complex of any of aspects 83-86, wherein the TβRII ectodomain sequence comprises a substitution of any one, two, three, four, or all five of F30, D32, S52, E55, and/or D118 (e.g., with alanine or arginine). 88. The masked TGF-β construct or complex of any of aspects 83-87, comprising: a D118A or D118 R substitution (see e.g., SEQ ID NO:123 for the TβRII ectodomain with an N- terminal Δ25 deletion and a D118 substitution); or a D118A or D118R substitution and one, two, three, or all four of a F30A, D32N, S52L and/or E55A substitutions. 89. The masked TGF-β construct or complex of aspect 87, wherein the TβRII ectodomain sequence comprises an N-terminal deletion up to 14 aas (a Δ14 aa deletion) of SEQ ID NO:119 or SEQ ID NO:120 (see e.g., sequence in SEQ ID NO:121) and an D118 substitution (e.g., D118A or D118R); or a sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 70 (e.g., at least 80, at least 90, at least 100, at least 110, or 118) contiguous aas of any of those TβRII polypeptide sequences. 90. The masked TGF-β construct or complex of aspect 89, further comprising one, two, three, or all four of a F30A, D32N, S52L and/or E55A substitution. 91. The masked TGF-β construct or complex of aspect 87, wherein the TβRII ectodomain sequence comprises an N-terminal deletion up 25 aas (a Δ25 aa deletion) of SEQ ID NO:119 or SEQ ID NO:120 and D118 substitution (e.g., D118A or D118R, see SEQ ID NO:123); or a sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 70 (e.g., at least 80, at least 90, or at least 100) contiguous aas of any of those TβRII polypeptide sequences. 92. The masked TGF-β construct or complex of aspect 91, further comprising one, two, three, or all four of a F30A, D32N, S52L and/or E55A substitution. 93. The masked TGF-β construct or complex of aspect 82, wherein the TβR polypeptide sequence comprises a TβRI ectodomain sequence. 94. The masked TGF-β construct or complex of aspect 93, wherein the TβRI ectodomain sequence comprises an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 70 (e.g., at least 80, at least 90, or 93) contiguous aas of SEQ ID NO:115. 95. The masked TGF-β construct or complex of aspect 82, wherein the TβR polypeptide sequence comprises a TβRIII ectodomain sequence. 96. The masked TGF-β construct or complex of aspect 95, wherein the TβRIII ectodomain sequence comprises an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 70 (e.g., at least 80, 90, 100, 150, 200, 250, 300, 400, 500 or 600) contiguous aas of (aas 27-787of the A isoform SEQ ID NO:124 or aas 27-786 of the B isoform SEQ ID NO:125). 97. The masked TGF-β construct or complex of any of aspects 1 to 96, wherein the TGF-β polypeptide sequence comprises an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to polypeptide comprising at least 70 (e.g., at least 80, at least 90, at least 100, or at least 110) contiguous aas the mature form of a human TGF-β1 polypeptide, a human TGF-β2 polypeptide, or a human TGF-β3 polypeptide. 98. The masked TGF-β construct or complex of any of aspects 1 to 96, wherein the TGF-β polypeptide sequence is a TGF-β1 polypeptide comprising an amino acid sequence having at least 60% (at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 70 (e.g., at least 80, at least 90, at least 100, at least 110, or 112) contiguous aas of SEQ ID NO:105 (e.g., aas 279-390 of SEQ ID NO:106). 99. The masked TGF-β construct or complex of any of aspects 1 to 96, wherein the TGF-β polypeptide sequence is a TGF-β1 polypeptide bearing a C77S substitution comprising an amino acid sequence having at least 60% (at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) contiguous aa sequence identity to at least 70 (e.g., at least 80, at least 90, at least 100, at least 110, or 112) aas of SEQ ID NO:107. 100. The masked TGF-β construct or complex of any of aspects 1 to 96, wherein the TGF-β polypeptide sequence is a TGF-β2 polypeptide comprising an amino acid sequence having at least 60% (at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 70 (e.g., at least 80, at least 90, at least 100, at least 110, or 112) contiguous aas of (SEQ ID NO:108) (e.g. aas 302-413of SEQ ID NO:109). 101. The masked TGF-β construct or complex of any of aspects 1 to 96, wherein the TGF-β polypeptide sequence is a TGF-β2 polypeptide bearing a C77S substitution comprising an amino acid sequence having at least 60% (at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) contiguous aas sequence identity to at least 70 (e.g., at least 80, at least 90, at least 100, at least 110, or 112) aas of SEQ ID NO:110. 102. The masked TGF-β construct or complex of any of aspects 1 to 96, wherein the TGF-β polypeptide sequence is a TGF-β3 polypeptide comprising an amino acid sequence having at least 60% (at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 70 (e.g., at least 80, at least 90, at least 100, at least 110, or 112) contiguous aas of SEQ ID NO:111 (e.g. aas 301-412 of SEQ ID NO:112). 103. The masked TGF-β construct or complex of any of aspects 1 to 96, wherein the TGF-β polypeptide sequence is a TGF-β3 polypeptide bearing a C77S substitution comprising an amino acid sequence having at least 60% (at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 70 (e.g., at least 80, at least 90, at least 100, at least 110, or 112) contiguous aas of SEQ ID NO:113. 104. The masked TGF-β construct or complex of any of aspects 97-103, where in the TGF-β polypeptide sequence comprises a substitution at one or more of positions 25, 92 and/or 94 of the mature TGF-β polypeptide sequence (see e.g., SEQ ID NO:112 in FIG.3 and FIG.4). 105. The masked TGF-β construct or complex of any of aspects 100-101, where in the TGF-β polypeptide sequence comprises a substitution at one or more of positions 25, 92 and/or 94 of the mature TGF-β polypeptide sequence (see e.g., SEQ ID NO:112 in FIG.3 and FIG.4). 106. The masked TGF-β construct or complex of any of aspects 97-105 where in the TGF-β polypeptide sequence comprises: (i) an aa other than Lys or Arg at position 25 (ii) an aa other than Ile or Val at position 92; and/or (iii) an aa other than Lys or Arg at position 94 (e.g., based on SEQ ID NO:108 or SEQ ID NO:110). 107. The masked TGF-β construct or complex of any of aspects 1-106, wherein the masked TGF-β construct or complex has the form of any one of structures A-F in FIG.1. 108. The masked TGF-β construct or complex of aspect 107, wherein the masked TGF-β construct or complex is a masked TGF-β polypeptide having the form of structure A in FIG.1. 109. The masked TGF-β polypeptide of aspect 108, comprising at least one (e.g., one, two or more) wt. or variant IL-2 MOD polypeptide sequence. 110. The masked TGF-β construct or complex of aspect 107, wherein the masked TGF-β construct or complex is a masked TGF-β complex having the form of structure B in FIG.1. 111. The masked TGF-β polypeptide of aspect 110, comprising at least one (e.g., one, two or more) wt. or mutant IL-2 MOD polypeptide sequence. 112. The masked TGF-β construct or complex of aspect 107, wherein the masked TGF-β construct or complex is an interspecific masked TGF-β complex having the form of structure C in FIG.1. 113. The masked TGF-β polypeptide of aspect 112, comprising at least one (e.g., one, two or more) wt. or mutant IL-2 MOD polypeptide sequence. 114. The masked TGF-β construct or complex of aspect 107, wherein the masked TGF-β construct or complex is an interspecific masked TGF-β complex having the form of structure D or E in FIG.1. 115. The masked TGF-β polypeptide of aspect 114, comprising at least one (e.g., one, two or more) wt. or mutant IL-2 MOD polypeptide sequence. 116. The masked TGF-β construct or complex of aspect 107, wherein the masked TGF-β construct or complex is an interspecific masked TGF-β complex having the form of structure F in FIG.1. 117. The masked TGF-β polypeptide of aspect 116, comprising at least one (e.g., one, two or more) wt. or mutant IL-2 MOD polypeptide sequence. 118. The masked TGF-β construct or complex of any of aspects 107-117, wherein: the TGF-β polypeptide sequence comprises a wt. TGF-β3 polypeptide sequence (e.g., comprising the sequence of SEQ ID NO:111) or an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 70 (e.g., at least 80, at least 90, at least 100, at least 110, or at least 112) contiguous aas of the TGF-β3 sequence set forth in SEQ ID NO:111; the masking polypeptide sequence is a TβRII polypeptide sequence that comprises a wt. TβRII polypeptide sequence (e.g., comprising the sequence of SEQ ID NO:117) or an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 90 (e.g., at least 100, at least 110, at least 120, at least 130, at least 140, at least 150, or 154) contiguous aas of the TβRII isoform A ectodomain set forth in SEQ ID NO:117; and wherein the masked TGF-β construct or complex comprises a wt. IL-2 MOD polypeptide sequence (e.g., comprising the sequence of SEQ ID NO:9). 119. The masked TGF-β construct or complex of any of aspects 107-117, wherein: the TGF-β polypeptide sequence comprises a wt. TGF-β3 polypeptide sequence (e.g., comprising the sequence of SEQ ID NO:111) or an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 70 (e.g., at least 80, at least 90, at least 100, at least 110, or at least 112) contiguous aas of the TGF-β3 sequence set forth in SEQ ID NO:111; the masking polypeptide sequence is a TβRII polypeptide sequence that comprises a wt. TβRII polypeptide sequence (e.g., comprising the sequence of SEQ ID NO:119) or an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 90 (e.g., at least 100, at least 110, at least 120, at least 130, at least 140, at least 143) contiguous aas of the TβRII isoform B ectodomain set forth in SEQ ID NO:119; and wherein the masked TGF-β construct or complex comprises a wt. IL-2 MOD polypeptide sequence (e.g., comprising the sequence of SEQ ID NO:9). 120. The masked TGF-β construct or complex of any of aspects 107-117, wherein: the TGF-β polypeptide sequence comprises a wt. TGF-β3 polypeptide sequence (e.g., comprising the sequence of SEQ ID NO:111) or an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 70 (e.g., at least 80, at least 90, at least 100, at least 110, or at least 112) contiguous aas of the TGF-β3 sequence set forth in SEQ ID NO:111; the masking polypeptide sequence is a TβRII polypeptide sequence that comprises a wt. TβRII polypeptide sequence (e.g., comprising the sequence of SEQ ID NO:120) or an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 90 (e.g., at least 100, at least 110, at least 120, or at least 129) contiguous aas of the TβRII isoform B ectodomain set forth in SEQ ID NO:120; and wherein the masked TGF-β construct or complex comprises a wt. IL-2 MOD polypeptide sequence (e.g., comprising the sequence of SEQ ID NO:9). 121. The masked TGF-β construct or complex of any of aspects 107-117, wherein: the TGF-β polypeptide sequence comprises a wt. TGF-β3 polypeptide sequence (e.g., comprising the sequence of SEQ ID NO:111) or an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 70 (e.g., at least 80, at least 90, at least 100, at least 110, or at least 112) contiguous aas of the TGF-β3 sequence set forth in SEQ ID NO:111; the masking polypeptide sequence is a TβRII polypeptide sequence that comprises a wt. TβRII polypeptide sequence (e.g., comprising the sequence of SEQ ID NO:117) or an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 90 (e.g., at least 100, at least 110, at least 120, at least 130, at least 140, at least 150, or 154) contiguous aas of the TβRII isoform A ectodomain set forth in SEQ ID NO:117; and wherein the masked TGF-β construct or complex comprises a variant IL-2 MOD polypeptide sequence comprising an aa sequence having at least 80% (at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 80 (e.g., 90, 100, 110, 120, 130 or 133) contiguous aas of SEQ ID NO:9. 122. The masked TGF-β construct or complex of any of aspects 107-117, wherein: the TGF-β polypeptide sequence comprises a wt. TGF-β3 polypeptide sequence (e.g., comprising the sequence of SEQ ID NO:111) or an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 70 (e.g., at least 80, at least 90, at least 100, at least 110, or at least 112) contiguous aas of the TGF-β3 sequence set forth in SEQ ID NO:111; the masking polypeptide sequence is a TβRII polypeptide sequence that comprises a wt. TβRII polypeptide sequence (e.g., comprising the sequence of SEQ ID NO:119) or an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 90 (e.g., at least 100, at least 110, at least 120, at least 130, at least 140, at least 143) contiguous aas of the TβRII isoform B ectodomain set forth in SEQ ID NO:119; and wherein the masked TGF-β construct or complex comprises a variant IL-2 MOD polypeptide sequence comprising an aa sequence having at least 80% (at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 80 (e.g., 90, 100, 110, 120, 130 or 133) contiguous aas of SEQ ID NO:9. 123. The masked TGF-β construct or complex of any of aspects 107-117, wherein: the TGF-β polypeptide sequence comprises a wt. TGF-β3 polypeptide sequence (e.g., comprising the sequence of SEQ ID NO:111) or an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 70 (e.g., at least 80, at least 90, at least 100, at least 110, or at least 112) contiguous aas of the TGF-β3 sequence set forth in SEQ ID NO:111; the masking polypeptide sequence is a TβRII polypeptide sequence that comprises a wt. TβRII polypeptide sequence (e.g., comprising the sequence of SEQ ID NO:120) or an amino acid sequence having at least 60% (e.g., at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 90 (e.g., at least 100, at least 110, at least 120, or at least 129) contiguous aas of the TβRII isoform B ectodomain set forth in SEQ ID NO:120; and wherein the masked TGF-β construct or complex comprises a variant IL-2 MOD polypeptide sequence comprising an aa sequence having at least 80% (e.g., at least 85%, at least 90%, at least 95%, at least 98%, at least 99%, or 100%) aa sequence identity to at least 80 (e.g., 90, 100, 110, 120, 130 or 133) contiguous aas of SEQ ID NO:9. 124. The masked TGF-β construct or complex of any of aspects 121-123, wherein the TGF-β3 polypeptide sequence comprises a C77S substitution. 125. The masked TGF-β construct or complex of any of aspects 121-124, wherein the TβRII polypeptide sequence comprises a N-terminal Δ14 and either a D118A or a D118R sequence modifications, or a N-terminal Δ25 and either a D118A or a D118R sequence modifications. 126. The masked TGF-β construct or complex of any of aspects 121-125, wherein the IL-2 MOD polypeptide sequence comprises an aa substitution at H16 or an aa substitution at F42. 127. The masked TGF-β construct or complex of any of aspects 121-125, wherein the IL-2 MOD polypeptide sequence comprises an aa substitution at H16 and F42. 128. The masked TGF-β construct or complex of any of aspects 125-127, wherein the substitutions at H16 and F42 are selected from the group consisting of: H16A, H16T, F42A, and F42T (e.g., H16A and F42A or H16T and F42A). 129. The masked TGF-β construct or complex of any of aspects 121-128, wherein the IL-2 MOD polypeptide sequence further comprises an N88R aa substitution. 130a. The masked TGF-β construct or complex of any of aspects 121-129a wherein: the TGF-β3 polypeptide sequence comprises a C77S substitution; the TβRII polypeptide sequence comprises either N-terminal Δ14 and D118A or D118R sequence modifications or N-terminal Δ25 and D118A or D118R sequence modifications; and the IL-2 MOD polypeptide sequence comprises an aa substitution at H16 and F42. 130b. The masked TGF-β construct or complex of aspect 130a, wherein the substitutions at H16 and F42 are either an H16A and F42A substitution or an H16T and F42A substitutions. 131. The masked TGF-β construct or complex of any of aspects 1-130b further comprising a wild type or variant MOD polypeptide sequence selected from the group consisting of: PD-L1, FAS-L, IL-1, IL-2, IL-4, IL-6, IL-7, IL-10, IL-15, IL-21 and IL-23. 132. The masked TGF-β construct or complex of any of aspects 1-130b comprising a wild type or variant MOD polypeptide sequence selected from the group consisting of: PD-L1, FAS-L, IL-10. 133. The masked TGF-β construct or complex of any of aspects 1-132, wherein the TGF-β polypeptide/complexes comprises a variant TGF-β polypeptide with reduced affinity for the masking polypeptide (e.g., TGF-β receptor polypeptide) sequence at least 10% less (e.g., at least 20% less, at least 30% less, at least 40% less, at least 50% less, at least 60% less, at least 70% less, at least 80% less, at least 90% less, at least 95% less, or more than 95% less) relative to an otherwise identical wt. TGF-β polypeptide without the sequence variations. 134. The masked TGF-β construct or complex of any of aspects 1-133, wherein the TGF-β polypeptide/complex comprises a TβR polypeptide sequence with one or more sequence variations (e.g., one or more aa deletions, insertions or substitutions) with reduced affinity for the TGF-β polypeptide (at least 10% less, at least 20% less, at least 30% less, at least 40% less, at least 50% less, at least 60% less, at least 70% less, at least 80% less, at least 90% less, at least 95% less, or more than 95% less) relative to the corresponding wt. TβR polypeptide sequence without the sequence variations. 135. The masked TGF-β complex PSM-4033-4039. 136. One or more nucleic acids (e.g., expression vector(s)) encoding a masked TGF-β construct or complex of any of aspects 1-135 or encoding a masked TGF-β complex of any of aspects 4 and 6-135. 137. A method of inducing Treg cells in a mammalian (e.g., a human) subject or a cell, tissue, or bodily fluid thereof, the method comprising administering to a subject one or more masked TGF-β constructs or complexes according to any of aspects 1-135. 138. The method of aspect 137, where at least one of the one or more masked TGF-β constructs or complexes comprises a wt. or variant IL-2 MOD polypeptide sequence. 139. The method of aspect 137, where at least one of the one or more masked TGF-β constructs or complexes comprises (i) a wt. or variant IL-2 MOD polypeptide sequence, and (ii) a wt. or variant PL- L1 polypeptide sequence. 140. The method of any of aspects 137-139, wherein the one or more masked TGF-β constructs or complexes is administered before, during (concurrent or combined administration) or after administration of any one or more of vitamin D (e.g., 1α, 25-dihydroxy vitamin D3 or a vitamin D analog (e.g., vitamin D3), an mTOR inhibitor (e.g., rapamycin), and/or a retinoic acid (e.g., all trans retinoic acid). 141. The method of any of aspects 137-140, wherein the administration leads to an increase in the number of FoxP3+ Treg cells (e.g., any one or more of induced regulatory T cells (iTregs); thymus- derived Treg cells (tTreg), and/or peripheral Treg cells (pTreg)) in a volume of tissue or bodily fluid (e.g., blood or lymph) fluid from a subject relative to the number of those cells either: (i) before or absent administration of the one or more masked TGF-β constructs or complexes; or (ii) relative to the amount of the Treg cells in the tissue or bodily fluid of a treatment group (e.g., one subject or an average from two or more subjects) that are matched with the subject (e.g., one or more of disease state, age, sex, height, weight, and/or smoking habit) but that have not been administered TGF-β or a masked TGF-β construct or complex. 142. The method of aspect 141, wherein the number of Treg cells (e.g., FoxP3+ cells, iTregs, tTregs, and/or pTregs) increases in a volume of tissue or bodily fluid by at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 2-fold, at least 5-fold, at least 10-fold or more) relative to the number of Tregs in a volume of the tissue or the bodily fluid prior to administration of the one or more masked TGF-β constructs or complexes, or relative to the average value of the matched control group that did not receive the one or more masked TGF-β constructs or complexes. 143. A method of inducing Th9 cells a mammalian (e.g., a human) subject or a tissue or bodily fluid thereof, the method comprising administering to the subject one or more masked TGF-β constructs or complexes according to any of aspects 1-134. 144. The method of aspect 143, where at least one of the one or more masked TGF-β constructs or complexes comprises a wt. or variant IL-4 MOD polypeptide sequence. 145. The method of any of aspects 143-144, wherein the administration leads to an increase in the number of Th9 cells in a volume of tissue or bodily fluid (e.g., blood or lymph) fluid from a subject relative to the number of those cells either: (i) before or absent administration of the one or more masked TGF-β constructs or complexes ; or (ii) relative to the amount of Th9 cells in the tissue or bodily fluid of a control treatment group (e.g., the average from a group of individuals) matched with the subject (e.g., one or more of disease state, age, sex, height, weight, and/or smoking habit) but that have not been administered TGF-β or a masked TGF-β construct or complex. 146. The method of aspect 145, wherein the number of Th9 cells increases in a volume of tissue or bodily fluid by at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 2-fold, at least 5- fold, at least 10-fold or more) relative to the number of Th9 cells in a volume of the tissue or the bodily fluid prior to administration of the one or more masked TGF-β constructs or complexes, or relative to the average value of the matched control group that did not receive the one or more masked TGF-β constructs or complexes. 147. A method of inducing Th17 cells a mammalian (e.g, a human) subject or a tissue or bodily fluid thereof, the method comprising administering to the subject one or more masked TGF-β constructs or complexes according to any of aspects 1-134. 148. The method of aspect 147, where at least one of the one or more masked TGF-β constructs or complexes comprises a wt. or variant IL-6 MOD polypeptide sequence. 149. The method of any of aspects 147-148, wherein the administration leads to an increase in the number of Th17 cells in a volume of tissue or bodily fluid (e.g., blood or lymph) fluid from a subject relative to the number of those cells either: (i) before or absent administration of the one or more masked TGF-β constructs or complexes ; or (ii) relative to the amount of Th17 cells in the tissue or bodily fluid of a control treatment group (e.g., the average from a group of individuals) matched with the subject (e.g., one or more of disease state, age, sex, height, weight, and/or smoking habit) but that have not been administered TGF-β or a masked TGF-β construct or complex. 150. The method of aspect 149, wherein the number of Th17 cells increases in a volume of tissue or bodily fluid by at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 2-fold, at least 5- fold, at least 10-fold or more) relative to the number of Th17 cells in a volume of the tissue or the bodily fluid prior to administration of the one or more masked TGF-β constructs or complexes, or relative to the average value of the matched control group that did not receive the one or more masked TGF-β constructs or complexes. 151. A method of inducing Thf cells in a mammalian (e.g, a human) subject or a tissue or bodily fluid thereof, the method comprising administering to the subject one or more masked TGF-β constructs or complexes according to any of aspects 1-134. 152. The method of aspect 151, where at least one of the one or more masked TGF-β constructs or complexes comprises at least one wt. or variant IL-21 and/or IL-23 MOD polypeptide sequence. 153. The method of aspect 152, where at least one of the one or more masked TGF-β constructs or complexes comprises at least one wt. or variant IL-21 and at least one wt. or variant IL-23 MOD polypeptide sequence. 154. The method of any of aspects 151-153, wherein the administration leads to an increase in the number of Thf cells in a volume of tissue or bodily fluid (e.g., blood or lymph) fluid from a subject relative to the number of those cells either: (i) before or absent administration of the one or more masked TGF-β constructs or complexes ; or (ii) relative to the number of Thf in the tissue or bodily fluid of a control treatment group (e.g., the average from a group of individuals) matched with the subject (e.g., one or more of disease state, age, sex, height, weight, and/or smoking habit) but that have not been administered TGF-β or a masked TGF- β construct or complex. 155. The method of aspect 154, wherein the number of Thf cells increases in a volume of tissue or bodily fluid by at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 2-fold, at least 5- fold, at least 10-fold or more) relative to the number of Thf cells in a volume of the tissue or the bodily fluid prior to administration of the one or more masked TGF-β constructs or complexes, or relative to the average value of the matched control group that did not receive the one or more masked TGF-β constructs or complexes. 156. A method of inhibiting the action of Th1 cells in a mammalian subject (or a tissue or bodily fluid thereof), the method comprising administering to the subject one or more masked TGF-β constructs or complexes according to any of aspects 1-134. 157. The method of aspect 156, where at least one of the one or more masked TGF-β constructs or complexes comprises a wt. or variant IL-4 MOD polypeptide sequence. 158. The method of any of aspects 156-157, wherein the administration leads to an inhibition of Th1 mediated release of interferon γ and/or TNF into (or resulting concentration in) a volume of tissue or bodily fluid (e.g., blood or lymph) fluid from a subject relative to amount: (i) before or absent administration of the one or more masked TGF-β constructs or complexes ; or (ii) relative to the amount of interferon γ and/or TNF in the tissue or bodily fluid of a control treatment group (e.g., the average from a group of individuals) matched with the subject (e.g., one or more of disease state, age, sex, height, weight, and/or smoking habit) but that have not been administered TGF-β or a masked TGF-β construct or complex. 159. The method of aspect 149, wherein the amount of interferon γ and/or TNF in a volume of tissue or bodily fluid is decreased by at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 2- fold, at least 5-fold, at least 10-fold or more) relative to the amount of interferon γ and/or TNF in a volume of the tissue or the bodily fluid prior to administration of the one or more masked TGF-β constructs or complexes, or relative to the average value of the matched control group that did not receive the one or more masked TGF-β constructs or complexes. 160. A method of inhibiting the action and/or prolifation of Th2 cells in a mammalian (e.g, a human) subject or a tissue or bodily fluid thereof, the method comprising administering to the subject one or more masked TGF-β constructs or complexes according to any of aspects 1-134. 161. The method of aspect 160, wherein the administration leads to an inhibition of Th2 mediated release of IL-4, IL-5, and/or IL-13 into (or resulting concentration in) a volume of tissue or bodily fluid (e.g., blood or lymph) fluid from a subject relative to amount: (i) before or absent administration of the one or more masked TGF-β constructs or complexes ; or (ii) relative to the amount in the tissue or bodily fluid of a control treatment group (e.g., the average from a group of individuals) matched with the subject (e.g., one or more of disease state, age, sex, height, weight, and/or smoking habit) but that have not been administered TGF-β or a masked TGF-β construct or complex. 162. The method of aspect 161, wherein the amount of IL-4, IL-5, and/or IL-13 in a volume of tissue or bodily fluid is decreased by at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, or at least 90%) relative to the amount of IL-4, IL-5, and/or IL-13 in a volume of the tissue or the bodily fluid prior to administration of the one or more masked TGF-β constructs or complexes, or relative to the average value of IL-4, IL-5, and/or IL-13 in the tissue, or the bodily fluid from the matched control group that did not receive the one or more masked TGF-β constructs or complexes. 163. A method of inhibiting the action of type II innate lymphoid cells (ILC2 cells) in a mammalian (e.g, a human) subject or a tissue or bodily fluid thereof, the method comprising administering to the subject one or more masked TGF-β constructs or complexes according to any of aspects 1-134, wherein at least one of the one or more masked TGF-β constructs or complexes optionally comprise one or more independently selected wt. or variant IL-10 polypeptide sequences (e.g., a monomeric form such as IL- 10M1). 164. The method of aspect 160, wherein the administration leads to an inhibition of ILC2 cells mediated release of IL-5, and/or IL-13 into (or resulting concentration in) a volume of tissue or bodily fluid (e.g., blood or lymph) fluid from a subject relative to amount: (i) before or absent administration of the treatment with the one or more masked TGF-β constructs or complexes; or (ii) relative to the amount in the tissue or bodily fluid of a control treatment group (e.g., the average from a group of individuals) matched with the subject (e.g., one or more of disease state, age, sex, height, weight, and/or smoking habit) but that have not been administered TGF-β or a masked TGF-β construct or complex. 165. The method of aspect 164, wherein the amount of IL-5, and/or IL-13 in a volume of tissue or bodily fluid is decreased by at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, or at least 90%) relative to the amount of IL-5 and/or IL-13 in a volume of tissue, or the bodily fluid prior to administration of the one or more masked TGF-β constructs or complexes, or relative to the average value of IL-5 and/or IL-13 in the volume of tissue or the bodily fluid from the matched control group that did not receive the one or more masked TGF-β constructs or complexes. 166. The method of aspect 164, wherein the amount of IL-5, and/or IL-13 in a volume of tissue or bodily fluid is decreased by at at least 25%, relative to the amount of IL-5 and/or IL-13 in a volume of tissue, or the bodily fluid prior to administration of the one or more masked TGF-β constructs or complexes, or relative to the average value of IL-5 and/or IL-13 in the volume of tissue or the bodily fluid from the matched control group that did not receive the one or more masked TGF-β constructs or complexes. 167. A method of supporting the development and/or survival of invariant natural killer T (iNKT) cells in a mammalian (e.g, a human) subject,or a tissue or bodily fluid thereof, the method comprising administering to the subject one or more masked TGF-β constructs or complexes according to any of aspects 1-134. 168. The method of aspect 167, where at least one of the one or more masked TGF-β constructs or complexes comprises at least one wt. or variant MOD polypeptide sequence. 169. The method of any of aspects 167-168, wherein the administration leads to an increase in the number of iNKT cells in a volume of tissue or bodily fluid (e.g., blood or lymph) fluid from a subject relative to the number of those cells either: (i) before or absent administration of the one or more masked TGF-β constructs or complexes ; or (ii) relative to the number of iNKT cells in the tissue or bodily fluid of a control treatment group (e.g., the average from a group of individuals) matched with the subject (e.g., one or more of disease state, age, sex, height, weight, and/or smoking habit) but that have not been administered TGF-β or a masked TGF-β construct or complex. 170. The method of aspect 169, wherein the number of iNKT cells increases in a volume of tissue or bodily fluid by at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, or at least 90%) relative to the number of iNKT cells in a volume of the tissue or the bodily fluid prior to ad ministration of the one or more masked TGF-β constructs or complexes, or relative to the average value of the matched control group that did not receive the one or more masked TGF-β constructs or complexes. 171. The method of aspect 169, wherein the number of iNKT cells increases in a volume of tissue or bodily fluid by at least 25 relative to the number of iNKT cells in a volume of the tissue or the bodily fluid prior to ad ministration of the one or more masked TGF-β constructs or complexes, or relative to the average value of the matched control group that did not receive the one or more masked TGF-β constructs or complexes. 172. A method of blocking an increase in the number of CD4+ T cells or reducing the number of CD4+ T cells in a mammalian (e.g, a human) subject or a tissue or bodily fluid thereof, the method comprising administering to the subject one or more masked TGF-β constructs or complexes according to any of aspects 1-134. 173. The method of aspect 172, where at least one of the one or more masked TGF-β constructs or complexes comprises at least one wt. or variant MOD polypeptide sequence in addition to the TGF-β polypeptide sequence. 174. The method of any of aspects 172-173, wherein the administration leads to a decrease in the number of CD4+ T cells in a volume of tissue or bodily fluid (e.g., blood or lymph) fluid from a subject relative to the number of those cells either: (i) before or absent administration of the one or more masked TGF-β constructs or complexes ; or (ii) relative to the number of CD4+ T cells in the tissue or bodily fluid of a control treatment group (e.g., the average from a group of individuals) matched with the subject (e.g., one or more of disease state, age, sex, height, weight, and/or smoking habit) but that have not been administered TGF-β or a masked TGF-β construct or complex. 175. The method of aspect 174, wherein the number of CD4+cells decreases in a volume of tissue or bodily fluid by at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 2-fold, at least 5- fold, at least 10-fold or more) relative to the number of CD4+ cells in a volume of the tissue or the bodily fluid prior to administration of the one or more masked TGF-β constructs or complexes, or relative to the average value of the matched control group that did not receive the one or more masked TGF-β constructs or complexes. 176. The method of aspect 174, wherein the number of CD4+cells decreases in a volume of tissue or bodily fluid by at least 25% relative to the number of CD4+ cells in a volume of the tissue or the bodily fluid prior to administration of the one or more masked TGF-β constructs or complexes, or relative to the average value of the matched control group that did not receive the one or more masked TGF-β constructs or complexes. 177. A method of blocking an increase in the number of CD8+ T cells or reducing the number of CD4+ T cells in a mammalian (e.g, a human) subject or a tissue or bodily fluid thereof, the method comprising administering to the subject one or more masked TGF-β constructs or complexes according to any of aspects 1-134. 178. The method of aspect 172, where at least one of the one or more masked TGF-β constructs or complexes comprises at least one wt. or variant MOD polypeptide sequence in addition to the TGF-β polypeptide sequence. 179. The method of any of aspects 172-173, wherein the administration leads to a decrease in the number of CD8+ T cells in a volume of tissue or bodily fluid (e.g., blood or lymph) fluid from a subject relative to the number of those cells either: (i) before or absent administration of the one or more masked TGF-β constructs or complexes ; or (ii) relative to the number of CD8+ T cells in the tissue or bodily fluid of a control treatment group (e.g., the average from a group of individuals) matched with the subject (e.g., one or more of disease state, age, sex, height, weight, and/or smoking habit) but that have not been administered TGF-β or a masked TGF-β construct or complex. 180. The method of aspect 174, wherein the number of CD8+ cells decreases in a volume of tissue or bodily fluid by at least 5% (e.g., at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 2-fold, at least 5- fold, at least 10-fold or more) relative to the number of CD8+ cells in a volume of the tissue or the bodily fluid prior to administration of the one or more masked TGF-β constructs or complexes, or relative to the average value of the matched control group that did not receive the one or more masked TGF-β constructs or complexes. 181. A method of providing treatment or prophylaxis of a wound, an allergic reaction, a disease or disorder, the method comprising administering to a subject (e.g., a human) in need thereof either (i) one or more independently selected masked TGF-β constructs or complexes according to any of aspects 1- 134, and/or (ii) one more nucleic acids encoding the one or more independently selected masked TGF-β constructs or complexes according to any of aspects 1-134. 182. The method of aspect 181, wherein at least one of the one or more masked TGF-β constructs or complexes comprises at least one (e.g., at least two, or at least three) independently selected wt. or variant IL-2 MOD polypeptide sequences. 183. The method of aspect 182, wherein the independently selected wt. or variant IL-2 MOD polypeptide comprises the IL-2 polypeptide of SEQ ID NO:9 or a variant thereof. 184. The method of aspect 183, wherein the independently selected variant IL-2 MOD polypeptide sequence comprises a sequence having: (i) at least 80% (e.g., at least 85%, at least 90%, at least 95%, at least 98%, or at least 99%, aa sequence identity to at least 80 (e.g., at least 90, 100, 110, 120, 130 or 133) contiguous aas of SEQ ID NO:9; or (ii) at least 80% (e.g., at least 85%, at least 90%, at least 95%, at least 98%, or at least 99%) aa sequence identity to at least 80 (e.g., at least 90, 100, 110, 120, 130 or 133) contiguous aas of any of SEQ ID NOs: 15-27. 185. The method of any one of aspects 182-184, wherein the independently selected variant IL-2 MOD polypeptide sequence comprises a substitution at any one, two, or all three of N88, F42 and/or H16. 186. The method of any one of aspects 182-185, wherein the independently selected variant IL-2 MOD polypeptide sequence comprises a substitution or pair of substitutions selected from the group consisting of: (i)F42A; (ii) F42T; (iii) H16A; (iv) H16T; (v) F42A and H16A; (vi) F42T and H16A; (vii) F42A and H16T; or (viii) F42T and H16T substitutions. 187. The method of any one of aspects 181-186, wherein the masked TGF-β constructs or complexes comprise at least one (e.g., at least two) independently selected wt. or variant PD-L1 polypeptide sequences. 188. The method of aspect 187, wherein the independently selected variant PD-L1 polypeptide sequence comprises a polypeptide sequences having at least 80% (e.g., at least 85%, at least 90%, at least 95%, at least 98%, or at least 99%) aa sequence identity to at least 170 contiguous aa (e.g., at least 180, 190 or 200 contiguous aa) of SEQ ID NO:2. 189. The method of any one of aspects 181-188, wherein at least one of the one or more masked TGF-β polypeptides comprise an independently selected wt. or variant IL-10 polypeptide sequence (e.g., a monomeric isomer such as IL-10M1). 190. The method of aspect 189, wherein the independently selected wt. or variant IL-10 polypeptide sequence comprise a polypeptide sequence with at least 80% (at least 85%, at least 90%, at least 95%, at least 98%, or at least 99%) aa sequence identity to at least 50 contiguous aa (e.g., at least 60, at least 70, at least 80, at least 90, at least 100, at least 110, at least 120, at least 130, at least 140, at least 150, or at least 160) contiguous aa of SEQ ID NOs: 50 or 51 (e.g. which have at least one aa substitution, deletion or insertion when the sequence is a variant IL-10 sequence); and wherein variant IL-10 polypeptide sequence optionally comprises a 5-7 aa insertion between N49 and K50 of SEQ ID NO:51, or at the equivalent location in SEQ ID NOs:49 or 50 (e.g., IL-10M1 GGGSGG inserted into SEQ ID NO:51 between aa 49 and aa 50). 191. The method of any one of aspects 181-190, wherein at least one of the independently selected masked TGF-β constructs or complexes comprise an independently selected wt. or variant FasL polypeptide sequence. 192. The method of aspect 191, wherein the independently selected wt. or variant FasL polypeptide sequence comprise a polypeptide sequence with at least 80% (e.g., at least 85%, at least 90%, at least 95%, at least 98%, or at least 99%) aa sequence identity to at least 50 contiguous aa (e.g., at least 60, at least 70, at least 80, at least 90, at least 100, at least 110, at least 120, at least 140, at least 160, or at least 180 contiguous aa) of SEQ ID NO:144 (e.g., which have at least one aa substitution, deletion or insertion). 193. The method of any one of aspects 181-192, wherein the one or more masked TGF-β constructs or complexes is administered before, concurrently, combined with, or following administration of any one, two or all three of vitamin D (e.g., 1 α,25-dihydroxy vitamin D3), retinoic acid (e.g., all trans retinoic acid), and/or rapamycin. 194. The method of any one of aspects 181-193, wherein the autoimmune disease is selected from the group consisting of: Addison's disease, alopecia areata, ankylosing spondylitis, autoimmune encephalomyelitis, autoimmune hemolytic anemia, autoimmune hepatitis, autoimmune-associated infertility, autoimmune thrombocytopenic purpura, bullous pemphigoid, celiac disease, Crohn's disease, Goodpasture's syndrome, glomerulonephritis (e.g., crescentic glomerulonephritis, proliferative glomerulonephritis), Grave's disease, Hashimoto's thyroiditis, mixed connective tissue disease, multiple sclerosis, myasthenia gravis (MG), pemphigus (e.g., pemphigus vulgaris), pernicious anemia, polymyositis, psoriasis, psoriatic arthritis, rheumatoid arthritis, scleroderma, Sjögren's syndrome, systemic lupus erythematosus (SLE), type 1 diabetes (T1D), vasculitis, and vitiligo. 195. The method of any of aspects 181-193, wherein the autoimmune disease is T1D or celiac disease. 196. The method of any of aspects 181-193, wherein the autoimmune disease is other than T1D or celiac disease. 197. The method of any one of aspects 181-193, wherein the method is a method of treatment or prophylaxis of an allergic reaction. 198. The method of aspect 197 where the allergic reaction is a reaction to a peanut, tree nut, plant pollens, latex, bee venom or wasp venom allergen. 199. The method of any one of aspects 181-190, wherein the method is a method of providing treatment or prophylaxis for a burn or a wound 200. The method of aspect 199, wherein the wound is an abrasion, avulsion, incision, laceration, or puncture of the epidermis or mucosa. 201. The method of aspect 200, wherein the i) one or more independently selected masked TGF-β constructs or complexes according to any of aspects 1-134, and/or (ii) one more nucleic acids encoding the one or more independently selected masked TGF-β constructs or complexes according to any of aspects 1-134, is administered before, during and/or after formation of the wound. 202. The method of any of aspects 199-201, wherein the burn and/or wound occurs during, or is the result of, a surgical or other medical procedure. 203. The method of any of aspects 199-202, wherein one or more independently selected masked TGF-β constructs or complexes is administered to the site of the wound or burn. 204. The method of any of aspects 199-203, wherein administration of a masked TGF-β construct or complex (an effective amount) and/or one or more nucleic acids (e.g., recombinant expression vectors) encoding the masked TGF-β construct or complex speeds wound closure (reduce time until closure), reduce healing time, or to reduce scar formation relative to an untreated subject or wound. 205. The method of aspect 181, wherein at least one of the masked TGF-β constructs or complexes comprises at least one (e.g., at least two, or at least three) independently selected wt. (e.g., SEQ ID NO:29 or SEQ ID NO:31) or variant IL-4 polypeptide sequences. 206. The method of aspect 205, wherein the variant IL-4 polypeptide sequences comprise a polypeptide sequences having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, or at least 99% aa sequence identity to at least 80 contiguous aa (e.g., at least 100, or 110 contiguous aa) of SEQ ID NO:29 or SEQ ID NO:31 (e.g., which have at least one aa substitution, deletion or insertion). 207. The method of any of aspects 205-206, wherein the disease or disorder is a helminth infection. 208. The method of aspect 181, wherein at least one of the masked TGF-β constructs or complexes comprises at least one (e.g., at least two, or at least three) independently selected wt. (e.g., the polypeptide of SEQ ID NO:35) or variant IL-6 polypeptide sequences. 209. The method of aspect 208, wherein the variant IL-6 polypeptide sequences comprise a polypeptide sequences having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, or at least 99% aa sequence identity to at least 80 contiguous aa (e.g., at least 100, or 110 contiguous aa) of SEQ ID NO:35 (e.g., which has at least one aa substitution, deletion or insertion). 210. The method of any of aspects 204-209, wherein the disease or disorder is a bacterial and/or fungal infection (e.g., in the gut). 211. The method of aspect 181, wherein at least one of the masked TGF-β constructs or complexes comprises at least one (e.g., at least two, or at least three) independently selected wt. or variant IL-21 and/or IL-23 polypeptide sequences. 212. The method of aspect 209, wherein the at least one (e.g., at least two) IL-21 MOD polypeptide sequence comprises (i) a polypeptide of sequence of SEQ ID NO:58 or 60) or (ii) a polypeptide sequence having at least 80% (e.g., at least 85%, at least 90%, at least 95%, at least 98%, or at least 99%) aa sequence identity to at least 50 (e.g., at least 60, at least 70, at least 80, at least 90, at least 100, or at least 110) contiguous aa of SEQ ID NO:58 or 60, and which have at least one aa substitution, deletion or insertion. 213. The method of aspect 211 or 212, wherein the at least one (e.g., at least two) IL-23 MOD polypeptide sequence comprises (i) a polypeptide of sequence of SEQ ID NO:63 or 65) or (ii) a polypeptide sequence having at least 80% (e.g., at least 85%, at least 90%, at least 95%, at least 98%, or at least 99%) aa sequence identity to at least 50 (e.g., at least 60, at least 70, at least 80, at least 90, at least 100, at least 110, at least 120, at least 140, at least 160, at least 180, at least 200, at least 220, at least 240, at least 260, at least 280, at least 300, at least 320, or at least 340) contiguous aas of SEQ ID NO:63 and/or 65, and which have at least one aa substitution, deletion or insertion. 214. The method of any of aspects 211-213, wherein the disease or disorder is an inability to produce high affinity antibodies or sufficient amounts of high affinity antibodies. 215. A method of inducing tolerance a mammalian subject, the method comprising administering to the subject: (i) one or more masked TGF-β constructs or complexes, or one or more nucleic acids (e.g., expression vector(s)) encoding a masked TGF-β construct or complex according to any of aspects 1-136, (ii) one or more masked TGF-β constructs or complexes, or one or more nucleic acids (e.g., expression vector(s)) encoding a masked TGF-β construct or complex according to any of aspects 1-136, wherein at least one of the one or more masked TGF-β constructs or complexes comprises an wt. or variant IL-2 polypeptide sequence; (iii) one or more masked TGF-β constructs or complexes, or one or more nucleic acids (e.g., expression vector(s)) encoding a masked TGF-β construct or complex according to any of aspects 1-136, wherein at least one of the one or more masked TGF-β constructs or complexes comprises an wt. or variant FasL polypeptide sequence; or (iv) one or more masked TGF-β constructs or complexes, or one or more nucleic acids (e.g., expression vector(s)) encoding a masked TGF-β construct or complex according to any of aspects 1-136, wherein at least one of the one or more masked TGF-β constructs or complexes comprises an wt. or variant IL-2 polypeptide sequence, and wherein at least one of the one or more masked TGF-β constructs or complexes comprises an wt. or variant FasL polypeptide sequence or a wt. or variant IL-10 polypeptide sequence. 216. The method of any of aspects 137-215, further comprising administering a non-steroidal anti- inflammatory drug (NSAID) (e.g., Cox-1 and/or Cox-2 inhibitors such as Celecoxib, Diclofenac, Diflunisal, Etodolac, Ibuprofen, Indomethacin, Ketoprofen, and Naproxen) before, during (concurrent or combined administration) or after administering the one or more masked TGF-β constructs or complexes. 217. The method of any of aspects 137-216, further comprising administering a Corticosteroid (e.g., Cortisone, Dexamethasone, Hydrocortisone, Ethamethasoneb, Fludrocortisone, Methylprednisolone, Prednisone, Prednisolone and Triamcinolone) before, during (concurrent or combined administration) or after administering the one or more masked TGF-β constructs or complexes. 218. The method of any of aspects 137-217, further comprising administering an agent that blocks one or more actions of tumor necrosis factor alpha (e.g., an anti-TNF alpha such as golimumab, infliximab, certolizumab, adalimumab or a TNF alpha decoy receptor such as etanercept) before, during (concurrent or combined administration) or after administering the one or more masked TGF-β constructs or complexes. 219. The method of any of aspects 137-218, further comprising administering an agent that binds to the IL-1 receptor competitively with IL-1 (e.g., anakinra) before, during (concurrent or combined administration) or after administering the one or more masked TGF-β constructs or complexes. This aspect can be subject to the proviso that an agent that binds to the IL-1 receptor competitively with IL-1 is not administered if any of the one or more masked TGF-β constructs or complexes administered to the subject comprises an IL-1 polypeptide. 220. The method of any of aspects 137-219, further comprising administering an agent that binds to the IL-6 receptor and inhibits IL-6 from signaling through the receptor (e.g., tocilizumab) before, during (concurrent or combined administration) or after administering the one or more masked TGF-β constructs or complexes. This aspect can be subject to the proviso that an agent that binds to the IL-6 receptor is not administered if any of the one or more masked TGF-β constructs or complexes administered to the subject comprises an IL-6 polypeptide. 221. The method of any of aspects 137-220, further comprising administering an agent that binds to CD80 or CD86 receptors and inhibits T cell proliferation and/or B cell immune response (e.g., abatacept) before, during (concurrent or combined administration) or after administering the one or more masked TGF-β constructs or complexes. 222. The method of any of aspects 137-221, further comprising administering an agent that binds to CD20 resulting in B-Cell death (e.g., rituximab) before, during (concurrent or combined administration) or after administering the one or more masked TGF-β constructs or complexes. 223. The method of any of aspects 137-222, wherein the mammalian subject is selected from: human, bovine canine, feline, rodent, murine, caprine, simian, ovine, equine, lappine, porcine, etc. subjects. 224. The method of any of aspects 137-223, wherein the subject is a human (e.g., a human patient or a human subject in need of treatment or prophylaxis). 225. A method of delivering a TGF-β polypeptide or a TGF-β polypeptide and an immunomodulatory polypeptide (MOD) to a cell, comprising contacting the cell with (i) a one or more masked TGF-β constructs or complexes of any one of aspects 1-134, (ii) one or more masked TGF-β constructs or complexes comprising one or more independently selected wt. or variant MOD sequences of any one of aspects 1-134, or (iii) one or more nucleic acids encoding one or more masked TGF-β constructs or complexes of any one of aspects 135-136 optionally encoding one or more independently selected wt. or variant MODs. 226. A method of producing cells expressing a masked TGF-β construct or complex, the method comprising introducing one or more nucleic acids (e.g., expression vector(s)) encoding a masked TGF-β construct or complex of any of aspects 1-134 into the cells (e.g., a mammalian cell in vitro), and optionally selecting for cells comprising all or part of the one or more nucleic acids unintegrated and/or integrated into at least one cellular chromosome (e.g., antibiotic selection followed by analysis to determine if any of the one or more nucleic acids had integrated into a cell chromosome). 227. The method of aspect 224, wherein the cell is a cell of a mammalian cell line selected from the HeLa cells, CHO cells, 293 cells, Vero cells, NIH 3T3 cells, Huh-7 cells, BHK cells, PC12, COS cells, COS-7 cells, RAT1 cells, mouse L cells, human embryonic kidney (HEK) cells, and HLHepG2 cells. 228. A cell transiently or stably expressing a masked TGF-β construct or complex prepared by the method of aspect 226 or 227. 229. The cell of aspect 228, wherein cells express from about 25 to about 350 mg/liter or more (e.g., from about 25 to about 100, from about 100 to about 200, from about 200 to about 300, from about 300 to about 350 mg/liter, or greater than 350 mg/liter) of masked TGF-β construct or complex without substantial reduction (less than a 5%, 10%, or 15% reduction) in viability relative to otherwise identical cells not expressing the masked TGF-β construct or complex. 230. The method of any of aspects 138-142, wherein the administering of the masked TGF-β constructs or complexes comprising a wt. or variant IL-2 MOD polypeptide sequence results in modulation of one or more T cells (e.g., inflammatory T cell such as Th1, Th2, Th17 and/or Th22 cells) in the subject, cell, tissue, or bodily fluid. 231. The method of aspect 230, wherein the one or more T cells are Th1 cells and modulation is assessed by a reduction in the number of Th1 cells, a reduction in the expression or secretion of interferon γ by the Th1 cells, or the level of interferon γ in the subject, cell, tissue, or bodily fluid: (i) before or absent administration of the one or more masked TGF-β constructs or complexes; or (ii) relative to the amount of interferon γ in the subject, cell, tissue, or bodily fluid of a treatment group (e.g., one subject or an average from two or more subjects) that are matched with the subject (e.g., one or more of disease state, age, sex, height, weight, and/or smoking habit) but that have not been administered TGF-β or a masked TGF-β construct or complex. 232. The method of aspect 230, wherein the one or more T cells are Th2 cells, and modulation is assessed by a reduction in the number of Th2 cells, a reduction in the expression or secretion of IL-4, IL-5, and/or IL-13 by the Th2 cells, or the level of L-4, IL-5, and/or IL-13 in the subject, cell, tissue, or bodily fluid: (i) before or absent administration of the one or more masked TGF-β constructs or complexes; or (ii) relative to the amount of L-4, IL-5, and/or IL-13 in the subject, cell, tissue, or bodily fluid of a treatment group (e.g., one subject or an average from two or more subjects) that are matched with the subject (e.g., one or more of disease state, age, sex, height, weight, and/or smoking habit) but that have not been administered TGF-β or a masked TGF-β construct or complex. 233. The method of aspect 230, wherein the one or more T cells are Th17, cell and modulation is assessed by a reduction in the number of Th17 cells, a reduction in the expression or secretion of IL-17 and/or IL-22 by the Th17 cells, or the level of IL-17 and/or IL-22 in the subject, cell, tissue, or bodily fluid: (i) before or absent administration of the one or more masked TGF-β constructs or complexes; or (ii) relative to the amount of IL-17 and/or IL-22 in the subject, cell, tissue, or bodily fluid of a treatment group (e.g., one subject or an average from two or more subjects) that are matched with the subject (e.g., one or more of disease state, age, sex, height, weight, and/or smoking habit) but that have not been administered TGF-β or a masked TGF-β construct or complex. 234. The method of aspect 230, wherein the one or more T cells are Th22, cell and modulation is assessed by a reduction in the number of Th22 cells, a reduction in the expression or secretion of at least two or IL-22, IL-13 and/or TNF-alpha by the Th22 cells, or the level of IL-22, IL-13 and/or TNF-alpha in the subject, cell, tissue, or bodily fluid: (i) before or absent administration of the one or more masked TGF-β constructs or complexes; or (ii) relative to the amount of IL-22, IL-13, and TNF-alpha in the subject, cell, tissue, or bodily fluid of a treatment group (e.g., one subject or an average from two or more subjects) that are matched with the subject (e.g., one or more of disease state, age, sex, height, weight, and/or smoking habit) but that have not been administered TGF-β or a masked TGF-β construct or complex. 235. The method of aspect 234, wherein the method further comprises assessing the expressession, secretion of one or more of IL-4, IL-17 and/or interferon γ, or the levels one or more of IL-4, IL-17 and/or interferon γ in the subject, cell, tissue, or bodily fluid. 236. The method of any of aspects 230-235, wherein the T cells are bystander T cells. 237. The method of any of aspects 230-236, wherein the one or more masked TGF-β constructs or complexes is administered before, during (concurrent or combined administration) or after administration of any one or more of vitamin D (e.g., 1α, 25-dihydroxy vitamin D3 or a vitamin D analog (e.g., vitamin D3), an mTOR inhibitor (e.g., rapamycin), and/or a retinoic acid (e.g., all trans retinoic acid). 238. The method of any of aspects 230-237 wherein the masked masked TGF-β constructs or complexes comprising a wt. or variant IL-2 MOD has a structure set forth in FIG, 1 structures A to F. 239, The method of aspect 238, wherein the Fc region lacks immunoglobulin effector sequences (reduced complement component 1q (“C1q”) binding compared to the wt. protein, and accordingly a reduction in the ability to participate in complement-dependent cytotoxicity). VI. Examples [00458] The following examples are put forth so as to provide those of ordinary skill in the art with a more complete disclosure and description of how to make and use the present invention, and are not intended to limit the scope of what the inventors regard as their invention nor are they intended to represent that the experiments below are all or the only experiments performed. Efforts have been made to ensure accuracy with respect to numbers used (e.g. amounts, temperature, etc.) but some experimental errors and deviations should be accounted for. Unless indicated otherwise, parts are parts by weight, molecular weight is weight average molecular weight, temperature is in degrees Celsius, and pressure is at or near atmospheric. Standard abbreviations may be used, e.g., bp, base pair(s); kb, kilobase(s); ); μl, microliter(s); pl, picolitre(s); s or sec, second(s); min, minute(s); h or hr, hour(s); aa, amino acid(s); kb, kilobase(s); bp, base pair(s); nt, nucleotide(s); i.m., intramuscular(ly); i.p., intraperitoneal(ly); s.c., subcutaneous(ly); wt., wild type; and the like. A. Example 1: 1 Single Polypeptide Chain Masked TGF-β Constructs [00459] The stable expression of an intact single polypeptide chain presenting a masked TGF-β protein was demonstrated by preparing a nucleic acid encoding the desired components, and driving expression using an expression vector for a mammalian cell. The nucleic acids encode polypeptides comprising, from N- to C-terminus: a MOD polypeptide sequence (e.g., a wt. IL-2 polypeptide sequence, such as SEQ ID NO:20, or a variant of that IL-2 polypeptide bearing substitutions at H16 and/or F42; an IgG1 Fc scaffold polypeptide sequence bearing L234A and L235A substitutions along with substitutions that prevent Fc dimerization, a type II TGF-β receptor (e.g., a TGF-βRII B isoform polypeptide sequence with D32N and/or D118A sequence variations), and a TGF-β polypeptide sequence (e.g. wt. TGF-β3 or a C77S sequence variant). A schematic having the overall structure of the expressed proteins is shown in FIG. 1 as structure A, one example of which is shown in Fig. 7A as construct 3470 (SEQ ID NO:146), another example of such a polypeptide’s aa sequence is construct No. 3472 aligned with the elements labeled is shown in FIG. 7G as SEQ ID NO:157. After constructing the nucleic acid in a plasmid suitable for mammalian protein expression (e.g., in Chinese Hamster Ovary or CHO cells) the proteins were expressed and purified using protein A and size separation chromatography. [00460] In addition to the construction and isolation of constructs 3470 and 3472 two additional single polypeptide chain masked TGF-β constructs, 3466 and 3468 were prepared. Construct 3470, along with constructs 3472, 3466, and 3468 (numbered as (i) to (iii) below) demonstrate the feasibility of preparing single chain masked TGF-β proteins, that do not substantially dimerize, particularly through classical Fc association. The polypeptides comprise, from N- to C-terminus the following polypeptide sequences: (i) wt. IL-2−IgG Fc−TβRIIΔ25(D32N, D118A) substitutions−TGF-β3 (C77S) (FIG.7G, Construct No.3472) SEQ ID NO:157; (ii) IL-2 (H16T, F42A)−IgG Fc−TβRII Δ25(D118)−TGF-β3 (C77S) (FIG. 7H, Construct No. 3466)SEQ ID NO:158; and (iii) IL-2 (H16T, F42A)−IgG Fc− TβRII Δ25(D32N, D118)− TGF-β3 (C77S) (FIG 7I, Construct No.3468) SEQ ID NO:159. As indicated above, single polypeptide chain masked TGF-β constructs may comprise substitutions that prevent the dimerization of the Fc region, for example at L131 (e.g., L131K), T146 (e.g., T146S), P175 (e.g., P175V), F185 (e.g., F185R), Y187 (e.g., Y187A), and K189 (e.g., K189Y) numbered as in the IgG1 sequence of SEQ ID NO:71. Above-mentioned constructs in (i) to (iii) comprise L131K, T146S, P175V, F185R, Y187A, and K189Y as numbered in the IgG1 sequence of SEQ ID NO:71. 2 Heterodimeric Polypeptide Chain [00461] The stable expression of a masked TGF-β complex comprised of two polypeptides was demonstrated masked TGF-β constructs by preparing a nucleic acid encoding a first polypeptide comprising a TGF-β polypeptide sequence, and a second nucleic acid encoding a TGF-β receptor polypeptide sequence, and expressing the polypeptides using mammalian expression vectors (e.g., plasmid expression systems in CHO cells). The first polypeptide comprising, for example, a MOD polypeptide sequence (e.g., a wt. or variant IL-2 polypeptide sequence), an IgG Fc scaffold polypeptide sequence (e.g., a KiH Fc), and a TGF-β polypeptide sequence (e.g. wt. or sequence variant bearing TGF- β1 or wt. TGF-β3) (see e.g., FIG 7J construct 3618). The second polypeptide comprising, for example, a MOD polypeptide sequence (e.g., a wt. or variant IL-2 polypeptide sequence), an IgG Fc scaffold polypeptide sequence (e.g., the counter part of the KiH sequence of the first polypeptide), and a type II TGF-β receptor (TGF-β RII) polypeptide sequence (wt. or with sequence variations) (see e.g., FIG 7J construct 3621). A schematic structure of the expressed protein is shown in FIG. 1 as structure D. Expression and purification (protein A and size separation by chromatography) of one such pair of polypeptides, (iv.a) and (iv.b), comprising, from N- to C-terminus the following polypeptide sequences: (iv.a) IL-2 (wt. MOD)- knob-in-hole Fc (e.g., knob Fc)-TGF-β3(wt.) see FIG 7J construct 3618 (SEQ ID NO:148); and (iv.b) IL-2 (wt. MOD)- knob-in-hole Fc (e.g., hole Fc)- TβRII (D32N) see FIG 7J construct 3621 (SEQ ID) NO:160. In construct (iv.a) or (iv.b), the IL-2 polypeptide may comprise substitutions at H16 and/or H42, such as H16T and F42A substitutions or H16A and F42A substitutions. 3 Activity of Masked TGF-β Constructs [00462] Various concentrations of the purified masked TGF-β polypeptides complexes and constructs (e.g., constructs (i) to (iii) and the complex of polypeptides (vi.a) and (vi.b) prepared in parts 1 and 2 of this example) were tested for their ability to induce naïve CD4 cells to produce FoxP3. For the assays 10 5 naïve CD4 cells were plated in wells containing 5 μg/ml bound anti-CD3 with 1 μg/ml of anti-CD28 and the masked TGF-β polypeptides complexes or constructs as indicated. After five days in culture the number of FoxP3 CD4+ double positive cells were assessed using fluorescently labeled anti-CD4 and anti-FoxP3 by flow cytometry. Controls poroviding stimulation by either TGF-β3 or TGF-β3 and recombinant human IL-2100 U/ml were also run in parallel. [00463] In FIG.6 at A a comparison of a masked TGF-β construct having the overall structure shown in FIG.1 at A comprising wt. IL-2−IgG Fc (mFc)−TβRII with a D32N substitution −TGF-β3 was tested for FoxP3 expression in comparison to the effect of wt. TGF-β3 in the presence or absence of of IL-2. The results show in FIG. 6 at A indicate that wt. TGF-β3 does not effectively stimulate FoxP3 under the test conditions, but that wt. IL-2 supplementation can lead to FoxP3 expression. [00464] In FIG.6 at B a comparison of a masked TGF-β construct (i), (ii) and (iii) from parts 1 and 2 of this example, and masked TGF-β complex comprising polypeptdes (iv.a) and (iv.b) were tested for FoxP3 expression in comparison to the effect of wt. TGF-β3 in the presence of IL-2. The results show in FIG.6 at B indicate that masked TGF-β constructs and complexs with wt. IL-2 are more potent than those with the IL-2 substitution H16T and F42A. The substitutions at H16T and F42A shift the potency of the masked complexes by an order of magnitude from about 5 nanomolar to about 50 nanomolar without substantive change in the maximal efficacy based on the number of cells expressing FoxP3. As with the results shown in FIG 6 at A, the and masked TGF-β constructs and complexs were more effective at inducing T cells to produce FoxP3 than IL-2 and TGF-β3. [00465] An example of the gating and separation of cells based on CD4+ and FoxP3 is shown in FIG.6 at C. The results demonstrate an induction of FoxP3 in cells exposed to a masked TGF-β construct at 1,000 nM show an increase of approximately 30-fold in FoxP3 expression over cells exposed to 0.1 nM of the same construct. B. Example 2 1 Scaffolds that are non-interspecific [00466] This section describes masked TGF beta sequences that do not employ interspecific scaffolds, and accordingly are either monomeric, or if they dimerize, they not preferentially form heterodimers with a counterpart sequence a. Single Polypeptide Chain Masked TGF-β Constructs [00467] A nucleic acids encoding a polypeptide comprising, from N- to C-terminus, a MOD polypeptide sequence: a wt. IL-2 polypeptide sequence (SEQ ID NO:20), an IgG1 Fc scaffold polypeptide sequence wt. IgG1 aas 11-215 (Δ10) bearing a L234A and L235A (“LALA”), L351K, T366S, P395V, F405R, Y407A, and K409Y substitutions, a TGF-β RII isoform B polypeptide sequence from aa 26 to 136 aas of the mature protein with a D118A substitution (*D119A see the note in FIG 5B), and a human TGF-β type 3 isoform 1 polypeptide sequence with a C77S substitution. A schematic structure of the expressed protein is shown in FIG. 1 as structure A (SEQ ID NO:146). The protein was purified by protein A and size chromatography. b. Homodimeric polypeptide complex [00468] A nucleic acids encoding a polypeptide comprising, from N- to C-terminus, a MOD polypeptide sequence (IL-2 SEQ ID NO:20 with H16T and F42A substitutions), an IgG1 Fc scaffold polypeptide sequence (e.g., wt. IgG1 bearing a L234A and L235A (“LALA”) substitutions), a TGF-β RII isoform B polypeptide sequence from aa 26 to 136 aas of the mature protein with a D118A substitution (*D119A see the note in FIG 5B), and a human TGF-β type 3 isoform 1polypeptide sequence with a C77S substitution. A schematic structure of the expressed protein is shown in FIG. 1 as structure B. The corresponding aa acid sequence aligned with the elements labeled is shown in FIG.7B (SEQ ID NO:147). The protein was purified by protein A and size chromatograph. 2 Heterodimeric masked TGF-β complexes with interspecific scaffolds polypeptides a. Heterodimeric masked TGF-β complexes having interspecific scaffolds each bearing IL-2 MOD polypeptides [00469] The stable expression of a masked TGF-β complex comprised of two polypeptides was demonstrated masked TGF-β constructs by preparing a nucleic acid encoding a first polypeptide comprising a TGF-β polypeptide sequence, and a second nucleic acid encoding a TGF-β receptor polypeptide sequence, and expressing the polypeptides using mammalian expression vectors (e.g., plasmid expression systems in CHO cells). [00470] The first polypeptide comprising, a wt. IL-2 polypeptide (SEQ ID NO:20), an IgG1 Fc scaffold polypeptide sequence (e.g., wt. IgG1 residues 1-225 bearing L234A and L235A (“LALA”) substitutions), and a T366W KiH “knob” substitution, and a human TGF-β type 3 isoform 1polypeptide sequence with a C77S substitution. [00471] The second polypeptide comprising a wt. IL-2 polypeptide (SEQ ID NO:20), an IgG1 Fc scaffold polypeptide sequence (e.g., wt. IgG1 residues 1-225 bearing L234A and L235A (“LALA”) substitutions), and T366S, L368A and Y407V KiH “hole” substitutions, and a TGF-β RII isoform B polypeptide sequence from aa 26 to 136 aas of the mature protein with a D118A substitution. A schematic structure of the expressed protein is shown in FIG. 1 as structure D. The corresponding aa acid sequences are aligned with the elements labeled is shown in FIG.7C. Expression and purification (protein A followed by size exclusion chromatography) provides the heterodimer complex. b. Heterodimeric masked TGF-β complexes having interspecific scaffolds with a single chain bearing an MOD polypeptides [00472] The stable expression of a masked TGF-β complex comprised of two polypeptides was demonstrated masked TGF-β constructs by preparing a nucleic acid encoding a first polypeptide comprising a TGF-β polypeptide sequence, and a second nucleic acid encoding a TGF-β receptor polypeptide sequence, and expressing the polypeptides using mammalian expression vectors (e.g., plasmid expression systems in CHO cells). [00473] The first polypeptide comprising, a wt. IL-2 polypeptide (SEQ ID NO:20), an IgG1 Fc scaffold polypeptide sequence (e.g., wt. IgG1 residues 1-225 bearing L234A and L235A (“LALA”) substitutions, and a T366W (knob) substitution, and a human TGF-β type 3 isoform 1 polypeptide sequence with a C77S substitution. [00474] The second polypeptide comprising an IgG1 Fc scaffold polypeptide sequence (e.g., wt. IgG1 residues 1-225 bearing L234A and L235A (“LALA”) substitutions), and T366S, L368A and Y407V “hole” substitutions, and a TGF-β RII isoform B polypeptide sequence from aa 26 to 136 aas of the mature protein with a D118A substitution. [00475] A schematic structure of the expressed protein is shown in FIG. 1 as structure E. The corresponding aa acid sequence aligned with the elements labeled is shown in FIG. 7 D Expression and purification (protein A followed by size exclusion chromatography) provides the heterodimer complex. c. Heterodimeric masked TGF-β complexes having interspecific scaffold polypeptide stabilization, with a single chain bearing MOD polypeptides [00476] The stable expression of a masked TGF-β complex comprised of two polypeptides was demonstrated masked TGF-β constructs by preparing a nucleic acid encoding a first polypeptide comprising a TGF-β polypeptide sequence, and a second nucleic acid encoding a TGF-β receptor polypeptide sequence, and expressing the polypeptides using mammalian expression vectors (e.g., plasmid expression systems in CHO cells). [00477] The first polypeptide comprising an IL-2 polypeptide sequence (SEQ ID NO 20 with H16T and F42A substitutions), an IgG1 Fc scaffold polypeptide sequence (e.g., wt. IgG1 residues 1-225 bearing L234A and L235A (“LALA”) substitutions), and a T366W (knob) substitution, a TGF-β RII isoform B polypeptide sequence from aa 26 to 136 aas of the mature protein with a D118A substitution, and a human TGF-β type 3 isoform 1 polypeptide sequence with a C77S substitution. [00478] The second polypeptide comprising an IgG1 Fc scaffold polypeptide sequence (e.g., wt. IgG1 residues 1-225 bearing L234A and L235A (“LALA”) substitutions), and T366S, L368A and Y407V “hole” substitutions. [00479] A schematic structure of the expressed protein is shown a variation of the structure in FIG.1 as structure F, but lacking any immunomodulatory polypeptide sequences on the second polypeptide. The corresponding aa acid sequence aligned with the elements labeled is shown in FIG. 7E. Expression and purification (protein A followed by size exclusion chromatography) provides the heterodimer complex. C. Example 3 Expression and purification [00480] Nucleic acids encoding a masked TGF-β construct nucleic acids encoding two masked TGF-β complexes were prepared (see FIG.8). Samples of the complexes were prepared by transfecting ExpiCHO cells with the nucleic acid constructs and permitting the cells to expressing the polypeptides. The polypeptides were purified by protein A chromatography followed by size exclusion chromatography. The purified proteins were subjected to SDS-PAGE and the resulting gels were stained with Coomassie blue. NR = not reducing or unreduced samples, and R = reduced samples (reduction with a disulfide reducing agent). D. Example 4 Biological activity and affinity between the masking polypeptide and TGF-β [00481] A series of masked TGF-β constructs were prepared to demonstrate the biological availability of TGF-β, and that its ability to interact with TβRII is inversely proportional to the affinity of the masking polypeptide for the TGF-β polypeptide sequence. The constructs were of the form structure A in FIG. 1, and, from N-terminus to C-terminus, the MOD is an IL-2 polypeptide; the scaffold is an IgG polypeptide; the masking receptor is a TβRII polypeptide of SEQ ID NO. 119 with N-terminal aas 1-25 (Δ25) deleted and a D118A substitution (and that comprise the additional substitution E55A, D32N, or S52L as indicated), and a TGF-β3 polypeptide sequence. [00482] Interaction of the masked TGF-β constructs with TβRII was assessed using a capture assay in which a TβRII-Ig Fc fusion was captured in the wells of a microtiter plate and various concentrations of the four constructs were applied to the wells. After rinsing off unbound constructs, the bound construct was detected and measured using biotin labeled anti IL-2 followed by streptavidin-horse radish peroxidase and colorimetric detection (3,3’,5,5’-tetramethylbenzidine) at 450 nm. The results, which are shown in FIG. 9, indicate that the Δ25 - D118A construct had the lowest affinity for the TβRII (TβRII-Ig fusion). Addition of an E55A, D32N or S52L, with have increasingly larger impacts of the dissociation constant for TGF-β3−TβRII complexes, provides complexes with increasing affinity for exogenous TβRII (the TβRII-Ig fusion in this case). E. Example 5 Biological activity of heterodimeric masked TGF-β complex (PSM-4033-4039) having interspecific scaffold polypeptide stabilization, with a single chain bearing a variant IL-2 MOD polypeptide [00483] A masked TGF-β complex, PSM-4033-4039, as shown in FIG.10A was prepared. The complex comprises first and second polypeptides 4033 and 4039 shown in FIGS. 10B and 10C, respectively. A series of experiments then was performed with PSM-4033-4039. Experiment 1: Induction of Foxp3 + iTregs from human peripheral naïve CD4 + T cells. [00484] Naïve CD4+ T cells were sorted from human blood and plated with anti-human CD3 (5 ug/mL), anti-human CD28 (1 ug/mL), and an increasing dose of PSM-4033-4039 or a single dose of recombinant TGFb3 and IL-2 as a positive control. After 5 days in culture, cells were assessed by flow cytometry for expression of the transcription factor Foxp3. n = 2, stdev. The results, provided in FIG. 11 show a significant induction of FoxP3 in cells exposed to PSM-4033-4039 at concentrations up to 1,000 nM. These results are similar to those shown in FIG.6B with other masked TGF-β constructs and complexes, further demonstrating that masked TGF-β3 constructs and complexes disclosed herein can effect a significant induction of FoxP3, which is a master regulator of gene expression in Tregs, including both natural and induced Tregs, and central to Treg identity and function. Experiment 2: Suppresion of T cell proliferation by PSM-4033-4039 induced Foxp3 + iTregs. [00485] PSM-4033-4039 induced Foxp3+ T regulatory cells (iTreg) were cultured at different ratios to conventional T cells (Tresponder) and stimulated with anti-human CD3 (1 ug/mL) and mitomycin C treated peripheral blood mononuclear cells (PBMCs). Proliferation was assessed by flow cytometry after four days by the dilution of cell trace violet (CTV) dye in Tresponder cells. The data, shown in FIG. 12, represents an average of three donors, plated in duplicate each. TGF-β3 and IL-2 induced T regulatory cells or total peripheral CD4+ T cells were used in place of iTregs, as controls. Suppression is defined as % less CTV dilution compared to no added iTreg controls (avg. 78% CTV diluted). The results of this experiment demonstrate that Foxp3+ T regulatory cells induced by the masked TGF-β3 constructs and complexes disclosed herein, e.g., PSM-4033-4039, can suppress the proliferation of T cells activated by CD3 cross-linking and co-stimulation, provided by antigen presenting cells in PBMCs. [00486] A defining characteristic of Tregs beyond their expression of the transcription factor, Foxp3, is their ability to suppress the activation and function of other leukocytes. This experiment demonstrates that iTregs induced by masked TGF-β3 constructs and complexes disclosed herein can indeed suppress the proliferation of T cells activated by CD3 cross-linking and co-stimulation, provided by antigen presenting cells in PBMCs. Experiment 3: Induction of Foxp3 + expression from human peripheral CD4 + T cells by PSM- 4033-4039. [00487] Total CD4+ T cells were sorted from human blood and plated with anti-human CD3 (5 ug/mL), anti-human CD28 (1 ug/mL), and an increasing dose of PSM-4033-4039. After 5 days in culture, cells were assessed by flow cytometry for expression of the transcription factor Foxp3. n = 2. The data is illustrated in FIG.13A. [00488] To determine which cell type in a mixture of CD4+ T cell types could differentiate into Foxp3 expressing cells, different populations were sorted and treated with PSM-4033-4039 individually. Accordingly, naïve, total, and memory CD4+ T cells for a different donor than the donors of FIG. 13A were sorted and cultured in the same way as above, with or without PSM-4033-4039 (300 nM), and Foxp3 was assessed by flow cytometry at day 5. The data is illustrated in FIG.13B. [00489] Total CD4+ T cells, which were differentiated into Foxp3 expressing cells in this experiment, represent both naïve and memory peripheral T cells, a mixture of cell types that masked TGF-β3 constructs and complexes disclosed herein, e.g., PSM-4033-4039, would encounter when administered in vivo. This data shows that even in a mixed T cell population, masked TGF-β3 constructs and complexes disclosed herein, e.g., PSM-4033-4039, can increase the frequency of cells that express Foxp3, a master regulator of a gene expression defining T regulatory cells. The results shown in FIG. 13B show that PSM-4033- 4039 can induce memory CD4+ T cells to differentiate into Foxp3+ cells, even if at a lower frequency than naïve CD4+ T cells. Experiment 4: Induction of Foxp3 + iTregs by PSM-4033-4039 from CD4 + T cells activated by an allogeneic lymphocyte reaction. [00490] Total peripheral CD4+ T cells were sorted from human blood and plated with allogeneic monocyte-derived DCs (moDCs) to induce T cell proliferation. T cells were mixed with autologous moDCs as a control, and both allogeneic or autologous donor combinations were treated with soluble anti- CD3 (1 ug/mL) as an additional control. T cells were labeled with cell trace violet (CTV) dye to track cells which responded to allogeneic activation. Proliferation and expression of Foxp3 were analyzed by fl t t d 5 d th f f lif t d ll th t F 3 l tt d i FIGS 14A and B. Two donor combinations are shown. n = 2, stdev. Among other things, the results demonstrate to potential use of the masked TGF-β3 constructs and complexes disclosed herein, e.g., PSM-4033-4039, for the treatment of graft vs. host disease occurring in bone marrow or stem cell transplantation patients. Experiment 5: PK experiment in mice using PSM-4033-4039. [00491] PSM-4033-4039 was administered intravenously as single doses to Balb/c mice at 0.1, 1, or 10 mg/kg. Peripheral serum samples were then collected 5 minutes, 2, 8, 24, and 72 hours post-dose. Serum concentrations of PSM-4033-4039 were then determined using a ligand binding assay that captured the molecule using an anti-IL2 antibody, and detected the molecule using an anti-TGFB3 antibody. The results provided in FIG.15 show that the masked TGF-β3 constructs and complexes disclosed herein, e.g., PSM-4033-4039, can remain present in the serum at biologically relevant concentrations for more than 72 hours after administration. The sequence of construct 4033 is provided in Fig. 10 B (SEQ ID NO:191), and the sequence of construct 4039 is provided in FIG 10C (SEQ ID NO:192). * * * [00492] While the present disclosure has been described with reference to the specific embodiments thereof, it should be understood by those skilled in the art that various changes may be made and equivalents may be substituted without departing from the true spirit and scope of the disclosure. In addition, many modifications may be made to adapt a particular situation, material, composition of matter, process, process step or steps, to the objective, spirit and scope of the present disclosure. All such modifications are intended to be within the scope of the claims appended hereto.
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