ENNAJDAOUI HANANE (US)
JAIN SUVI (US)
RUZO MATIAS ALBERTO (US)
SHAH JAGESH V (US)
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WO2019222403A2 | 2019-11-21 | |||
WO2020014209A1 | 2020-01-16 | |||
WO2020102485A1 | 2020-05-22 | |||
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WO2020102503A2 | 2020-05-22 | |||
WO2013148327A1 | 2013-10-03 | |||
WO2017182585A1 | 2017-10-26 | |||
WO2011058052A1 | 2011-05-19 | |||
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WO1998017815A1 | 1998-04-30 | |||
WO2001079518A2 | 2001-10-25 | |||
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WO1999041397A1 | 1999-08-19 | |||
WO2012156839A2 | 2012-11-22 | |||
WO2018023094A1 | 2018-02-01 | |||
WO2017161010A1 | 2017-09-21 | |||
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WO2017058753A1 | 2017-04-06 | |||
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WO2016126608A1 | 2016-08-11 | |||
WO2013040557A2 | 2013-03-21 | |||
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US20070224176A1 | 2007-09-27 | |||
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CLAIMS 1. A non-cell particle comprising CD24 or a biologically active portion thereof on an exposed surface of the particle, wherein the non-cell particle is 1 µm or smaller. 2. The non-cell particle of claim 1, wherein the CD24 or the biologically active portion thereof binds Siglec-10. 3. The non-cell particle of claim 1 or claim 2, wherein the CD24 or biologically active portion thereof is human. 4. The non-cell particle of any of claims 1-3, wherein the CD24 or biologically active portion thereof: (i) comprises the sequence set forth in SEQ ID NO: 2; (ii) an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:2 that binds Siglec-10; or (iii) a binding portion of (i) or (ii) that binds to Siglec-10. 5. The non-cell particle of any of claims 1-4, wherein the CD24 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:2. 6. The non-cell particle of any of claims 1-5, wherein the CD24 or biologically active portion is displayed on an exposed surface of the particle via a Glycosylphosphatidylinositol (GPI) membrane anchor. 7. The non-cell particle of any of claims 1-6, wherein the CD24 or the biologically active portion thereof is encoded by a nucleic molecule encoding the sequence set forth in SEQ ID NO:3 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:3 that binds Siglec-10. 8. The non-cell particle of any of claims 1-6, wherein the CD24 or the biologically active portion thereof is encoded by a nucleic molecule encoding the sequence set forth in SEQ ID NO:15 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:15 that binds Siglec-10. 9. The non-cell particle of any of claims 1-5, wherein the CD24 or biologically active portion is displayed on an exposed surface of the particle via a transmembrane domain. 10. The non-cell particle of any of claims 1-9, wherein the CD24 or biologically active portion is a glycoprotein 11. The non-cell particle of any of claims 1-10, wherein the CD24 or biologically active portion is sialylated. 12. The non-cell particle of any of claims 1-11, wherein the CD24 or biologically active portion comprises an a2-3-linked sialoside and/or an a2-6-linked sialoside. 13. The non-cell particle of any of claims 1-12, wherein the CD24 or biologically active portion has a molecular weight of between at or about 35 kDa and at or about 45 kDa. 14. The non-cell particle of any of claims 1-13, wherein the non-cell particle further comprises a CD47 or a biologically active portion thereof on an exposed surface of the non-cell particle. 15. The non-cell particle of claim 14, wherein the CD47 or biologically active portion binds to SIRPa. 16. The non-cell particle of claim 14 or claim 15, wherein the CD47 or biologically active portion is human. 17. The non-cell particle of any one of claims 14-16, wherein the CD47 or biologically active portion comprises the extracellular domain or CD47 or a binding portion thereof that binds to SIRPa. 18. The non-cell particle of any of claims 14-17, wherein the CD47 or biologically active portion thereof: (i) comprises the sequence set forth in SEQ ID NO: 7; (ii) an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:7 that binds to SIRPa; or (iii) a binding portion of (i) or (ii) that binds to SIRPa. 19. The non-cell particle of any of claims 14-18, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:7. 20. The non-cell particle of any of claims 14-18, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:11. 21. The non-cell particle of any of claims 14-18 and 20, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:9. 22. The non-cell particle of any of claims 14-18 and 20, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:10. 23. The non-cell particle of any of claims 14-18 and 20, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:12. 24. The non-cell particle of any of claims 14-23, wherein the CD47 or biologically active portion is displayed on an exposed surface of the particle via a transmembrane domain. 25. The non-cell particle of any of claims 14-19 and 24, wherein the CD47 or biologically active portion comprises SEQ ID NO: 8 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% identity to SEQ ID NO:8 that binds to SIRPa. 26. The non-cell particle of any of claims 14-19, 24 and 25, wherein the CD47 or the biologically active portion thereof is encoded by a nucleic molecule encoding the sequence set forth in SEQ ID NO:5 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:5 that binds to SIRPa. 27. The non-cell particle of any of claims 1-26, wherein the non-cell particle is a synthetic particle, a viral particle or a cell-derived particle. 28. The non-cell particle of any of claims 1-27, further comprising a nucleic acid comprising a payload gene encoding an exogenous agent. 29. The non-cell particle of any of claims 1-28, wherein the non-cell particle is a synthetic particle selected from the group consisting of a liposome, a microparticle, a nanoparticle, a nanogel, a dendrimer and a dendrisome. 30. The non-cell particle of any of claims 1-28, wherein the exposed surface is a lipid bilayer and the non-cell particle further comprises a lumen comprising a cytosol, wherein the lumen is surrounded by the lipid bilayer. 31. The non-cell particle of claim 30, wherein the lumen further comprises a nucleic acid comprising a payload gene encoding an exogenous agent. 32. The non-cell particle of claim 30 or claim 31, wherein the non-cell particle is a fusosome and the lipid bilayer further comprises a fusogen. 33. The non-cell particle of any of claims 1-28 and 30-32, wherein the non-cell particle is derived from a source cell. 34. The non-cell particle of any of claims 1-33, wherein the non-cell particle does not comprise a nucleus. 35. The non-cell particle of any of claims 1-28 and 30-32, wherein the non-cell particle is a virus particle or a virus-like particle (VLP). 36. The non-cell particle of claims 35, wherein the virus particle or virus-like particle is a retroviral particle or retrovirus-like particle. 37. The non-cell particle of claim 36, wherein the retroviral particle or retrovirus-like particle is a lentiviral particle or a lentiviral-like particle. 38. The non-cell particle of any of claims 35-37, comprising a fusogen that is a viral fusogen selected from a Class I viral membrane fusion protein, a Class II viral membrane protein, a Class II viral membrane fusion protein, a viral membrane glycoprotein, or a viral envelope protein. 39. The non-cell particle of claim 38, wherein the fusogen is endogenous to the virus. 40. The non-cell particle of claim 38, wherein the fusogen is a pseudotyped fusogen. 41. The non-cell particle of any of claims 32-40, wherein the fusogen is a re-targeted fusogen that binds to a target cell. 42. The non-cell particle of claim 41, wherein the fusogen comprises a targeting moiety that binds to the target cell. 43. The non-cell particle of any of claims 35-42, wherein the virus or virus-like particle further comprising a lumen comprising a nucleic acid. 44. The non-cell particle of claim 43, wherein the nucleic acid comprises a viral nucleic acid comprising one or more of (e.g., all of) the following nucleic acid sequences: 5’ LTR (e.g., comprising U5 and lacking a functional U3 domain), Psi packaging element (Psi), Central polypurine tract (cPPT)/central termination sequence (CTS) (e.g. DNA flap), Poly A tail sequence, a posttranscriptional regulatory element (e.g. WPRE), a Rev response element (RRE), and 3’ LTR (e.g., comprising U5 and lacking a functional U3). 45. The non-cell particle of any of claims 35-44, wherein the non-cell particle is a virus-like particle (e.g. retrovirus-like particle) that is a replication defective. 46. A pseudotyped lentivirus or lentiviral-like particle comprising CD24 or a biologically active portion thereof on an exposed surface of the lentiviral particle. 47. The pseudotyped lentivirus or lentiviral-like particle of claim 46, wherein the particle is pseudotyped with a vesicular stomatitis virus envelope glycoprotein (VSV-G). 48. The pseudotyped lentivirus or lentiviral particle of claim 46, wherein the lentiviral particle is pseudotyped with a protein derived from an envelope glycoprotein of a virus of the Paramyxovirus family. 49. The pseudotyped lentivirus or lentiviral-like particle of claim 46, wherein the particle is pseudotyped with a cell targeting fusion protein comprising a protein derived from a Paramyxoviridae envelope protein G or H or a biologically active portion thereof and at least one cell targeting domain. 50. The pseudotyped lentivirus or lentiviral particle of claim 48 or claim 49, wherein the virus of the Paramyxovirus family is a Henipavirus or is a Morbillivirus. 51. The pseudotyped lentivirus or lentiviral particle of any of claims 48-50, wherein the envelope glycoprotein is an envelope glycoprotein G or H or a biologically active portion thereof. 52. The pseudotyped lentivirus or lentiviral-like particle of any of claims 48-51, wherein the envelope glycoprotein is Nipah virus G (Niv-G) protein or a biologically active portion thereof. 53. The pseudotyped lentivirus or lentiviral-like particle of any of claims 48-51, wherein the envelope glycoprotein is a Hendra virus G protein or a biologically active portion thereof. 54. The pseudotyped lentivirus or lentiviral-like particle of any of claims 48-51, wherein the envelope glycoprotein is a measles virus glycoprotein or a biologically active portion thereof. 55. The pseudotyped lentivirus or lentiviral-like particle of any of claims 48-54, wherein said protein derived from an envelope glycoprotein G or H of a virus of the Paramyxoviridae family is at least partially unable to bind at least one natural receptor of said envelope glycoprotein G or H. 56. The pseudotyped lentivirus or lentiviral-like particle of any of claims 48-55, furtehr comprising an F protein molecule or a biologically active portion thereof from a Paramyxovirus. 57. The pseudotyped lentivirus or lentiviral-like particle of claim 56, wherein the Paramyxovirus is a Henipavirus. 58. The pseudotyped lentivirus or lentiviral-like particle of claim 56 or claim 57, wherein the protein protein molecule or a biologically active portion is a NiV-F protein or a biologically active portion. 59. The pseudotyped lentivirus or lentiviral-like particle of any of claims 46-58, wherein the CD24 or biologically active portion thereof: (i) comprises the sequence set forth in SEQ ID NO: 2; (ii) an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:2 that binds to Siglec-10; or (iii) a binding portion of (i) or (ii) that binds to Siglec-10. 60. The pseudotyped lentivirus or lentiviral-like particle of any of claims 46-59, wherein the CD24 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:2. 61. The pseudotyped lentivirus or lentiviral-like particle of any of claims 46-60, wherein the CD24 or biologically active portion is displayed on an exposed surface of the particle via a Glycosylphosphatidylinositol (GPI) membrane anchor. 62. The pseudotyped lentivirus or lentiviral-like particle of any of claims 46-61, wherein the CD24 or the biologically active portion thereof is encoded by a nucleic molecule encoding the sequence set forth in SEQ ID NO:3 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:3 that binds to Siglec- 10. 63. The pseudotyped lentivirus or lentiviral-like particle of any of claims 46-62, wherein the CD24 or the biologically active portion thereof is encoded by a nucleic molecule encoding the sequence set forth in SEQ ID NO:15 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:15 that binds to Siglec- 10. 64. The pseudotyped lentivirus or lentiviral-like particle of any of claims 46-60, wherein the CD24 or biologically active portion is displayed on an exposed surface of the particle via a transmembrane domain. 65. The pseudotyped lentivirus or lentiviral-like particle of any of claims 46-64, wherein the CD24 or biologically active portion is a glycoprotein 66. The pseudotyped lentivirus or lentiviral-like particle of any of claims 46-65, wherein the CD24 or biologically active portion is sialylated. 67. The pseudotyped lentivirus or lentiviral-like particle of any of claims 46-66, wherein the CD24 or biologically active portion comprises an a2-3-linked sialoside and/or an a2-6-linked sialoside. 68. The pseudotyped lentivirus or lentiviral-like particle of any of claims 46-67, wherein the CD24 or biologically active portion has a molecular weight of between at or about 35 kDa and at or about 45 kDa. 69. The pseudotyped lentivirus or lentiviral-like particle of any of claims 46-68, wherein the non-cell particle further comprises a CD47 or a biologically active portion thereof on an exposed surface of the non-cell particle. 70. The pseudotyped lentivirus or lentiviral-like particle of claim 69, wherein the CD47 or biologically active portion binds to SIRPa. 71. The pseudotyped lentivirus or lentiviral-like particle of claim 69 or claim 70, wherein the CD47 or biologically active portion is human. 72. The pseudotyped lentivirus or lentiviral-like particle of any one of claims 69-71, wherein the CD47 or biologically active portion comprises the extracellular domain or CD47 or a binding portion thereof that binds to SIRPa. 73. The pseudotyped lentivirus or lentiviral-like particle of any of claims 69-72, wherein the CD47 or biologically active portion thereof: (i) comprises the sequence set forth in SEQ ID NO: 7; (ii) an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:7 that binds to SIRPa; or (iii) a binding portion of (i) or (ii) that binds to SIRPa. 74. The pseudotyped lentivirus or lentiviral-like particle of any of claims 69-73, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:7. 75. The pseudotyped lentivirus or lentiviral-like particle of any of claims 69-73, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:11. 76. The pseudotyped lentivirus or lentiviral-like particle of any of claims 69-73 and 75, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:9. 77. The pseudotyped lentivirus or lentiviral-like particle of any of claims 69-73 and 75, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:10. 78. The pseudotyped lentivirus or lentiviral-like particle of any of claims 69-73 and 77, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:12. 79. The pseudotyped lentivirus or lentiviral-like particle of any of claims 69-78, wherein the CD47 or biologically active portion is displayed on an exposed surface of the particle via a transmembrane domain. 80. The pseudotyped lentivirus or lentiviral-like particle of any of claims 69-74 and 79, wherein the CD47 or biologically active portion comprises SEQ ID NO: 8 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% identity to SEQ ID NO:8 that binds to SIRPa. 81. The pseudotyped lentivirus or lentiviral-like particle of any of claims 69-74, 79 and 80, wherein the CD47 or the biologically active portion thereof is encoded by a nucleic molecule encoding the sequence set forth in SEQ ID NO:5 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:5 that binds to SIRPa. 82. The non-cell particle of any of claims 1-45 or the pseudotyped lentivirus or lentiviral-like particle of any of claims 46-81, further comprising a nucleic acid comprising a payload gene encoding an exogenous agent. 83. The non-cell particle of claim 28, claim 31 or claim 82 or the pseudotyped lentivirus or lentiviral-like particle of claim 82, wherein the exogenous agent encodes a therapeutic agent or a diagnostic agent. 84. The non-cell particle of any of claims 1-45, 82 and 83 or the pseudotyped lentivirus or lentiviral-like particle of any of claims 46-83, wherein phagocytosis of the particle by a phagocytic cells, optionally a macrophage, is reduced compared to a reference particle that is otherwise similar but does not comprise the CD24 or biologically active portion, optionally wherein phagocytosis is reduced by at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, or 90%. 85. The non-cell particle of any of claims 1-45 and 82-84 or the pseudotyped lentivirus or lentiviral-like particle of any of claims 46-84, wherein the half-life of the particle in vivo is increased compared to a reference particle that is otherwise similar but does not comprise the CD24 or biologically active portion, optionally wherein the half-life is increased by at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, or 90%. 86. A polynucleotide comprising a first nucleic acid sequence encoding CD24 or a biologically active portion and a second nucleic acid encoding CD47 or a biologically active portion. 87. The polynucleotide of claim 86, wherein the encoded CD24 or the biologically active portion thereof binds Siglec-10. 88. The polynucleotide of claim 86 or claim 87, wherein the encoded CD24 or biologically active portion thereof is human. 89. The polynucleotide of any of claims 84-88, wherein the encoded CD24 or biologically active portion thereof: (i) comprises the sequence set forth in SEQ ID NO: 2; (ii) an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:2 that binds to Siglec-10; or (iii) a binding portion of (i) or (ii) that binds to Siglec-10. 90. The polynucleotide of any of claims 84-89, wherein the encoded CD24 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:2. 91. The polynucleotide of any of claims 84-90, wherein the encoded CD24 or biologically active portion is displayed on an exposed surface of the particle via a Glycosylphosphatidylinositol (GPI) membrane anchor. 92. The polynucleotide of any of claims 84-91, wherein: the first nucleic acid encoding CD24 or a biologically active portion encodes the sequence set forth in SEQ ID NO:3 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:3 that binds to Siglec-10; or the first nucleic acid encoding CD24 or a biologically active portion encodes the sequence set forth in SEQ ID NO:15 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:15 that binds to Siglec-10. 93. The polynucleotide of any of claims 84-92, wherein the first nucleic acid encoding CD24 comprises the sequence set forth in SEQ ID NO:4 or a sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:4; 94. The polynucleotide of any of claims 84-93, wherein the encoded CD47 or biologically active portion binds to SIRPa. 95. The polynucleotide of any of claims 84-94, wherein the encoded CD47 or biologically active portion is human. 96. The polynucleotide of any of claims 84-95, wherein the encoded CD47 or biologically active portion comprises the extracellular domain or CD47 or a binding portion thereof that binds to SIRPa. 97. The polynucleotide of any of claims 84-96, wherein the encoded CD47 or biologically active portion thereof: (i) comprises the sequence set forth in SEQ ID NO: 7; (ii) an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:7 that binds to SIRPa; or (iii) a binding portion of (i) or (ii) that binds to SIRPa. 98. The polynucleotide of any of claims 84-97, wherein the encoded CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:7. 99. The polynucleotide of any of claims 84-97, wherein the encoded CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:11. 100. The polynucleotide of any of claims 84-97 and 99, wherein the encoded CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:9. 101. The polynucleotide of any of claims 84-97 and 99, wherein the encoded CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:10. 102. The polynucleotide of any of claims 84-97 and 99, wherein the encoded CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:12. 103. The polynucleotide of any of claims 84-102, wherein the encoded CD47 or biologically active portion comprises a transmembrane domain. 104. The polynucleotide of any of claims 84-103, wherein: the second nucleic acid encodes the sequence set forth in SEQ ID NO: 5 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% identity to SEQ ID NO:5 that binds to SIRPa; or the second nucleic acid encodes the sequence set forth in SEQ ID NO: 8 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% identity to SEQ ID NO:8 that binds to SIRPa. 105. The polynucleotide of any of claims 84-104, wherein the second nucleic acid encoding CD47 comprises the sequence set forth in SEQ ID NO:13 or a sequence having at least at or about 90%, at least at or about 91%, at or about 92%, at least at or about 93%, at least at or about 94%, at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% identity to SEQ ID NO:13. 106. The polynucleotide of any of claims 84-105, further comprising at least one promoter that is operatively linked to control expression of the CD24 or biologically active portion and/or the CD47 or biologically active portion. 107. The polynucleotide of any of claims 84-106, wherein the first and second nucleic acid are operatively linked to the same promoter. 108. The polynucleotide of any of claims 84-106, wherein the first nucleic acid is operatively linked to a first promoter and the second nucleic acid is operatively linked to a second promoter. 109. The polynucleotide of claim 108, wherein the first and second promoter are different. 110. The polynucleotide of any of claims 106-109, wherein the promoter, or each promoter individually, is a heterologous promoter. 111. The polynucleotide of any of claims 106-110, wherein the promoter, or each promoter individually, is an inducible promoter. 112. The polynucleotide of any of claims 84-111, further comprising a nucleic acid sequence encoding a linking peptide between the first and second nucleic acid sequences, wherein the linking peptide separates the translation products of the first and second nucleic acid sequences during or after translation. 113. The polynucleotide of claim 112, wherein the linking peptide comprises an internal ribosome entry site (IRES), a self-cleaving peptide, or a peptide that causes ribosome skipping, optionally a T2A peptide. 114. A vector, comprising the polynucleotide of any of claims 84-112. 115. The vector of claim 114, wherein the vector is a mammalian vector, viral vector or artificial chromosome, optionally wherein the artificial chromosome is a bacterial artificial chromosome (BAC). 116. A method of making a non-cell particle comprising CD24 or a biologically active portion, comprising: a) providing a cell that comprises a nucleic acid encoding CD24 or a biologically active portion thereof; b) culturing the cell under conditions that allow for production of a non-cell particle, and c) separating, enriching, or purifying the particle from the cell, thereby making the fusosome. 117. The method of claim 116, wherein the cell further comprises a nucleic acid encoding CD47 or a biologically active portion thereof or the nucleic acid further encodes CD47 or a biologically active portion thereof. 118. A method of making a non-cell particle comprising CD24 or a biologically active portion, comprising: a) providing a cell that comprises the polynucleotide of any of claims 84-112 or the vector of claim 114 or claim 115; b) culturing the cell under conditions that allow for production of a non-cell particle, and c) separating, enriching, or purifying the non-cell particle from the cell, thereby making the fusosome. 119. The method of any of claims 116-118, wherein the cell is a mammalian cell and the non-cell particle is a vesicle or an exosome, optionally wherein the vesicle is a microvesicle or a nanovesicle. 120. The method of any of claims 116-118, wherein the cell is a producer cell and the non-cell particle is a viral particle or a viral-like particle, optionally a retroviral particle or a retroviral-like particle, optionally a lentiviral particle or lentiviral-like particle. 121. The method of any of claims 116-120, wherein the cell further comprises an exogenous nucleic acid sequence encoding an exogenous agent. 122. The method of any of claims 116-121, wherein the cell further comprises a fusogen. 123. A non-cell particle made by the method of any of claims 116-122. 124. A mammalian cell comprising (i) a viral nucleic acid(s) and (ii) nucleic acid encoding an exogenous CD24 or a biologically active portion thereof, optionally wherein the viral nucleic acid(s) are lentiviral nucleic acids. 125. The mammalian cell of claim 124, wherein the viral nucleic acid(s) lacks one or more genes involved in viral replication. 126. The mammalian cell of claim 124 or claim 125, wherein the viral nucleic acid comprises: one or more of (e.g., all of) the following nucleic acid sequences: 5’ LTR (e.g., comprising U5 and lacking a functional U3 domain), Psi packaging element (Psi), Central polypurine tract (cPPT)/central termination sequence (CTS) (e.g. DNA flap), Poly A tail sequence, a posttranscriptional regulatory element (e.g. WPRE), a Rev response element (RRE), and 3’ LTR (e.g., comprising U5 and lacking a functional U3); a nucleic acid encoding a viral envelope protein; and/or a nucleic acid encoding a viral packaging protein selected from one or more of Gag, Pol, Rev and Tat. 127. The mammalian cell of any of claims 124-126, wherein the the exogenous CD24 or biologically active portion comprises: (i) the sequence set forth in SEQ ID NO: 2; (ii) an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:2 that binds Siglec-10; or (iii) a binding portion of (i) or (ii) that binds to Siglec-10. 128. The mammalian cell of claim 127, wherein the nucleic acid encoding exogenous CD24 further encodes a a Glycosylphosphatidylinositol (GPI) membrane anchor signal sequence or a transmembrane domain. 129. The mammalian cell of any of claims 124-128, wherein the cell further comprises a nucleic acid encoding exogenous CD47 or a biologically active portion. 130. The mammalian cell of claim 129, wherein the exogenous CD47 or biologically active portion comprises: (i) the sequence set forth in SEQ ID NO: 7; (ii) an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:7 that binds to SIRPa; or (iii) a binding portion of (i) or (ii) that binds to SIRPa. 131. The mammalian cell of claim 130, wherein the nucleic acid encoding exogenous CD47 further encodes a Glycosylphosphatidylinositol (GPI) membrane anchor signal sequence or a transmembrane domain. 132. The mammalian cell of any of claims 124-131, wherein the nucleic acid encoding the exogenous CD24 or biologically active portion and the nucleic acid encoding the exogenous CD47 or biologically active portion are encoded by the polynucleotide of any of claims 84-112. 133. A viral vector particle or viral-like particle produced from the mammalian cell of any of claims 124-132. 134. A composition comprising a plurality of non-cell particles of any of claims 1-45. 135. A composition comprising a plurality of pseudotyped lentivirus or lentiviral-like particles of any of claims 46-81. 136. The composition of claim 134 or claim 135 further comprising a pharmaceutically acceptable carrier. 137. The pharmaceutical composition of any of claims 134-136, wherein the plurality of particles comprise an average diameter of less than 1 µm. 138. A method of delivering an exogenous agent to a subject (e.g., a human subject) , the method comprising administering to the subject the non-cell particle of any of claims 1-45 or the pseudotyped lentivirus or lentiviral-like particles of any of claims 46-81 or the composition of any of claims 134-137. 139. A method of treating a disease or disorder in a subject (e.g., a human subject), the method comprising administering to the subject a non-cell particle of any of claims 1-45 or the pseudotyped lentivirus or lentiviral-like particles of any of claims 46-81 or the composition of any of claims 134-137. 140. A method of evading phagocytosis of a particle by a phagocytic cell, the method comprising contacting a phagocytic cell with a non-cell particle of any of claims 1-45 or the pseudotyped lentivirus or lentiviral-like particles of any of claims 46-81 or the composition of any of claims 134-137, whereby said particles evades phacocytosis by said phagocytic cell. 141. A method of increasing the life of a particle in vivo in a mammal, method comprising administering the non-cell particle of any of claims 1-45 or the pseudotyped lentivirus or lentiviral-like particles of any of claims 46-81 or the composition of any of claims 134-137 to a mammalian subject wherein said administered particles have a longer half-life in said mammal than an otherwise similar particle that does not have CD24 expressed thereon. 142. The non-cell particle of any of claims 1-27, 29, 30, and 32-45, further comprising an exogenous agent. 143. The non-cell particle of any of claims 28, 31, 82, 83, and 142, wherein the exogenous agent comprises a protein. 144. The non-cell particle of any of claims 28, 31, 82, 83, 142, and 143, wherein the exogenous agent comprises a membrane protein. 145. The non-cell particle of any of claims 28, 31, 82, 83, and 142-144, wherein the exogenous agent comprises a chimeric antigen receptor (CAR), a T cell receptor, an integrin, an ion channel, a pore forming protein, a Toll-Like Receptor, an interleukin receptor, a cell adhesion protein, or a transport protein. 146. The non-cell particle of any of claims 28, 31, 82, 83, and 142-145, wherein the exogenous agent comprises a CAR comprising an antigen binding domain, a transmembrane domain, and one or more signaling domains. 147. The non-cell particle of claim 146, wherein the antigen binding domain binds to a surface antigen characteristic of a cell type or a disorder. 148. The non-cell particle of claim 146 or 147, wherein the antigen binding domain binds to a surface antigen characteristic of a neoplastic cell, a T cell, an autoimmune or inflammatory disorder, a senescent cell, or an infectious disease. 149. A method of delivering an exogenous agent to a subject (e.g., a human subject), the method comprising administering to a subject the non-cell particle of any of claims 28, 31, 82, 83, and 142-148, wherein the payload gene encoding the exogenous agent or the exogenous agent is delivered to a target cell. 150. The method of claim 149, wherein the exogenous agent is a CAR. 151. The method of claim 149 or claim 150, wherein the target cell is a T cell. 152. The method of any of claims 149-151, wherein the target cell is any of a CD4+ T cell, a CD8+ T cell, an alpha beta T cell, a gamma delta T cell, a naive T cell, an effector T cell, a cytotoxic T cell (e.g., a CD8+ cytotoxic T cell), a regulatory T cell (e.g., a thymus-derived regulatory T cell, a peripherally derived regulatory T cell, a CD4+Foxp3+ regulatory T cell, or a CD4+FoxP3- type 1 regulatory T (Trl) cell), a helper T cell (e.g., a CD4+ helper T cell, a Thl cell, a Th2 cell, a Th3 cell, a Th9 cell, a Thl7 cell, a Th22 cell, or a T follicular helper (Tfh) cell), a memory T cell (e.g., a stem cell memory T cell, a central memory T cell, or an effector memory T cell), a NKT cell, and a Mucosal associated invariant T (MAIT) cell. |
[0357] In some embodiments, the G protein has a sequence set forth in any of SEQ ID NOS: 19-29 or is a functionally active variant or biologically active portion thereof that has a sequence that is at least at or about 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at least at or about 84%, at least at or about 85%, at least at or about 86%, at least at or about 87%, at least at or about 88%, at least at or about 89%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% identical to any one of SEQ ID NOS: 19, 20, 21, 22, 23, 24, 25, 26, 27, 28 or 29. [0358] In particular embodiments, the G protein or functionally active variant or biologically active portion is a protein that retains fusogenic activity in conjunction with a Henipavirus F protein, e.g. NiV-F or HeV-F. Fusogenic activity includes the activity of the G protein in conjunction with a Henipavirus F protein to promote or facilitate fusion of two membrane lumens, such as the lumen of the targeted lipid particle having embedded in its lipid bilayer a henipavirus F and G protein, and a cytoplasm of a target cell, e.g. a cell that contains a surface receptor or molecule that is recognized or bound by the targeted envelope protein. In some embodiments, the F protein and G protein are from the same Henipavirus species (e.g. NiV-G and NiV-F). In some embodiments, the F protein and G protein are from different Henipavirus species (e.g. NiV-G and HeV-F). [0359] In particular embodiments, the G protein has the sequence of amino acids set forth in SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28 or SEQ ID NO: 29 or is a functionally active variant thereof or a biologically active portion thereof that retains fusogenic activity. In some embodiments, the functionally active variant comprises an amino acid sequence having at least at or about 80%, at least at or about 85%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28 or SEQ ID NO: 29 and retains fusogenic activity in conjunction with a Henipavirus F protein (e.g., NiV-F or HeV-F). In some embodiments, the biologically active portion has an amino acid sequence having at least at or about 80%, at least at or about 85%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28 or SEQ ID NO: 29 and retains fusogenic activity in conjunction with a Henipavirus F protein (e.g., NiV-F or HeV-F). [0360] Reference to retaining fusogenic activity includes activity (in conjunction with a Henipavirus F protein) that is between at or about 10% and at or about 150% or more of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28 or SEQ ID NO: 29 such as at least or at least about 10% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 15% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 20% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 25% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 30% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 35% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 40% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 45% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 50% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 55% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 60% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 65% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 70% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 75% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 80% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 85% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 90% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 95% of the level or degree of fusogenic activity of the corresponding wild-type G protein, such as at least or at least about 100% of the level or degree of fusogenic activity of the corresponding wild-type G protein, or such as at least or at least about 120% of the level or degree of fusogenic activity of the corresponding wild-type G protein. [0361] In some embodiments the G protein is a mutant G protein that is a functionally active variant or biologically active portion containing one or more amino acid mutations, such as one or more amino acid insertions, deletions, substitutions or truncations. In some embodiments, the mutations described herein relate to amino acid insertions, deletions, substitutions or truncations of amino acids compared to a reference G protein sequence. In some embodiments, the reference G protein sequence is the wild-type sequence of a G protein or a biologically active portion thereof. In some embodiments, the functionally active variant or the biologically active portion thereof is a mutant of a wild-type Hendra (HeV) virus G protein, a wild-type Nipah (NiV) virus G-protein (NiV-G), a wild-type Cedar (CedPV) virus G-protein, a wild-type Mojiang virus G- protein, a wild-type bat Paramyxovirus G-protein or biologically active portion thereof. In some embodiments, the wild-type G protein has the sequence set forth in any one of SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28 or SEQ ID NO: 29. [0362] In some embodiments, the G protein is a mutant G protein that is a biologically active portion that is an N-terminally and/or C-terminally truncated fragment of a wild-type Hendra (HeV) virus G protein, a wild-type Nipah (NiV) virus G-protein (NiV-G), a wild-type Cedar (CedPV) virus G-protein, a wild-type Mojiang virus G-protein, a wild-type bat Paramyxovirus G-protein. In particular embodiments, the truncation is an N-terminal truncation of all or a portion of the cytoplasmic domain. In some embodiments, the mutant G protein is a biologically active portion that is truncated and lacks up to 49 contiguous amino acid residues at or near the N-terminus of the wild-type G protein, such as a wild-type G protein set forth in any one of SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28 or SEQ ID NO: 29. In some embodiments, the mutant F protein is truncated and lacks up to 49 contiguous amino acids, such as up to 49, 48, 47, 46, 45, 44, 43, 42, 41, 40, 30, 38, 37, 36, 35, 34, 33, 32, 31, 30, 29, 28, 27, 26, 25, 24, 23, 22, 21, 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2 or 1 contiguous amino acids at the N-terminus of the wild-type G protein. [0363] In some embodiments, the G protein is a wild-type Nipah virus G (NiV-G) protein or a Hendra virus G protein, or is a functionally active variant or biologically active portion thereof.In some embodiments, the G protein is a NiV-G protein that has the sequence set forth in SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23, or is a functional variant or a biologically active portion thereof that has an amino acid sequence having at least at or about 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at least at or about 84%, at least at or about 85%, at least at or about 86%, at least at or about 87%, at least at or about 88%, at least at or about 89%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, at least at or about 99% sequence identity to SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23. [0364] In some embodiments, the G protein is a mutant NiV-G protein that is a biologically active portion of a wild-type NiV-G. In some embodiments, the biologically active portion is an N-terminally truncated fragment. In some embodiments, the mutant NiV-G protein is truncated and lacks up to 5 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 6 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 7 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 8 contiguous amino acid residues at or near the N- terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 9 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23) up to 10 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 11 contiguous amino acid residues at or near the N- terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 12 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein SEQ ID NO:23, SEQ ID NO:19, or SEQ ID NO:22), up to 13 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 14 contiguous amino acid residues at or near the N- terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 15 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23) up to 16 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 17 contiguous amino acid residues at or near the N- terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 18 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 19 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 20 contiguous amino acid residues at or near the N- terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 21 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 22 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 23 contiguous amino acid residues at or near the N- terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 24 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 25 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 26 contiguous amino acid residues at or near the N- terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 27 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 28 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 29 contiguous amino acid residues at or near the N- terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 30 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 31 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 32 contiguous amino acid residues at or near the N- terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 33 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 34 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 35 contiguous amino acid residues at or near the N- terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 36 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 37 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23) up to 38 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 39 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 40 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 41 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 42 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 43 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), up to 44 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23), or up to 45 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:19, SEQ ID NO:22 or SEQ ID NO:23). [0365] In some embodiments, the NiV-G protein is a biologically active portion that does not contain a cytoplasmic domain. In some embodiments, the NiV-G protein without the cytoplasmic domain is encoded by SEQ ID NO: 40. [0366] In some embodiments, the mutant NiV-G protein comprises a sequence set forth in any of SEQ ID NOS: 30-40, or is a functional variant thereof that has an amino acid sequence having at least at or 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at or about 84%, at least at or about 85%, at least at or about 86%, or at least at or about 87%, at least at or about 88%, or at least at or about 89%, about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NOS: 30-40. [0367] In some embodiments, the mutant NiV-G protein has a 5 amino acid truncation at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:30, SEQ ID NO: 31 or SEQ ID NO:32), such as set forth in SEQ ID NO: 33 or a functional variant thereof having at least at or about 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at or about 84%, at least at or about 85%, at least at or about 86%, or at least at or about 87%, at least at or about 88%, or at least at or about 89%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:33 or such as set forth in SEQ ID NO: 34 or a functional variant thereof having at least at or about 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at or about 84%, at least at or about 85%, at least at or about 86%, or at least at or about 87%, at least at or about 88%, or at least at or about 89%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:34 or such as set forth in SEQ ID NO: 35 or a functional variant thereof having at least at or about 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at or about 84%, at least at or about 85%, at least at or about 86%, or at least at or about 87%, at least at or about 88%, or at least at or about 89%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:35. In some embodiments, the mutant NiV-G protein has a 10 amino acid truncation at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:36, SEQ ID NO:37 or SEQ ID NO:38), such as set forth in SEQ ID NO: 36 or a functional variant thereof having at least at or about 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at or about 84%, at least at or about 85%, at least at or about 86%, or at least at or about 87%, at least at or about 88%, or at least at or about 89%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:36, or such as set forth in SEQ ID NO: 37 or a functional variant thereof having at least at or about 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at or about 84%, at least at or about 85%, at least at or about 86%, or at least at or about 87%, at least at or about 88%, or at least at or about 89%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:37 or such as set forth in SEQ ID NO: 38 or a functional variant thereof having at least at or about 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at or about 84%, at least at or about 85%, at least at or about 86%, or at least at or about 87%, at least at or about 88%, or at least at or about 89%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:38. [0368] In some embodiments, the mutant NiV-G protein has a 15 amino acid truncation at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO:39, or SEQ ID NO:40), such as set forth in SEQ ID NO: 39 or a functional variant thereof that has an amino acid sequence having at least at or about 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at or about 84%, at least at or about 85%, at least at or about 86%, or at least at or about 87%, at least at or about 88%, or at least at or about 89%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:39 or such as set forth in SEQ ID NO: 40 or a functional variant thereof having at least at or about 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at or about 84%, at least at or about 85%, at least at or about 86%, or at least at or about 87%, at least at or about 88%, or at least at or about 89%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:40. [0369] In some embodiments, the G protein is a mutant HeV-G protein that is a biologically active portion of a wild-type HeV-G. In some embodiments, the biologically active portion is an N-terminally truncated fragment. [0370] In some embodiments, the mutant G protein is a mutant HeV-G protein that has the sequence set forth in SEQ ID NO:41 or 42, or is a functional variant or biologically active portion thereof that has an amino acid sequence having at least at or about 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at least at or about 84%, at or about 85%, at least at or about 86%, at least at or about 87%, at or about 88%, at least at or about 89%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:41 or 42. [0371] In some embodiments, the G protein is a mutant HeV-G protein that is a biologically active portion of a wild-type HeV-G. In some embodiments, the biologically active portion is an N-terminally truncated fragment. In some embodiments, the mutant HeV-G protein is truncated and lacks up to 5 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO:41 or 42), up to 6 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO:41 or 42), up to 7 contiguous amino acid residues at or near the N-terminus of the wild- type HeV-G protein (SEQ ID NO:41 or 42 or up to 8 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO:41 or 42), up to 9 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO:41 or 42), up to 10 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO:41 or 42), up to 11 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO:41 or 42), up to 12 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO:41 or 42), up to 13 contiguous amino acid residues at or near the N- terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 14 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 15 contiguous amino acid residues at or near the N-terminus of the wild- type HeV-G protein (SEQ ID NO: 41 or 42), up to 16 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 17 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 18 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 19 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 20 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 21 contiguous amino acid residues at or near the N- terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 22 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 23 contiguous amino acid residues at or near the N-terminus of the wild- type HeV-G protein (SEQ ID NO: 41 or 42), up to 24 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 25 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 26 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 27 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 28 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 29 contiguous amino acid residues at or near the N- terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 30 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 31 contiguous amino acid residues at or near the N-terminus of the wild- type HeV-G protein (SEQ ID NO: 41 or 42), up to 32 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 33 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 34 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 35 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 36 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 37 contiguous amino acid residues at or near the N- terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 38 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 39 contiguous amino acid residues at or near the N-terminus of the wild- type HeV-G protein (SEQ ID NO: 41 or 42), up to 40 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 41 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 42 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 43 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), up to 44 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), or up to 45 contiguous amino acid residues at or near the N-terminus of the wild-type HeV-G protein (SEQ ID NO: 41 or 42). In some embodiments, the HeV-G protein is a biologically active portion that does not contain a cytoplasmic domain. In some embodiments, the mutant HeV-G protein lacks the N-terminal cytoplasmic domain of the wild-type HeV-G protein (SEQ ID NO: 41 or 42), such as set forth in SEQ ID NO:44 or a functional variant thereof having at least at or about 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at or about 84%, at least at or about 85%, at least at or about 86%, or at least at or about 87%, at least at or about 88%, or at least at or about 89%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:44. [0372] In some embodiments, the G protein or the functionally active variant or biologically active portion thereof binds to Ephrin B2 or Ephrin B3. In some aspects, the G protein has the sequence of amino acids set forth in any one of SEQ ID NO:42, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or is a functionally active variant thereof or a biologically active portion thereof that is able to bind to Ephrin B2 or Ephrin B3. In some embodiments, the functionally active variant or biologically active portion has an amino acid sequence having at least at or about 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at least at or about 84%, at least at or about 85%, at or about 86%, at least at or about 87%, at least at or about 88%, or at least at or about 89% , at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to any of SEQ ID NO:42, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or a functionally active variant or biologically active portion thereof, and retains binding to Ephrhin B2 or B3. [0373] In some embodiments, the functionally active variant or biologically active portion has an amino acid sequence having at least about 80%, at least about 85%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or a functionally active variant or biologically active portion thereof, and retains binding to Ephrhin B2 or B3. Reference to retaining binding to Ephrin B2 or B3 includes binding that is at least or at least about 5% of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or a functionally active variant or biologically active portion thereof, 10% of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or a functionally active variant or biologically active portion thereof, 15% of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or a functionally active variant or biologically active portion thereof, 20% of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or a functionally active variant or biologically active portion thereof, 25% of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or a functionally active variant or biologically active portion, 30% of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or a functionally active variant or biologically active portion thereof, 35% of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or a functionally active variant or biologically active portion thereof, 40% of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or a functionally active variant or biologically active portion thereof, 45% of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or a functionally active variant or biologically active portion thereof, 50% of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or a functionally active variant or biologically active portion thereof, 55% of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or a functionally active variant or biologically active portion thereof, 60% of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or a functionally active variant or biologically active portion thereof, 65% of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28,, or a functionally active variant or biologically active portion thereof, 70% of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28 or a functionally active variant or biologically active portion thereof, such as at least or at least about 75% of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or a functionally active variant or biologically activ portion thereof, such as at least or at least about 80% of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28,, or a functionally active variant or biologically active portion thereof, such as at least or at least about 85% of the level or degree of binding of the corresponding wild- type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or a functionally active variant or biologically active portion thereof, such as at least or at least about 90% of the level or degree of binding of the corresponding wild-type G protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28, or a functionally active variant or biologically active portion thereof, or such as at least or at least about 95% of the level or degree of binding of the corresponding wild-type protein, such as set forth in SEQ ID NO:45, SEQ ID NO:41 or SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO: 23, SEQ ID NO:26 or SEQ ID NO:28,, or a functionally active variant or biologically active portion thereof.In some embodiments, the G protein is NiV-G or a functionally active variant or biologically active portion thereof and binds to Ephrin B2 or Ephrin B3. In some aspects, the NiV-G has the sequence of amino acids set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45, or is a functionally active variant thereof or a biologically active portion thereof that is able to bind to Ephrin B2 or Ephrin B3. In some embodiments, the functionally active variant or biologically active portion has an amino acid sequence having at least about 80%, at least about 85%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45 and retains binding to Eprhin B2 or B3. Exemplary biologically active portions include N-terminally truncated variants lacking all or a portion of the cytoplasmic domain, e.g. 1 or more, such as 1 to 49 contiguous N-terminal amino acid residues. Reference to retaining binding to Ephrin B2 or B3 includes binding that is at least or at least about 5% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45, 10% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45, 15% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45, 20% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45, 25% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45, 30% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45, 35% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45, 40% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45, 45% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:4550% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:68, 55% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45, 60% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45, 65% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45, 70% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:8, SEQ ID NO:9 or SEQ ID NO:44, such as at least or at least about 75% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45, such as at least or at least about 80% of the level or degree of binding of the corresponding wild-type NIV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45, such as at least or at least about 85% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45, such as at least or at least about 90% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45, or such as at least or at least about 95% of the level or degree of binding of the corresponding wild-type NiV-G, such as set forth in SEQ ID NO:22, SEQ ID NO:23 or SEQ ID NO:45. [0374] In some embodiments, the G protein or the biologically thereof is a mutant G protein that exhibits reduced binding for the native binding partner of a wild-type G protein. In some embodiments, the mutant G protein or the biologically active portion thereof is a mutant of wild- type Niv-G and exhibits reduced binding to one or both of the native binding partners Ephrin B2 or Ephrin B3. In some embodiments, the mutant G-protein or the biologically active portion, such as amutant NiV-G protein, exhibits reduced binding to the native binding partner. In some embodiments, the reduced binding to Ephrin B2 or Ephrin B3 is reduced by greater than at or about 5%, at or about 10%, at or about 15%, at or about 20%, at or about 25%, at or about 30%, at or about 40%, at or about 50%, at or about 60%, at or about 70%, at or about 80%, at or about 90%, or at or about 100%. [0375] In some embodiments, the mutations described herein can improve transduction efficiency. In some embodiments, the mutations described herein allow for specific targeting of other desired cell types that are not Ephrin B2 or Ephrin B3. In some embodiments, the mutations described herein result in at least the partial inability to bind at least one natural receptor, such has reduce the binding to at least one of Ephrin B2 or Ephrin B3. In some embodiments, the mutations described herein interfere with natural receptor recognition. [0376] In some embodiments, the G protein is HeV-G or a functionally active variant or biologically active portion thereof and binds to Ephrin B2 or Ephrin B3. In some aspects, the HeV-G has the sequence of amino acids set forth in SEQ ID NO:41 or 42, or is a functionally active variant thereof or a biologically active portion thereof that is able to bind to Ephrin B2 or Ephrin B3. In some embodiments, the functionally active variant or biologically active portion has an amino acid sequence having at least about 80%, at least about 85%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO: 40 or 41 and retains binding to Eprhin B2 or B3. Exemplary biologically active portions include N- terminally truncated variants lacking all or a portion of the cytoplasmic domain, e.g. 1 or more, such as 1 to 49 contiguous N-terminal amino acid residues. Reference to retaining binding to Ephrin B2 or B3 includes binding that is at least or at least about 5% of the level or degree of binding of the corresponding wild-type HeV-G, such as set forth in SEQ ID NO: 39 or 40, 10% of the level or degree of binding of the corresponding wild-type HeV-G, such as set forth in SEQ ID NO: 39 or 40, 15% of the level or degree of binding of the corresponding wild-type HeV-G, such as set forth in SEQ ID NO:66 or 67, 20% of the level or degree of binding of the corresponding wild-type HeV-G, such as set forth in SEQ ID NO: 41 or 42, 25% of the level or degree of binding of the corresponding wild-type HeV-G, such as set forth in SEQ ID NO: 41 or 42, 30% of the level or degree of binding of the corresponding wild-type HeV-G, such as set forth in SEQ ID NO: 41 or 42, 35% of the level or degree of binding of the corresponding wild- type HeV-G, such as set forth in SEQ ID NO: 41 or 42, 40% of the level or degree of binding of the corresponding wild-type HeV-G, such as set forth in SEQ ID NO: 41 or 42, 45% of the level or degree of binding of the corresponding wild-type HeV-G, such as set forth in SEQ ID NO: 41 or 42, 50% of the level or degree of binding of the corresponding wild-type HeV-G, such as set forth in SEQ ID NO: 41 or 42, 55% of the level or degree of binding of the corresponding wild- type HeV-G, such as set forth in SEQ ID NO: 41 or 42, 60% of the level or degree of binding of the corresponding wild-type HeV-G, such as set forth in SEQ ID NO: 41 or 42, 65% of the level or degree of binding of the corresponding wild-type HeV-G, such as set forth in SEQ ID NO: 41 or 42, 70% of the level or degree of binding of the corresponding wild-type HeV-G, such as set forth in SEQ ID NO:18 or 52, such as at least or at least about 75% of the level or degree of binding of the corresponding wild-type HeV-G, such as set forth in SEQ ID NO: 41 or 42, such as at least or at least about 80% of the level or degree of binding of the corresponding wild-type NIV-G, such as set forth in SEQ ID NO: 41 or 42, such as at least or at least about 85% of the level or degree of binding of the corresponding wild-type HeV-G, such as set forth in SEQ ID NO: 41 or 42, such as at least or at least about 90% of the level or degree of binding of the corresponding wild-type HeV-G, such as set forth in SEQ ID NO: 41 or 42, or such as at least or at least about 95% of the level or degree of binding of the corresponding wild-type HeV-G, such as set forth in SEQ ID NO: 41 or 42. [0377] In some embodiments, the G protein or the biologically thereof is a mutant G protein that exhibits reduced binding for the native binding partner of a wild-type G protein. In some embodiments, the mutant G protein or the biologically active portion thereof is a mutant of wild-type Niv-G and exhibits reduced binding to one or both of the native binding partners Ephrin B2 or Ephrin B3. In some embodiments, the mutant G-protein or the biologically active portion, such as amutant NiV-G protein, exhibits reduced binding to the native binding partner. In some embodiments, the reduced binding to Ephrin B2 or Ephrin B3 is reduced by greater than at or about 5%, at or about 10%, at or about 15%, at or about 20%, at or about 25%, at or about 30%, at or about 40%, at or about 50%, at or about 60%, at or about 70%, at or about 80%, at or about 90%, or at or about 100%. [0378] In some embodiments, the G protein contains one or more amino acid substitutions in a residue that is involved in the interaction with one or both of Ephrin B2 and Ephrin B3. In some embodiments, the amino acid substitutions correspond to mutations E501A, W504A, Q530A and E533A with reference to numbering set forth in SEQ ID NO:39. [0379] In some embodiments, the G protein is a mutant G protein containing one or more amino acid substitutions selected from the group consisting of E501A, W504A, Q530A and E533A with reference to numbering set forth in SEQ ID NO:22. In some embodiments, the G protein is a mutant G protein that contains one or more amino acid substitutions elected from the group consisting of E501A, W504A, Q530A and E533A with reference to SEQ ID NO:22 and is a biologically active portion thereof containing an N- terminal truncation. In some embodiments, the mutant NiV-G protein or the biologically active portion thereof is truncated and lacks up to 5 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), 6 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), 7 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), 8 contiguous amino acid residues at or near the N-terminus of the wild- type NiV-G protein (SEQ ID NO: 22), 9 contiguous amino acid residues at or near the N- terminus of the wild-type NiV-G protein (SEQ ID NO: 22), up to 10 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), 11 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), 12 contiguous amino acid residues at or near the N-terminus of the wild- type NiV-G protein (SEQ ID NO: 22), 13 contiguous amino acid residues at or near the N- terminus of the wild-type NiV-G protein (SEQ ID NO: 22), 14 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), up to 15 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), 16 contiguous amino acid residues at or near the N-terminus of the wild- type NiV-G protein (SEQ ID NO: 22), 17 contiguous amino acid residues at or near the N- terminus of the wild-type NiV-G protein (SEQ ID NO: 22), 18 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), 19 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), up to 20 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), 21 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22) 22 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), 23 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), 24 contiguous amino acid residues at or near the N-terminus of the wild- type NiV-G protein (SEQ ID NO: 22), up to 25 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), 26 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), 27 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), 28 contiguous amino acid residues at or near the N-terminus of the wild- type NiV-G protein (SEQ ID NO: 22), 29 contiguous amino acid residues at or near the N- terminus of the wild-type NiV-G protein (SEQ ID NO: 22), up to 30 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (EQ ID NO: 22), up to 31 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), 32 contiguous amino acid residues at or near the N-terminus of the wild- type NiV-G protein (SEQ ID NO: 22), 33 contiguous amino acid residues at or near the N- terminus of the wild-type NiV-G protein (SEQ ID NO: 22) 34 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), 35 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22) up to 36 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (EQ ID NO: 22), up to 37 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (EQ ID NO: 22), up to 38 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (EQ ID NO: 22), up to 39 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (SEQ ID NO: 22), or up to 40 contiguous amino acid residues at or near the N-terminus of the wild-type NiV-G protein (EQ ID NO: 22). [0380] In some embodiments, the mutant NiV-G protein has the amino acid sequence set forth in SEQ ID NO: 35 or 36 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO: 35 or 36. In particular embodiments, the G protein has the sequence of amino acids set forth in SEQ ID NO 35 or 36. [0381] In some embodiments, the G protein is a mutant G protein containing one or more amino acid substitutions selected from the group consisting of E501A, W504A, Q530A and E533A with reference to numbering set forth in SEQ ID NO:24. In some embodiments, the G protein is a mutant G protein that contains one or more amino acid substitutions elected from the group consisting of E501A, W504A, Q530A and E533A with reference to SEQ ID NO:24 and is a biologically active portion thereof containing an N-terminal truncation. b. F Proteins [0382] In some embodiments, the vector-surface targeting moiety comprises a protein with a hydrophobic fusion peptide domain. In some embodiments, the vector-surface targeting moiety comprises a henipavirus F protein molecule or biologically active portion thereof. In some embodiments, the Henipavirus F protein is a Hendra (Hev) virus F protein, a Nipah (NiV) virus F-protein, a Cedar (CedPV) virus F protein, a Mojiang virus F protein or a bat Paramyxovirus F protein or a biologically active portion thereof. [0383] Table 2 provides non-limiting examples of F proteins. In some embodiments, the N- terminal hydrophobic fusion peptide domain of the F protein molecule or biologically active portion thereof is exposed on the outside of lipid bilayer. [0384] F proteins of henipaviruses are encoded as F0 precursors containing a signal peptide (e g corresponding to amino acid residues 1-26 of SEQ ID NO:46) Following cleavage of the signal peptide, the mature F 0 (e.g. SEQ ID NO:47) is transported to the cell surface, then endocytosed and cleaved by cathepsin L into the mature fusogenic subunits F1 and F2. The F1 and F2 subunits are associated by a disulfide bond and recycled back to the cell surface. The F1 subunit contains the fusion peptide domain located at the N terminus of the F1 subunit, where it is able to insert into a cell membrane to drive fusion. In some aspects, fusion is blocked by association of the F protein with G protein, until the G protein engages with a target molecule resulting in its disassociation from F and exposure of the fusion peptide to mediate membrane fusion. [0385] Among different henipavirus species, the sequence and activity of the F protein is highly conserved. For examples, the F protein of NiV and HeV viruses share 89% amino acid sequence identity. Further, in some cases, the henipavirus F proteins exhibit compatibility with G proteins from other species to trigger fusion (Brandel-Tretheway et al. Journal of Virology. 2019. 93(13):e00577-19). In some aspects or the provided re-targeted lipid particles, the F protein is heterologous to the G protein, i.e. the F and G protein or biologically active portions are from different henipavirus species. For example, the F protein is from Hendra virus and the G protein is from Nipah virus. In other aspects, the F protein can be a chimeric F protein containing regions of F proteins from different species of Henipavirus. In some embodiments, switching a region of amino acid residues of the F protein from one species of Henipavirus to another can result in fusion to the G protein of the species comprising the amino acid insertion. (Brandel-Tretheway et al. Journal of Virology. 2019. 93(13):e00577-19). In some cases, the chimeric F protein contains an extracellular domain from one henipavirus species and a transmembrane and/or cytoplasmic domain from a different henipavirus species. For example, the F protein contains an extracellular domain of Hendra virus and a transmembrane/cytoplasmic domain of Nipah virus. F protein sequences disclosed herein are predominantly disclosed as expressed sequences including an N-terminal signal sequence. As such N-terminal signal sequences are commonly cleaved co- or post-translationally, the mature protein sequences for all F protein sequences disclosed herein are also contemplated as lacking the N-terminal signal sequence.
[0386] In some embodiments, the F protein is encoded by a nucleotide sequence that encodes the sequence set forth by any one of SEQ ID NO:16, SEQ ID NO:17, SEQ ID NO:18, SEQ ID NO:19, SEQ ID NO:20 , SEQ ID NO:21, SEQ ID NO:22, SEQ ID NO:23, SEQ ID NO:24, or SEQ ID NO:25or is a functionally active variant or a biologically active portion thereof that has a sequence that is at least at or about 80%, at least at or about 85%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% identical to any one of SEQ ID NO:46, SEQ ID NO:47, SEQ ID NO:48, SEQ ID NO:49, SEQ ID NO:50 , SEQ ID NO:51, SEQ ID NO:52, SEQ ID NO:53, SEQ ID NO:54, or SEQ ID NO:55. [0387] In particular embodiments, the F protein or the functionally active variant or biologically active portion thereof retains fusogenic activity in conjunction with a Henipavirus G protein, such as a G protein set forth in Section IV.A.2 (e.g. NiV-G or HeV-G). Fusogenic activity includes the activity of the F protein in conjunction with a G protein to promote or facilitate fusion of two membrane lumens, such as the lumen of the targeted lipid particle having embedded in its lipid bilayer a henipavirus F and G protein, and a cytoplasm of a target cell, e.g. a cell that contains a surface receptor or molecule that is recognized or bound by the targeted envelope protein. In some embodiments, the F protein and G protein are from the same Henipavirus species (e.g. NiV-G and NiV-F). In some embodiments, the F protein and G protein are from different Henipavirus species (e.g. NiV-G and HeV-F). In particular embodiments, the F protein of the functionally active variant or biologically active portion retains the cleavage site cleaved by cathepsin L(e.g. corresponding to the cleavage site between amino acids 109-110 of SEQ ID NO:48). [0388] In particular embodiments, the F protein has the sequence of amino acids set forth in SEQ ID NO:46, SEQ ID NO:47, SEQ ID NO:48, SEQ ID NO:49, SEQ ID NO:50 , SEQ ID NO:51, SEQ ID NO:52, SEQ ID NO:53, SEQ ID NO:54, or SEQ ID NO:55, or is a functionally active variant thereof or a biologically active portion thereof that retains fusogenic activity. In some embodiments, the functionally active variant comprises an amino acid sequence having at least at or about 80%, at least at or about 85%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:46, SEQ ID NO:47, SEQ ID NO:48, SEQ ID NO:49, SEQ ID NO:50 , SEQ ID NO:51, SEQ ID NO:52, SEQ ID NO:53, SEQ ID NO:54, or SEQ ID NO:55, and retains fusogenic activity in conjunction with a Henipavirus G protein (e.g., NiV-G or HeV-G). In some embodiments, the biologically active portion has an amino acid sequence having at least at or about 80%, at least at or about 85%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:46, SEQ ID NO:47, SEQ ID NO:48, SEQ ID NO:49, SEQ ID NO:50 , SEQ ID NO:51, SEQ ID NO:52, SEQ ID NO:53, SEQ ID NO:54, or SEQ ID NO:55. [0389] Reference to retaining fusogenic activity includes activity (in conjunction with a Henipavirus G protein) that between at or about 10% and at or about 150% or more of the level or degree of binding of the corresponding wild-type F protein, such as set forth in SEQ ID NO:46, SEQ ID NO:47, SEQ ID NO:48, SEQ ID NO:49, SEQ ID NO:50 , SEQ ID NO:51, SEQ ID NO:52, SEQ ID NO:53, SEQ ID NO:54, or SEQ ID NO:55, such as at least or at least about 10% of the level or degree of fusogenic activity of the corresponding wild-type F protein, such as at least or at least about 15% of the level or degree of fusogenic activity of the corresponding wild-type F protein, such as at least or at least about 20% of the level or degree of fusogenic activity of the corresponding wild-type F protein, such as at least or at least about 25% of the level or degree of fusogenic activity of the corresponding wild-type F protein, such as at least or at least about 30% of the level or degree of fusogenic activity of the corresponding wild- type F protein, such as at least or at least about 35% of the level or degree of fusogenic activity of the corresponding wild-type F protein, such as at least or at least about 40% of the level or degree of fusogenic activity of the corresponding wild-type F protein, such as at least or at least about 45% of the level or degree of fusogenic activity of the corresponding wild-type F protein, such as at least or at least about 50% of the level or degree of fusogenic activity of the corresponding wild-type F protein, such as at least or at least about 55% of the level or degree of fusogenic activity of the corresponding wild-type f protein, such as at least or at least about 60% of the level or degree of fusogenic activity of the corresponding wild-type F protein, such as at least or at least about 65% of the level or degree of fusogenic activity of the corresponding wild- type F protein, such as at least or at least about 70% of the level or degree of fusogenic activity of the corresponding wild-type F protein, such as at least or at least about 75% of the level or degree of fusogenic activity of the corresponding wild-type F protein, such as at least or at least about 80% of the level or degree of fusogenic activity of the corresponding wild-type F protein, such as at least or at least about 85% of the level or degree of fusogenic activity of the corresponding wild-type F protein, such as at least or at least about 90% of the level or degree of fusogenic activity of the corresponding wild-type F protein, such as at least or at least about 95% of the level or degree of fusogenic activity of the corresponding wild-type F protein, such as at least or at least about 100% of the level or degree of fusogenic activity of the corresponding wild-type F protein, or such as at least or at least about 120% of the level or degree of fusogenic activity of the corresponding wild-type F protein. [0390] In some embodiments, the F protein is a mutant F protein that is a functionally active fragment or a biologically active portion containing one or more amino acid mutations, such as one or more amino acid insertions, deletions, substitutions or truncations. In some embodiments, the mutations described herein relate to amino acid insertions, deletions, substitutions or truncations of amino acids compared to a reference F protein sequence. In some embodiments, the reference F protein sequence is the wild-type sequence of an F protein or a biologically active portion thereof. In some embodiments, the mutant F protein or the biologically active portion thereof is a mutant of a wild-type Hendra (Hev) virus F protein, a Nipah (NiV) virus F-protein, a Cedar (CedPV) virus F protein, a Mojiang virus F protein or a bat Paramyxovirus F protein. In some embodiments, the wild-type F protein is encoded by a sequence of nucleotides that encodes any one of SEQ ID NO:46, SEQ ID NO:47, SEQ ID NO:48, SEQ ID NO:49, SEQ ID NO:50 , SEQ ID NO:51, SEQ ID NO:52, SEQ ID NO:53, SEQ ID NO:54, or SEQ ID NO:55, [0391] In some embodiments, the mutant F protein is a biologically active portion of a wild- type F protein that is an N-terminally and/or C-terminally truncated fragment. In some embodiments, the mutant F protein or the biologically active portion of a wild-type F protein thereof comprises one or more amino acid substitutions. In some embodiments, the mutations described herein can improve transduction efficiency. In some embodiments, the mutations described herein can increase fusogenic capacity. Exemplary mutations include any as described, see e.g. Khetawat and Broder 2010 Virology Journal 7:312; Witting et al. 2013 Gene Therapy 20:997-1005; published international; patent application No. WO/2013/148327. [0392] In some embodiments, the mutant F protein is a biologically active portion that is truncated and lacks up to 20 contiguous amino acid residues at or near the C-terminus of the wild-type F protein, such as a wild-type F protein encoded by a sequence of nucleotides encoding the F protein set forth in any one of SEQ ID NOS: 46-55. In some embodiments, the mutant F protein is truncated and lacks up to 19 contiguous amino acids, such as up to 18 , 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 contiguous amino acids at the C-terminus of the wild-type F protein. [0393] In some embodiments, the F protein or the functionally active variant or biologically active portion thereof comprises an F1 subunit or a fusogenic portion thereof. In some embodiments, the F1 subunit is a proteolytically cleaved portion of the F0 precursor. In some embodiments, the F 0 precursor is inactive. In some embodiments, the cleavage of the F 0 precursor forms a disulfide-linked F1+F2 heterodimer. In some embodiments, the cleavage exposes the fusion peptide and produces a mature F protein. In some embodiments, the cleavage occurs at or around a single basic residue. In some embodiments, the cleavage occurs at Arginine 109 of NiV-F protein. In some embodiments, cleavage occurs at Lysine 109 of the Hendra virus F protein. [0394] In some embodiments, the F protein is a wild-type Nipah virus F (NiV-F) protein or is a functionally active variant or biologically active porteion thereof. In some embodiments, the F0 precursor is encoded by a sequence of nucleotides encoding the sequence set forth in SEQ ID NO: 37. The encoding nucleic acid can encode a signal peptide sequence that has the sequence MVVILDKRCY CNLLILILMI SECSVG (SEQ ID NO: 56). In some embodiments, the F protein has the sequence set forth in SEQ ID NO:18. In some examples, the F protein is cleaved into an F1 subunit comprising the sequence set forth in SEQ ID NO:57 and an F2 subunit comprising the sequence set forth in SEQ ID NO: 58. [0395] In some embodiments, the F protein is a NiV-F protein that is encoded by a sequence of nucleotides encoding the sequence set forth in SEQ ID NO:48, or is a functionally active variant or biologically active portion thereof that has an amino acid sequence having at least at or about 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at least at or about 84%, at least at or about 85%, at or about 86%, at least at or about 87%, at least at or about 88%, or at least at or about 89%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO: 48. In some embodiments, the NiV-F-protein has the sequence of set forth in SEQ ID NO: 25, or is a functionally active variant or a biologically active portion thereof that has an amino acid sequence having at least at or about 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at least at or about 84%, at least at or about 85%, at or about 86%, at least at or about 87%, at least at or about 88%, or at least at or about 89%, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO: 25. In particular embodiments, the F protein or the functionally active variant or biologically active portion thereof retains the cleavage site cleaved by cathepsin L. [0396] In some embodiments, the F protein or the functionally active variant or the biologically active portion thereof includes an F1 subunit that has the sequence set forth in SEQ ID NO: 57, or an amino acid sequence having, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:57. [0397] In some embodiments, the F protein or the functionally active variant or biologically active portion thereof includes an F2 subunit that has the sequence set forth in SEQ ID NO: 58, or an amino acid sequence having, at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:58. [0398] In some embodiments, the F protein or the functionally active variant or the biologically active portion thereof includes an F1 subunit that has the sequence set forth in SEQ ID NO: 23, or an amino acid sequence having, at least at or about 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at least at or about 84%, at least at or about 85%, at or about 86%, at least at or about 87%, at least at or about 88%, or at least at or about 89% at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:23. [0399] In some embodiments, the F protein or the functionally active variant or biologically active portion thereof includes an F2 subunit that has the sequence set forth in SEQ ID NO: 24, or an amino acid sequence having, at least at or about 80%, at least at or about 81%, at least at or about 82%, at least at or about 83%, at least at or about 84%, at least at or about 85%, at or about 86%, at least at or about 87%, at least at or about 88%, or at least at or about 89% at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:24. [0400] In some embodiments, the F protein is a mutant NiV-F protein that is a biologically active portion thereof that is truncated and lacks up to 20 contiguous amino acid residues at or near the C-terminus of the wild-type NiV-F protein (e.g. set forth SEQ ID NO:57). In some embodiments, the mutant NiV-F protein comprises an amino acid sequence set forth in SEQ ID NO:25. In some embodiments, the mutant NiV-F protein has a sequence that has at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO: 25. In some embodiments, the mutant F protein contains an F1 protein that has the sequence set forth in SEQ ID NO:26. In some embodiments, the mutant F protein has a sequence that has at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO: 26. [0401] In some embodiments, the F protein is a mutant NiV-F protein that is a biologically active portion thereof that comprises a 20 amino acid truncation at or near the C-terminus of the wild-type NiV-F protein (SEQ ID NO:57); and a point mutation on an N-linked glycosylation site. In some embodiments, the mutant NiV-F protein comprises an amino acid sequence set forth in SEQ ID NO: 27. In some embodiments, the mutant NiV-F protein has a sequence that has at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO: 27. [0402] In some embodiments, the F protein is a mutant NiV-F protein that is a biologically active portion thereof that comprises a 22 amino acid truncation at or near the C-terminus of the wild-type NiV-F protein (SEQ ID NO:57). In some embodiments, the NiV-F protein is encoded by a nucleotide sequence that encodes the sequence set forth in SEQ ID NO: 28. In some embodiments, the NiV-F proteins is encoded by a nucleotide sequence that encodes sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO: 28. B. Non-protein Fusogens [0403] In some embodiments, the non-cell particle can comprise one or more fusogenic lipids, such as saturated fatty acids. In some embodiments, the saturated fatty acids have between 10-14 carbons. In some embodiments, the saturated fatty acids have longer-chain carboxylic acids. In some embodiments, the saturated fatty acids are mono-esters. [0404] In some embodiments, the non-cell particle can comprise one or more unsaturated fatty acids. In some embodiments, the unsaturated fatty acids have between C16 and C18 unsaturated fatty acids. In some embodiments, the unsaturated fatty acids include oleic acid, glycerol mono-oleate, glycerides, diacylglycerol, modified unsaturated fatty acids, and any combination thereof. [0405] Without wishing to be bound by theory, in some embodiments negative curvature lipids promote membrane fusion In some embodiments the non-cell particle comprises one or more negative curvature lipids, e.g., exogenous negative curvature lipids, in the membrane. In embodiments, the negative curvature lipid or a precursor thereof is added to media comprising source cells or non-cell particles. In embodiments, the source cell is engineered to express or overexpress one or more lipid synthesis genes. The negative curvature lipid can be, e.g., diacylglycerol (DAG), cholesterol, phosphatidic acid (PA), phosphatidylethanolamine (PE), or fatty acid (FA). [0406] In some embodiments positive curvature lipids inhibit membrane fusion. In some embodiments, the non-cell particle comprises reduced levels of one or more positive curvature lipids, e.g., exogenous positive curvature lipids, in the membrane. In embodiments, the levels are reduced by inhibiting synthesis of the lipid, e.g., by knockout or knockdown of a lipid synthesis gene, in the source cell. The positive curvature lipid can be, e.g., lysophosphatidylcholine (LPC), phosphatidylinositol (PtdIns), lysophosphatidic acid (LPA), lysophosphatidylethanolamine (LPE), or monoacylglycerol (MAG). [0407] In some embodiments, the non-cell particle may be treated with fusogenic chemicals. In some embodiments, the fusogenic chemical is polyethylene glycol (PEG) or derivatives thereof. [0408] In some embodiments, the chemical fusogen induces a local dehydration between the two membranes that leads to unfavorable molecular packing of the bilayer. In some embodiments, the chemical fusogen induces dehydration of an area near the lipid bilayer, causing displacement of aqueous molecules between two membranes and allowing interaction between the two membranes together. [0409] In some embodiments, the chemical fusogen is a positive cation. Some nonlimiting examples of positive cations include Ca2+, Mg2+, Mn2+, Zn2+, La3+, Sr3+, and H+. [0410] In some embodiments, the chemical fusogen binds to the target membrane by modifying surface polarity, which alters the hydration-dependent intermembrane repulsion. [0411] In some embodiments, the chemical fusogen is a soluble lipid soluble. Some nonlimiting examples include oleoylglycerol, dioleoylglycerol, trioleoylglycerol, and variants and derivatives thereof. [0412] In some embodiments, the chemical fusogen is a water-soluble chemical. Some nonlimiting examples include polyethylene glycol, dimethyl sulphoxide, and variants and derivatives thereof. [0413] In some embodiments, the chemical fusogen is a small organic molecule. A nonlimiting example includes n-hexyl bromide. [0414] In some embodiments, the chemical fusogen does not alter the constitution, cell viability, or the ion transport properties of the fusogen or target membrane. [0415] In some embodiments, the chemical fusogen is a hormone or a vitamin. Some nonlimiting examples include abscisic acid, retinol (vitamin A1), a tocopherol (vitamin E), and variants and derivatives thereof. [0416] In some embodiments, the retroviral vector or VLP comprises actin and an agent that stabilizes polymerized actin. Without wishing to be bound by theory, stabilized actin in a retroviral vector or VLP can promote fusion with a target cell. In embodiments, the agent that stabilizes polymerized actin is chosen from actin, myosin, biotin-streptavidin, ATP, neuronal Wiskott–Aldrich syndrome protein (N-WASP), or formin. See, e.g., Langmuir. 2011 Aug 16;27(16):10061-71 and Wen et al., Nat Commun. 2016 Aug 31;7. In embodiments, the retroviral vector or VLP comprises exogenous actin, e.g., wild-type actin or actin comprising a mutation that promotes polymerization. In embodiments, the retroviral vector or VLP comprises ATP or phosphocreatine, e.g., exogenous ATP or phosphocreatine. [0417] In some embodiments, the non-cell particle may be treated with fusogenic small molecules. Some nonlimiting examples include halothane, nonsteroidal anti-inflammatory drugs (NSAIDs) such as meloxicam, piroxicam, tenoxicam, and chlorpromazine. [0418] In some embodiments, the small molecule fusogen may be present in micelle-like aggregates or free of aggregates. C. Re-targeted Fusogens [0419] In some embodiments, protein fusogens or viral envelope proteins may be re-targeted by mutating amino acid residues in a fusion protein or a targeting protein (e.g. the hemagglutinin protein). In particular embodiments, the fusogen (e.g. G protein) is mutated to reduce binding for the native binding partner of the fusogen. In some embodiments, the fusogen is or contains a mutant G protein or a biologically active portion thereof that is a mutant of wild-type Niv-G and exhibits reduced binding to one or both of the native binding partners Ephrin B2 or Ephrin B3, including any as described above. Thus, in some aspects, a fusogen can be retargeted to display altered tropism. In some embodiments, the binding confers re-targeted binding compared to the binding of a wild-type surface glycoprotein protein in which a new or different binding activity is conferred. In particular embodiments, the binding confers re-targeted binding compared to the binding of a wild-type G protein in which a new or different binding activity is conferred. In some embodiments the fusogen is randomly mutated. In some embodiments the fusogen is rationally mutated. In some embodiments the fusogen is subjected to directed evolution. In some embodiments the fusogen is truncated and only a subset of the peptide is used in the non-cell particle. In some embodiments, amino acid residues in the measles hemagglutinin protein may be mutated to alter the binding properties of the protein, redirecting fusion (doi:10.1038/nbt942, Molecular Therapy vol. 16 no. 8, 1427–1436 Aug. 2008, doi:10.1038/nbt1060, DOI: 10.1128/JVI.76.7.3558–3563.2002, DOI: 10.1128/JVI.75.17.8016–8020.2001, doi: 10.1073pnas.0604993103). [0420] In some embodiments, protein fusogens may be re-targeted by covalently conjugating a targeting-moiety to the fusion protein or targeting protein (e.g. the hemagglutinin protein). In some embodiments, the fusogen and targeting moiety are covalently conjugated by expression of a chimeric protein comprising the fusogen linked to the targeting moiety. In some embodiments, a target includes any peptide (e.g. a receptor) that is displayed on a target cell. In some embodiments, the target is expressed at higher levels on a target cell than non-target cells. In some embodiments, a single-chain variable fragment (scFv) can be conjugated to fusogens to redirect fusion activity towards cells that display the scFv binding target (doi:10.1038/nbt1060, DOI 10.1182/blood-2012-11-468579, doi:10.1038/nmeth.1514, doi:10.1006/mthe.2002.0550, HUMAN GENE THERAPY 11:817– 826, doi:10.1038/nbt942, doi:10.1371/journal.pone.0026381, DOI 10.1186/s12896-015-0142-z). In some embodiments, designed ankyrin repeat proteins (DARPin) can be conjugated to fusogens to redirect fusion activity towards cells that display the DARPin binding target (doi:10.1038/mt.2013.16, doi:10.1038/mt.2010.298, doi: 10.4049/jimmunol.1500956), as well as combinations of different DARPins (doi:10.1038/mto.2016.3). In some embodiments, receptor ligands and antigens can be conjugated to fusogens to redirect fusion activity towards cells that display the target receptor (DOI: 10.1089/hgtb.2012.054, DOI: 10.1128/JVI.76.7.3558–3563.2002). In some embodiments, a targeting protein can also include an antibody or an antigen-binding fragment thereof (e.g., Fab, Fab', F(ab')2, Fv fragments, scFv antibody fragments, disulfide-linked Fvs (sdFv), a Fd fragment consisting of the VH and CH1 domains, linear antibodies, single domain antibodies such as sdAb (either VL or VH), nanobodies, or camelid VHH domains), an antigen-binding fibronectin type III (Fn3) scaffold such as a fibronectin polypeptide minibody, a ligand, a cytokine, a chemokine, or a T cell receptor (TCRs). In some embodiments, protein fusogens may be re-targeted by non-covalently conjugating a targeting moiety to the fusion protein or targeting protein (e.g. the hemagglutinin protein). In some embodiments, the fusion protein can be engineered to bind the Fc region of an antibody that targets an antigen on a target cell, redirecting the fusion activity towards cells that display the antibody’s target (DOI: 10.1128/JVI.75.17.8016–8020.2001, doi:10.1038/nm1192). In some embodiments, altered and non-altered fusogens may be displayed on the same retroviral vector or VLP (doi: 10.1016/j.biomaterials.2014.01.051). [0421] In some embodiments, a targeting moiety comprises a humanized antibody molecule, intact IgA, IgG, IgE or IgM antibody; bi- or multi- specific antibody (e.g., Zybodies®, etc); antibody fragments such as Fab fragments, Fab’ fragments, F(ab’)2 fragments, Fd’ fragments, Fd fragments, and isolated CDRs or sets thereof; single chain Fvs; polypeptide-Fc fusions; single domain antibodies (e.g., shark single domain antibodies such as IgNAR or fragments thereof); cameloid antibodies; masked antibodies (e.g., Probodies®); Small Modular ImmunoPharmaceuticals (“SMIPsTM”); single chain or Tandem diabodies (TandAb®); VHHs; Anticalins®; Nanobodies®; minibodies; BiTE®s; ankyrin repeat proteins or DARPINs®; Avimers®; DARTs; TCR-like antibodies;, Adnectins®; Affilins®; Trans-bodies®; Affibodies®; TrimerX®; MicroProteins; Fynomers®, Centyrins®; and KALBITOR®s. [0422] In embodiments, the re-targeted fusogen binds a cell surface marker on the target cell, e.g., a protein, glycoprotein, receptor, cell surface ligand, agonist, lipid, sugar, class I transmembrane protein, class II transmembrane protein, or class III transmembrane protein. [0423] In some embodiments, vector-surface targeting moiety is a peptide. In some embodiments, vector-surface targeting moiety is an antibody, such as a single domain antibody. In some embodiments, the antibody can be human or humanized. In some embodiments, antibody or portion thereof is naturally occurring. In some embodiments, the antibody or portion thereof is synthetic. [0424] In some embodiments, the antibody can be generated from phage display libraries to have specificity for a desired target ligand. In some embodiments the target ligand is expressed in the lung, such as ACE2. In some embodiments, the phage display libraries are generated from a VHH repertoire of camelids immunized with various antigens, as described in Arbabi et al., FEBS Letters, 414, 521-526 (1997); Lauwereys et al., EMBO J., 17, 3512-3520 (1998); Decanniere et al., Structure, 7, 361-370 (1999). In some embodiments, the phage display library is generated comprising antibody fragments of a non-immunized camelid. In some embodiments, single domain antibodies a library of human single domain antibodies is synthetically generated by introducing diversity into one or more scaffolds. [0425] In some embodiments, the C-terminus of the vector-surface targeting moiety is attached to the C-terminus of the G protein (e.g., fusogen) or biologically active portion thereof. In some embodiments, the N-terminus of the vector-surface targeting moiety is exposed on the exterior surface of the lipid bilayer. In some embodiments, the N-terminus of the vector-surface targeting moiety binds to a cell surface molecule of a target cell. In some embodiments, the vector-surface targeting moiety specifically binds to a cell surface molecule present on a target cell. In some embodiments, the vector-surface targeting moiety is a protein, glycan, lipid or low molecular weight molecule. [0426] In some embodiments, the cell surface marker is a molecule expressed on a target cell that is an antigen or portion thereof recognized by the targeting moeity. [0427] Exemplary target cells include polymorphonuclear cells (also known as PMN, PML, PMNL, or granulocytes), stem cells, embryonic stem cells, neural stem cells, mesenchymal stem cells (MSCs), hematopoietic stem cells (HSCs), human myogenic stem cells, muscle-derived stem cells (MuStem), embryonic stem cells (ES or ESCs), limbal epithelial stem cells, cardio- myogenic stem cells, cardiomyocytes, progenitor cells, immune effector cells, lymphocytes, macrophages, dendritic cells, natural killer cells, T cells, cytotoxic T lymphocytes, allogenic cells, resident cardiac cells, induced pluripotent stem cells (iPS), adipose-derived or phenotypic modified stem or progenitor cells, CD133+ cells, aldehyde dehydrogenase-positive cells (ALDH+), umbilical cord blood (UCB) cells, peripheral blood stem cells (PBSCs), neurons, neural progenitor cells, pancreatic beta cells, glial cells, or hepatocytes, [0428] In some embodiments, the target cell is a cell of a target tissue. The target tissue can include liver, lungs, heart, spleen, pancreas, gastrointestinal tract, kidney, testes, ovaries, brain, reproductive organs, central nervous system, peripheral nervous system, skeletal muscle, endothelium, inner ear, or eye. [0429] In some embodiments, the target cell is a muscle cell (e.g., skeletal muscle cell), kidney cell, liver cell (e.g. hepatocyte), or a cadiac cell (e.g. cardiomyocyte). In some embodiments, the target cell is a cardiac cell, e.g., a cardiomyocyte (e.g., a quiescent cardiomyocyte), a hepatoblast (e.g., a bile duct hepatoblast), an epithelial cell, a T cell (e.g. a naive T cell), a macrophage (e.g., a tumor infiltrating macrophage), or a fibroblast (e.g., a cardiac fibroblast). [0430] In some embodiments, the target cell is a tumor-infiltrating lymphocyte, a T cell, a neoplastic or tumor cell, a virus-infected cell, a stem cell, a central nervous system (CNS) cell, a hematopoeietic stem cell (HSC), a liver cell or a fully differentiated cell. In some embodiments, the target cell is a CD3+ T cell, a CD4+ Tcell, a CD8+ T cell, a hepatocyte, a haematepoietic stem cell, a CD34+ haematepoietic stem cell, a CD105+ haematepoietic stem cell, a CD117+ haematepoietic stem cell, a CD105+ endothelial cell, a B cell, a CD20+ B cell, a CD19+ B cell, a cancer cell, a CD133+ cancer cell, an EpCAM+ cancer cell, a CD19+ cancer cell, a Her2/Neu+ cancer cell, a GluA2+ neuron, a GluA4+ neuron,a NKG2D+ natural killer cell, a SLC1A3+ astrocyte, a SLC7A10+ adipocyte, or a CD30+ lung epithelial cell. [0431] In some embodiments, the target cell is an antigen presenting cell, an MHC class II+ cell, a professional antigen presenting cell, an atypical antigen presenting cell, a macrophage, a dendritic cell, a myeloid dendritic cell, a plasmacyteoid dendritic cell, a CD11c+ cell, a CD11b+ cell, a splenocyte, a B cell, a hepatocyte, a endothelial cell, or a non-cancerous cell). [0432] In some embodiments, the cell surface marker is any one of CD8, CD4, asialoglycoprotein receptor 2 (ASGR2), transmembrane 4 L6 family member 5 (TM4SF5), low density lipoprotein receptor (LDLR) or asialoglycoprotein 1 (ASGR1). [0433] In some embodiments, non-cell particles may display targeting moieties that are not conjugated to protein fusogens in order to redirect the fusion activity towards a cell that is bound by the targeting moiety, or to affect homing. [0434] In some embodiments, the targeting moiety added to the non-cell particle is modulated to have different binding strengths. In some embodiments, scFvs and antibodies with various binding strengths may be used to alter the fusion activity of the non-cell particle towards cells that display high or low amounts of the target antigen (doi:10.1128/JVI.01415-07, doi:10.1038/cgt.2014.25, DOI: 10.1002/jgm.1151). In some embodiments, DARPins with different affinities may be used to alter the fusion activity of the non-cell particle towards cells that display high or low amounts of the target antigen (doi:10.1038/mt.2010.298). In some embodiments, targeting moieties may also be modulated to target different regions on the target ligand, which will affect the fusion rate with cells displaying the target (doi: 10.1093/protein/gzv005). [0435] In some embodiments protein fusogens can be altered to reduce immunoreactivity, e.g., as described herein. In some embodiments, protein fusogens may be decorated with molecules that reduce immune interactions, such as PEG (DOI: 10.1128/JVI.78.2.912– 921.2004). In some embodiments, the fusogen comprises PEG, e.g., is a PEGylated polypeptide. In some embodiments, amino acid residues in the fusogen that are targeted by the immune system may be altered to be unrecognized by the immune system (doi: 10.1016/j.virol.2014.01.027, doi:10.1371/journal.pone.0046667). In some embodiments the protein sequence of the fusogen is altered to resemble amino acid sequences found in humans (humanized). In some embodiments the protein sequence of the fusogen is changed to a protein sequence that binds MHC complexes less strongly. In some embodiments, the protein fusogens are derived from viruses or organisms that do not infect humans (and which humans have not been vaccinated against), increasing the likelihood that a patient’s immune system is naïve to the protein fusogens (e.g., there is a negligible humoral or cell-mediated adaptive immune response towards the fusogen) (doi:10.1006/mthe.2002.0550, doi:10.1371/journal.ppat.1005641, doi:10.1038/gt.2011.209, DOI 10.1182/blood-2014-02-558163). In some embodiments, glycosylation of the fusogen may be changed to alter immune interactions or reduce immunoreactivity. [0436] In some embodiments, a protein fusogen derived from a virus or organism that do not infect humans does not have a natural fusion targets in patients, and thus has high specificity. V. EXOGENOUS AGENT [0437] In some embodiments, the non-cell particle or pharmaceutical composition comprising same described herein contains an exogenous agent. In some embodiments, the non- cell particle or pharmaceutical composition comprising same described herein contains a nucleic acid that encodes an exogenous agent. In some embodiments, the non-cell particle contains the exogenous agent. In some embodiments, the non-cell particle contains a nucleic acid that encodes an exogenous agent. Reference to the coding sequence of the nucleic acid encoding the exogenous agent also is referred to herein as a payload gene. In some embodiments, the exogenous agent or the nucleic acid encoding the exogenous agent are present in the lumen of the non-cell particle [0438] In some embodiments, the exogenous agent is a protein or a nucleic acid (e.g., a DNA, a chromosome (e.g. a human artificial chromosome), an RNA, e.g., an mRNA or miRNA). In some embodiments, the exogenous agent comprises or encodes a membrane protein. In some embodiments, the exogenous agent comprises or encodes a therapeutic agent. In some embodiments, the therapeutic agent is chosen from one or more of a protein, e.g., an enzyme, a transmembrane protein, a receptor, or an antibody; a nucleic acid, e.g., DNA, a chromosome (e.g. a human artificial chromosome), RNA, mRNA, siRNA, or miRNA; or a small molecule. [0439] In some embodiments, the non-cell particle or pharmaceutical composition delivers to a target cell at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 96%, 97%, 98%, or 99% of the exogenous agent (e.g., an exogenous agent comprising or encoding a therapeutic agent) comprised by the non-cell particle. In some embodiments, the non-cell particle, e.g., fusosome, that contacts, e.g., fuses, with the target cell(s) delivers to the target cell an average of at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 96%, 97%, 98%, or 99% of the exogenous agent (e.g., an exogenous agent comprising or encoding a therapeutic agent) comprised by the non-cell particles, e.g., fusosomes, that contact, e.g., fuse, with the target cell(s). In some embodiments, the non-cell particle composition delivers to a target tissue at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 96%, 97%, 98%, or 99% of the exogenous agent (e.g., an exogenous agent comprising or encoding a therapeutic agent) comprised by the non-cell particle compositions. [0440] In some embodiments, the exogenous agent is not expressed naturally in the cell from which the non-cell particle is derived. In some embodiments, the exogenous agent is expressed naturally in the cell from which the non-cell particle is derived. In some embodiments, the exogenous agent is loaded into the non-cell particle via expression in the cell from which the non-cell particle is derived (e.g. expression from DNA or mRNA introduced via transfection, transduction, or electroporation). In some embodiments, the exogenous is expressed from DNA integrated into the genome or maintained episosomally. In some embodiments, expression of the exogenous agent is constitutive. In some embodiments, expression of the exogenous agent is induced. In some embodiments, expression of the exogenous agent is induced immediately prior to generating the non-cell particle. In some embodiments, expression of the exogenous agent is induced at the same time as expression of the fusogen. [0441] In some embodiments, the exogenous agent is loaded into the non-cell particle via electroporation into the non-cell particle itself or into the cell from which the non-cell particle is derived. In some embodiments, the exogenous agent is loaded into the non-cell particle via transfection (e.g., of a DNA or mRNA encoding the exogenous agent) into the non-cell particle itself or into the cell from which the non-cell particle is derived. [0442] In some embodiments, the exogenous agent may include one or more nucleic acid sequences, one or more polypeptides, a combination of nucleic acid sequences and/or polypeptides, one or more organelles, and any combination thereof. In some embodiments, the exogenous agent may include one or more cellular components. In some embodiments, the exogenous agent includes one or more cytosolic and/or nuclear components. [0443] In some embodiments, the non-cell particle contains an exogenous agent that is a nucleic acid or contains a nucleic acid encoding the exogenous agent. In some embodiments, the nucleic acid is operatively linked to a “positive target cell-specific regulatory element” (or positive TCSRE). In some embodiments, the positive TCSRE is a functional nucleic acid sequence. In some embodiments, the positive TCSRE comprises a promoter or enhancer. In some embodiments, the TCSRE is a nucleic acid sequence that increases the level of an exogenous agent in a target cell. In some embodiments, the positive target cell-specific regulatory element comprises a T cell-specific promoter, a T cell-specific enhancer, a T cell- specific splice site, a T cell-specific site extending half-life of an RNA or protein, a T cell- specific mRNA nuclear export promoting site, a T cell-specific translational enhancing site, or a T cell-specific post-translational modification site. In some embodiments, the T cell-specific promoter is a promoter described in Immgen consortium, herein incorporated by reference in its entirety, e.g., the T cell-specific promoter is an IL2RA (CD25), LRRC32, FOXP3, or IKZF2 promoter. In some embodiments, the T cell-specific promoter or enhancer is a promoter or enhancer described in Schmidl et a , Blood. 2014 Apr 24;123(17):e68-78., herein incorporated by reference in its entirety. In some embodiments, the T cell-specific promoter is a transcriptionally active fragment of any of the foregoing. In some embodiments, the T-cell specific promoter is a variant having at least 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99% identity to any of the foregoing. [0444] In some embodiments, the non-cell particle contains an exogenous agent that is a nucleic acid or contains a nucleic acid encoding the exogenous agent. In some embodiments, the nucleic acid is operatively linked to a “negative target cell-specific regulatory element” (or negative TCSRE). In some embodiments, the negative TCSRE is a functional nucleic acid sequence. In some embodiments, the negative TCSRE is a miRNA recognition site that causes degradation of inhibition of the non-cell particle in a non-target cell. In some embodiments, the exogenous agent is operatively linked to a “non-target cell-specific regulatory element” (or NTCSRE). In some embodiments, the NTCSRE comprises a nucleic acid sequence that decreases the level of an exogenous agent in a non-target cell compared to in a target cell. In some embodiments, the NTCSRE comprises a non-target cell-specific miRNA recognition sequence, non-target cell-specific protease recognition site, non-target cell-specific ubiquitin ligase site, non-target cell-specific transcriptional repression site, or non-target cell-specific epigenetic repression site. In some embodiments, the NTCSRE comprises a tissue-specific miRNA recognition sequence, tissue-specific protease recognition site, tissue-specific ubiquitin ligase site, tissue-specific transcriptional repression site, or tissue-specific epigenetic repression site. In some embodiments, the NTCSRE comprises a non-target cell-specific miRNA recognition sequence, non-target cell-specific protease recognition site, non-target cell-specific ubiquitin ligase site, non-target cell-specific transcriptional repression site, or non-target cell- specific epigenetic repression site. In some embodiments, the NTCSRE comprises a non-target cell-specific miRNA recognition sequence and the miRNA recognition sequence is able to be bound by one or more of miR31, miR363, or miR29c. In some embodiments, the NTCSRE is situated or encoded within a transcribed region encoding the exogenous agent, optionally wherein an RNA produced by the transcribed region comprises the miRNA recognition sequence within a UTR or coding region. A. Nucleic Acids [0445] In some embodiments, the exogenous agent may include a nucleic acid. For example, the exogenous agent may comprise RNA to enhance expression of an endogenous protein, or a siRNA or miRNA that inhibits protein expression of an endogenous protein. For example, the endogenous protein may modulate structure or function in the target cells. In some embodiments, the exogenous agent may include a nucleic acid encoding an engineered protein that modulates structure or function in the target cells In some embodiments the exogenous agent is a nucleic acid that targets a transcriptional activator that modulate structure or function in the target cells [0446] In some embodiments, a non-cell particle described herein comprises a nucleic acid, e.g., RNA or DNA. In some embodiments, the nucleic acid is, comprises, or consists of one or more natural nucleic acid residues. In some embodiments, the nucleic acid is, comprises, or consists of one or more nucleic acid analogs. In some embodiments, the nucleic acid has a nucleotide sequence that encodes a functional gene product such as an RNA or protein. In some embodiments, the nucleic acid includes one or more introns. In some embodiments, nucleic acids are prepared by one or more of isolation from a natural source, enzymatic synthesis by polymerization based on a complementary template (in vivo or in vitro), reproduction in a recombinant cell or system, and chemical synthesis. In some embodiments, the nucleic acid is at least 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 1 10, 120, 130, 140, 150, 160, 170, 180, 190, 20, 225, 250, 275, 300, 325, 350, 375, 400, 425, 450, 475, 500, 600, 700, 800, 900, 1000, 1500, 2000, 2500, 3000, 3500, 4000, 4500, 5000 or more residues long. In some embodiments, the nucleic acid is partly or wholly single stranded; in some embodiments, the nucleic acid is partly or wholly double stranded. In some embodiments the nucleic acid has a nucleotide sequence comprising at least one element that encodes, or is the complement of a sequence that encodes, a polypeptide. The nucleic acid may include variants, e.g., having an overall sequence identity with a reference nucleic acid of at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, or 99%. In some embodiments, a variant nucleic acid does not share at least one characteristic sequence element with a reference nucleic acid. In some embodiments, a variant nucleic acid shares one or more of the biological activities of the reference nucleic acid. In some embodiments, a nucleic acid variant has a nucleic acid sequence that is identical to that of the reference but for a small number of sequence alterations at particular positions. In some embodiments, fewer than about 20%, about 15%, about 10%, about 9%, about 8%, about 7%, about 6%, about 5%, about 4%, about 3%, or about 2% of the residues in a variant are substituted, inserted, or deleted, as compared to the reference. In some embodiments, a variant nucleic acid comprises about 10, about 9, about 8, about 7, about 6, about 5, about 4, about 3, about 2, or about 1 substituted residue as compared to a reference. In some embodiments, a variant nucleic acid comprises a very small number (e.g., fewer than about 5, about 4, about 3, about 2, or about 1) number of substituted, inserted, or deleted, functional residues that participate in a particular biological activity relative to the reference. In some embodiments, a variant nucleic acid comprises not more than about 15, about 12, about 9, about 3, or about 1 addition or deletion, and, in some embodiments, comprises no additions or deletions, as compared to the reference. In some embodiments, a variant nucleic acid comprises fewer than about 27, about 24, about 21, about 18, about 15, about 12, about 9, about 6, about 3, or fewer than about 9, about 6, about 3, or about 2 additions or deletions as compared to the reference. [0447] In some embodiments, the exogenous agent includes a nucleic acid, e.g., DNA, nDNA (nuclear DNA), mtDNA (mitochondrial DNA), protein coding DNA, gene, operon, chromosome, genome, transposon, retrotransposon, viral genome, intron, exon, modified DNA, mRNA (messenger RNA), tRNA (transfer RNA), modified RNA, microRNA, siRNA (small interfering RNA), tmRNA (transfer messenger RNA), rRNA (ribosomal RNA), mtRNA (mitochondrial RNA), snRNA (small nuclear RNA), small nucleolar RNA (snoRNA), SmY RNA (mRNA trans-splicing RNA), gRNA (guide RNA), TERC (telomerase RNA component), aRNA (antisense RNA), cis-NAT (Cis-natural antisense transcript), CRISPR RNA (crRNA), IncRNA (long noncoding RNA), piRNA (piwi-interacting RNA), shRNA (short hairpin RNA), tasiRNA (trans-acting siRNA), eRNA (enhancer RNA), satellite RNA, pcRNA (protein coding RNA), dsRNA (double stranded RNA), RNAi (interfering RNA), circRNA (circular RNA), reprograrnming RNAs, aptamers, and any combination thereof. In some embodiments, the nucleic acid is a wild-type nucleic acid. In some embodiments, the protein is a mutant nucleic acid. In some embodiments the nucleic acid is a fusion or chimera of multiple nucleic acid sequences [0448] In embodiments, the nucleic acid encodes one or more (e.g. two or more) inhibitory RNA molecules directed against one or more RNA targets. An inhibitory RNA molecule can be, e.g., a miRNA or an shRNA. In some embodiments, the inhibitory molecule can be a precursor of a miRNA, such as for example, a Pri-miRNA or a Pre-miRNA, or a precursor of an shRNA. In some embodiments, the inhibitory molecule can be an artificially derived miRNA or shRNA. In other embodiments, the inhibitory RNA molecule can be a dsRNA (either transcribed or artificially introduced) that is processed into an siRNA or the siRNA itself. In some embodiments, the inhibitory RNA molecule can be a miRNA or shRNA that has a sequence that is not found in nature, or has at least one functional segment that is not found in nature, or has a combination of functional segments that are not found in nature. In illustrative embodiments, at least one or all of the inhibitory RNA molecules are miR-l55. In some embodiments, a retroviral vector described herein encodes two or more inhibitory RNA molecules directed against one or more RNA targets. Two or more inhibitory RNA molecules, in some embodiments, can be directed against different targets. In other embodiments, the two or more inhibitory RNA molecules are directed against the same target. In some embodiments, the exogenous agent comprises a shRNA. A shRNA (short hairpin RNA) can comprise a double-stranded structure that is formed by a single self complementary RNA strand. shRNA constructs can comprise a nucleotide sequence identical to a portion, of either coding or non-coding sequence, of a target gene. RNA sequences with insertions, deletions, and single point mutations relative to the target sequence can also be used. Greater than 90% sequence identity, or even 100% sequence identity, between the inhibitory RNA and the portion of the target gene can be used. In certain embodiments, the length of the duplex-forming portion of an shRNA is at least 20, 21 or 22 nucleotides in length, e.g., corresponding in size to RNA products produced by Dicer-dependent cleavage. In certain embodiments, the shRNA construct is at least 25, 50, 100, 200, 300 or 400 bases in length. In certain embodiments, the shRNA construct is 400-800 bases in length. shRNA constructs are highly tolerant of variation in loop sequence and loop size. In embodiments, a retroviral vector that encodes an siRNA, an miRNA, an shRNA, or a ribozyme comprises one or more regulatory sequences, such as, for example, a strong constitutive pol III, e.g., human U6 snRNA promoter, the mouse U6 snRNA promoter, the human and mouse H l RNA promoter and the human tRNA-val promoter, or a strong constitutive pol II promoter. B. Polypeptides [0449] In some embodiments, the non-cell particle contains a nucleic acid that encodes a protein exogenous agent (also referred to as a “payload gene encoding an exogenous agent.”). In some embodiments, a non-cell particle described herein comprises an exogenous agent which is or comprises a protein. [0450] In some embodiments, the protein may include moieties other than amino acids (e.g., may be glycoproteins, proteoglycans, etc.) and/or may be otherwise processed or modified. In some embodiments, the protein can sometimes include more than one polypeptide chain, for example linked by one or more disulfide bonds or associated by other means. [0451] In some embodiments, the protein may contain L-amino acids, D-amino acids, or both and may contain any of a variety of amino acid modifications or analogs. In some embodiments, proteins may comprise natural amino acids, non-natural amino acids, synthetic amino acids, and combinations thereof. In some embodiments, proteins are antibodies, antibody fragments, biologically active portions thereof, and/or characteristic portions thereof. In some embodiments, a polypeptide may include its variants, e.g., having an overall sequence identity with a reference polypeptide of at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, or 99%. In some embodiments, a variant polypeptide does not share at least one characteristic sequence element with a reference polypeptide. In some embodiments, a variant polypeptide shares one or more of the biological activities of the reference polypeptide. In some embodiments, a polypeptide variant has an amino acid sequence that is identical to that of the reference but for a small number of sequence alterations at particular positions. In some embodiments, fewer than about 20%, about 15%, about 10%, about 9%, about 8%, about 7%, about 6%, about 5%, about 4%, about 3%, or about 2% of the residues in a variant are substituted, inserted, or deleted, as compared to the reference. In some embodiments, a variant polypeptide comprises about 10, about 9, about 8, about 7, about 6, about 5, about 4, about 3, about 2, or about 1 substituted residue as compared to a reference. In some embodiments, a variant polypeptide comprises a very small number (e.g., fewer than about 5, about 4, about 3, about 2, or about 1) number of substituted, inserted, or deleted, functional that participate in a particular biological activity relative to the reference. In some embodiments, a variant polypeptide comprises not more than about 5, about 4, about 3, about 2, or about 1 addition or deletion, and, in some embodiments, comprises no additions or deletions, as compared to the reference. In some embodiments, a variant polypeptide comprises fewer than about 25, about 20, about 19, about 18, about 17, about 16, about 15, about 14, about 13, about 10, about 9, about 8, about 7, about 6, and commonly fewer than about 5, about 4, about 3, or about 2 additions or deletions as compared to the reference.In some embodiments, the protein includes a polypeptide, e.g., enzymes, structural polypeptides, signaling polypeptides, regulatory polypeptides, transport polypeptides, sensory polypeptides, motor polypeptides, defense polypeptides, storage polypeptides, transcription factors, antibodies, cytokines, hormones, catabolic polypeptides, anabolic polypeptides, proteolytic polypeptides, metabolic polypeptides, kinases, transferases, hydrolases, lyases, isomerases, ligases, enzyme modulator polypeptides, protein binding polypeptides, lipid binding polypeptides, membrane fusion polypeptides, cell differentiation polypeptides, epigenetic polypeptides, cell death polypeptides, nuclear transport polypeptides, nucleic acid binding polypeptides, reprogramming polypeptides, DNA editing polypeptides, DNA repair polypeptides, DNA recombination polypeptides, transposase polypeptides, DNA integration polypeptides, targeted endonucleases (e.g. Zinc -finger nucleases, transcription-activator-like nucleases (TALENs), cas9 and homologs thereof), recombinases, and any combination thereof. In some embodiments, the protein targets a protein in the cell for degradation. In some embodiments, the protein targets a protein in the cell for degradation by localizing the protein to the proteasome. In some embodiments, the protein is a wild-type protein. In some embodiments, the protein is a mutant protein. [0452] Exemplary protein exogenous agents are described in the following subsections. In some embodiments, a non-cell particle provided herein can include any of such exogenous agents. In particular embodiments, a non-cell particle contains a nucleic acid encoding any of such exogenous agents. a. Cytosolic Proteins [0453] In some embodiments, the exogenous agent comprises a cytosolic protein, e.g., a protein that is produced in the recipient cell and localizes to the recipient cell cytoplasm. In some embodiments, the exogenous agent comprises a secreted protein, e.g., a protein that is produced and secreted by the recipient cell. In some embodiments, the exogenous agent comprises a nuclear protein, e.g., a protein that is produced in the recipient cell and is imported to the nucleus of the recipient cell. In some embodiments, the exogenous agent comprises an organellar protein (e.g., a mitochondrial protein), e.g., a protein that is produced in the recipient cell and is imported into an organelle (e.g., a mitochondrial) of the recipient cell. In some embodiments, the protein is a wild-type protein or a mutant protein. In some embodiments the protein is a fusion or chimeric protein. b. Membrane Proteins [0454] In some embodiments, the exogenous agent comprises a membrane protein. In some embodiments, the membrane protein comprises a chimeric antigen receptor (CAR), a T cell receptor, an integrin, an ion channel, a pore forming protein, a Toll-Like Receptor, an interleukin receptor, a cell adhesion protein, or a transport protein. 1) Chimeric Antigen Receptors (CARs) [0455] In some embodiments, a payload gene described herien encodes a chimeric antigen receptor (CAR) comprising an antigen binding domain. In some embodiments, an exogenous agent described herein comprises a chimeric antigen receptor (CAR) comprising an antigen binding domain. In some embodiments, the payload is or comprises a chimeric antigen receptor (CAR) comprising an antigen binding domain. In some embodiments, the CAR is or comprises a first generation CAR comprising an antigen binding domain, a transmembrane domain, and signaling domain (e.g., one, two or three signaling domains). In some embodiments, the CAR comprises a third generation CAR comprising an antigen binding domain, a transmembrane domain, and at least three signaling domains. In some embodiments, a fourth generation CAR comprising an antigen binding domain, a transmembrane domain, three or four signaling domains, and a domain which upon successful signaling of the CAR induces expression of a cytokine gene. In some embodiments, the antigen binding domain is or comprises an scFv or Fab. [0456] In some embodiments, the antigen binding domain targets an antigen characteristic of a cell type. In some embodiments, the antigen binding domain targets an antigen characteristic of a neoplastic cell. In some embodiments, the antigen characteristic of a neoplastic cell is selected from a cell surface receptor, an ion channel-linked receptor, an enzyme-linked receptor, a G protein-coupled receptor, receptor tyrosine kinase, tyrosine kinase associated receptor, receptor-like tyrosine phosphatase, receptor serine/ threonine kinase, receptor guanylyl cyclase, histidine kinase associated receptor, Epidermal Growth Factor Receptors (EGFR) (including ErbB1/EGFR, ErbB2/HER2, ErbB3/HER3, and ErbB4/HER4), Fibroblast Growth Factor Receptors (FGFR) (including FGF1, FGF2, FGF3, FGF4, FGF5, FGF6, FGF7, FGF18, and FGF21) Vascular Endothelial Growth Factor Receptors (VEGFR) (including VEGF-A, VEGF- B, VEGF-C, VEGF-D, and PIGF), RET Receptor and the Eph Receptor Family (including EphA1, EphA2, EphA3, EphA4, EphA5, EphA6, EphA7, EphA8, EphA9, EphA10, EphB1, EphB2. EphB3, EphB4, and EphB6), CXCR1, CXCR2, CXCR3, CXCR4, CXCR6, CCR1, CCR2, CCR3, CCR4, CCR5, CCR6, CCR8, CFTR, CIC-1, CIC-2, CIC-4, CIC-5, CIC-7, CIC- Ka, CIC-Kb, Bestrophins, TMEM16A, GABA receptor, glycin receptor, ABC transporters, NAV1.1, NAV1.2, NAV1.3, NAV1.4, NAV1.5, NAV1.6, NAV1.7, NAV1.8, NAV1.9, sphingosin-1-phosphate receptor (S1P1R), NMDA channel, transmembrane protein, multispan transmembrane protein, T-cell receptor motifs; T-cell alpha chains; T-cell b chains; T-cell g chains; T-cell d chains; CCR7; CD3; CD4; CD5; CD7; CD8; CD11b; CD11c; CD16; CD19; CD20; CD21 ; CD22; CD25; CD28; CD34; CD35; CD40; CD45RA; CD45RO; CD52; CD56; CD62L; CD68; CD80; CD95; CD117; CD127; CD133; CD137 (4-1 BB); CD163; F4/80; IL- 4Ra; Sca-1 ; CTLA-4; GITR; GARP; LAP; granzyme B; LFA-1 ; transferrin receptor; NKp46, perforin, CD4+; Th1; Th2; Th17; Th40; Th22; Th9; Tfh, Canonical Treg. FoxP3+; Tr1; Th3; Treg17; TREG; CDCP1, NT5E, EpCAM, CEA, gpA33, Mucins, TAG-72, Carbonic anhydrase IX, PSMA, Folate binding protein, Gangliosides (e.g., CD2, CD3, GM2), Lewis-g 2 , VEGF, VEGFR 1/2/3, aVb3, a5b1, ErbB1/EGFR, ErbB1/HER2, ErB3, c-MET, IGF1R, EphA3, TRAIL-R1, TRAIL-R2, RANKL, FAP, Tenascin, PDL-1, BAFF, HDAC, ABL, FLT3, KIT, MET, RET, IL-1b, ALK, RANKL, mTOR, CTLA-4, IL-6, IL-6R, JAK3, BRAF, PTCH, Smoothened, PIGF, ANPEP, TIMP1, PLAUR, PTPRJ, LTBR, or ANTXR1, Folate receptor alpha (FRa), ERBB2 (Her2/neu), EphA2, IL-13Ra2, epidermal growth factor receptor (EGFR), Mesothelin, TSHR, CD19, CD123, CD22, CD30, CD171, CS-1, CLL-1, CD33, EGFRvIII , GD2, GD3, BCMA, MUC16 (CA125), L1CAM, LeY, MSLN, IL13Ra1, L1-CAM, Tn Ag, prostate specific membrane antigen (PSMA), ROR1, FLT3, FAP, TAG72, CD38, CD44v6, CEA, EPCAM, B7H3, KIT, interleukin-11 receptor a (IL-11Ra), PSCA, PRSS21, VEGFR2, LewisY, CD24, platelet-derived growth factor receptor-beta (PDGFR-beta), SSEA-4, CD20, MUC1, NCAM, Prostase, PAP, ELF2M, Ephrin B2, IGF-1 receptor, CAIX, LMP2, gplOO, bcr- abl, tyrosinase, Fucosyl GM1, sLe, GM3, TGS5, HMWMAA, o-acetyl-GD2, Folate receptor beta, TEM1/CD248, TEM7R, CLDN6, GPRC5D, CXORF61, CD97, CD179a, ALK, Polysialic acid, PLACl, GloboH, NY-BR-1, UPK2, HAVCR1, ADRB3, PANX3, GPR20, LY6K, OR51E2, TARP, WT1, NY-ESO-1, LAGE-la, MAGE-A1, legumain, HPV E6, E7, ETV6-AML, sperm protein 17, XAGE1, Tie 2, MAD-CT-1, MAD-CT-2, Major histocompatibility complex class I-related gene protein (MR1), urokinase-type plasminogen activator receptor (uPAR), Fos- related antigen 1, p53, p53 mutant, prostein, survivin, telomerase, PCTA-1/Galectin 8, MelanA/MART1, Ras mutant, hTERT, sarcoma translocation breakpoints, ML-IAP, ERG (TMPRSS2 ETS fusion gene), NA17, PAX3, Androgen receptor, Cyclin B1, MYCN, RhoC, TRP-2, CYPIB I, BORIS, SART3, PAX5, OY-TES1, LCK, AKAP-4, SSX2, RAGE-1, human telomerase reverse transcriptase, RU1, RU2, intestinal carboxyl esterase, mut hsp70-2, CD79a, CD79b, CD72, LAIR1, FCAR, LILRA2, CD300LF, CLEC12A, BST2, EMR2, LY75, GPC3, FCRL5, IGLL1, a neoantigen, CD133, CD15, CD184, CD24, CD56, CD26, CD29, CD44, HLA-A, HLA-B, HLA-C, (HLA-A,B,C) CD49f, CD151 CD340, CD200, tkrA, trkB, or trkC, or an antigenic fragment or antigenic portion thereof. [0457] In some embodiments, the antigen binding domain targets an antigen characteristic of a T cell. In some embodiments, the antigen characteristic of a T cell is selected from a cell surface receptor, a membrane transport protein (e.g., an active or passive transport protein such as, for example, an ion channel protein, a pore-forming protein, etc.), a transmembrane receptor, a membrane enzyme, and/or a cell adhesion protein characteristic of a T cell. In some embodiments, an antigen characteristic of a T cell may be a G protein-coupled receptor, receptor tyrosine kinase, tyrosine kinase associated receptor, receptor-like tyrosine phosphatase, receptor serine/ threonine kinase, receptor guanylyl cyclase, histidine kinase associated receptor, AKT1; AKT2; AKT3; ATF2; BCL10; CALM1; CD3D (CD3d); CD3E (CD3e); CD3G (CD3g); CD4; CD8; CD28; CD45; CD80 (B7-1); CD86 (B7-2); CD247 (CD3z); CTLA4 (CD152); ELK1; ERK1 (MAPK3); ERK2; FOS; FYN; GRAP2 (GADS); GRB2; HLA-DRA; HLA-DRB1; HLA- DRB3; HLA-DRB4; HLA-DRB5; HRAS; IKBKA (CHUK); IKBKB; IKBKE; IKBKG (NEMO); IL2; ITPR1; ITK; JUN; KRAS2; LAT; LCK; MAP2K1 (MEK1); MAP2K2 (MEK2); MAP2K3 (MKK3); MAP2K4 (MKK4); MAP2K6 (MKK6); MAP2K7 (MKK7); MAP3K1 (MEKK1); MAP3K3; MAP3K4; MAP3K5; MAP3K8; MAP3K14 (NIK); MAPK8 (JNK1); MAPK9 (JNK2); MAPK10 (JNK3); MAPK11 (p38b); MAPK12 (p38g); MAPK13 (p38d); MAPK14 (p38a); NCK; NFAT1; NFAT2; NFKB1; NFKB2; NFKBIA; NRAS; PAK1; PAK2; PAK3; PAK4; PIK3C2B; PIK3C3 (VPS34); PIK3CA; PIK3CB; PIK3CD; PIK3R1; PKCA; PKCB; PKCM; PKCQ; PLCY1; PRF1 (Perforin); PTEN; RAC1; RAF1; RELA; SDF1; SHP2; SLP76; SOS; SRC; TBK1; TCRA; TEC; TRAF6; VAV1; VAV2; or ZAP70. [0458] In some embodiments, the antigen binding domain targets an antigen characteristic of a disorder. In some embodiments, the antigen binding domain targets an antigen characteristic of an autoimmune or inflammatory disorder. In some embodiments, the autoimmune or inflammatory disorder is selected from chronic graft-vs-host disease (GVHD), lupus, arthritis, immune complex glomerulonephritis, goodpasture, uveitis, hepatitis, systemic sclerosis or scleroderma, type I diabetes, multiple sclerosis, cold agglutinin disease, Pemphigus vulgaris, Grave's disease, autoimmune hemolytic anemia, Hemophilia A, Primary Sjogren's Syndrome, thrombotic thrombocytopenia purrpura, neuromyelits optica, Evan's syndrome, IgM mediated neuropathy, cyroglobulinemia, dermatomyositis, idiopathic thrombocytopenia, ankylosing spondylitis, bullous pemphigoid, acquired angioedema, chronic urticarial, antiphospholipid demyelinating polyneuropathy, and autoimmune thrombocytopenia or neutropenia or pure red cell aplasias, while exemplary non-limiting examples of alloimmune diseases include allosensitization (see, for example, Blazar et al., 2015, Am. J. Transplant, 15(4):931-41) or xenosensitization from hematopoietic or solid organ transplantation, blood transfusions, pregnancy with fetal allosensitization, neonatal alloimmune thrombocytopenia, hemolytic disease of the newborn, sensitization to foreign antigens such as can occur with replacement of inherited or acquired deficiency disorders treated with enzyme or protein replacement therapy, blood products, and gene therapy. In some embodiments, the antigen characteristic of an an autoimmune or inflammatory disorder is selected from a cell surface receptor, an ion channel- linked receptor, an enzyme-linked receptor, a G protein-coupled receptor, receptor tyrosine kinase, tyrosine kinase associated receptor, receptor-like tyrosine phosphatase, receptor serine/ threonine kinase, receptor guanylyl cyclase, or histidine kinase associated receptor. In some embodiments, a CAR antigen binding domain binds to a ligand expressed on B cells, plasma cells, plasmablasts, CD10, CD19, CD20, CD22, CD24, CD27, CD38, CD45R, CD138, CD319, BCMA, CD28, TNF, interferon receptors, GM-CSF, ZAP-70, LFA-1, CD3 gamma, CD5 or CD2. See US 2003/0077249; WO 2017/058753; WO 2017/058850, the contents of which are herein incorporated by reference. [0459] In some embodiments, the antigen binding domain targets an antigen characteristic of senescent cells, e.g., urokinase-type plasminogen activator receptor (uPAR). In some embodiments, the CAR may be used for treatment or prophylaxis of disorders characterized by the aberrant accumulation of senescent cells, e.g., liver and lung fibrosis, atherosclerosis, diabetes and osteoarthritis. [0460] In some embodiments, the antigen binding domain targets an antigen characteristic of an infectious disease. In some embodiments, wherein the infectious disease is selected from HIV, hepatitis B virus, hepatitis C virus, Human herpes virus, Human herpes virus 8 (HHV-8, Kaposi sarcoma-associated herpes virus (KSHV)), Human T-lymphotrophic virus-1 (HTLV-1), Merkel cell polyomavirus (MCV), Simian virus 40 (SV40), Eptstein-Barr virus, CMV, human papillomavirus. In some embodiments, the antigen characteristic of an infectious disease is selected from a cell surface receptor, an ion channel-linked receptor, an enzyme-linked receptor, a G protein-coupled receptor, receptor tyrosine kinase, tyrosine kinase associated receptor, receptor-like tyrosine phosphatase, receptor serine/ threonine kinase, receptor guanylyl cyclase, histidine kinase associated receptor, HIV Env, gpl20, or CD4-induced epitope on HIV-1 Env. [0461] In some embodiments, the CAR transmembrane domain comprises at least a transmembrane region of the alpha, beta or zeta chain of a T cell receptor, CD28, CD3 epsilon, CD45, CD4, CD5, CD8, CD9, CD16, CD22, CD33, CD37, CD64, CD80, CD86, CD134, CD137, CD154, or functional variant thereof. In some embodiments, the transmembrane domain comprises at least a transmembrane region(s) of CD8a, CD8b, 4-1BB/CD137, CD28, CD34, CD4, FceRIg, CD16, OX40/CD134, CD3z, CD3e, CD3g, CD3d, TCRa, TCRb, TCRz, CD32, CD64, CD64, CD45, CD5, CD9, CD22, CD37, CD80, CD86, CD40, CD40L/CD154, VEGFR2, FAS, and FGFR2B, or functional variant thereof. [0462] In some embodiments, the CAR comprises at least one signaling domain selected from one or more of B7-1/CD80; B7-2/CD86; B7-H1/PD-L1; B7-H2; B7-H3; B7-H4; B7-H6; B7-H7; BTLA/CD272; CD28; CTLA-4; Gi24/VISTA/B7-H5; ICOS/CD278; PD-1; PD-L2/B7- DC; PDCD6); 4-1BB/TNFSF9/CD137; 4-1BB Ligand/TNFSF9; BAFF/BLyS/TNFSF13B; BAFF R/TNFRSF13C; CD27/TNFRSF7; CD27 Ligand/TNFSF7; CD30/TNFRSF8; CD30 Ligand/TNFSF8; CD40/TNFRSF5; CD40/TNFSF5; CD40 Ligand/TNFSF5; DR3/TNFRSF25; GITR/TNFRSF18; GITR Ligand/TNFSF18; HVEM/TNFRSF14; LIGHT/TNFSF14; Lymphotoxin-alpha/TNF-beta; OX40/TNFRSF4; OX40 Ligand/TNFSF4; RELT/TNFRSF19L; TACI/TNFRSF13B; TL1A/TNFSF15; TNF-alpha; TNF RII/TNFRSF1B); 2B4/CD244/SLAMF4; BLAME/SLAMF8; CD2; CD2F-10/SLAMF9; CD48/SLAMF2; CD58/LFA-3; CD84/SLAMF5; CD229/SLAMF3; CRACC/SLAMF7; NTB-A/SLAMF6; SLAM/CD150); CD2; CD7; CD53; CD82/Kai-1; CD90/Thy1; CD96; CD160; CD200; CD300a/LMIR1; HLA Class I; HLA-DR; Ikaros; Integrin alpha 4/CD49d; Integrin alpha 4 beta 1; Integrin alpha 4 beta 7/LPAM-1; LAG-3; TCL1A; TCL1B; CRTAM; DAP12; Dectin- 1/CLEC7A; DPPIV/CD26; EphB6; TIM-1/KIM-1/HAVCR; TIM-4; TSLP; TSLP R; lymphocyte function associated antigen-1 (LFA-1); NKG2C, a CD3 zeta domain, an immunoreceptor tyrosine-based activation motif (ITAM), CD27, CD28, 4-1BB, CD134/OX40, CD30, CD40, PD-1, ICOS, lymphocyte function-associated antigen-1 (LFA-1), CD2, CD7, LIGHT, NKG2C, B7-H3, a ligand that specifically binds with CD83, or functional fragment thereof. [0463] In some embodiments, the CAR comprises a CD3 zeta domain or an immunoreceptor tyrosine-based activation motif (ITAM), or functional variant thereof. In some embodiments, the CAR comprises (i) a CD3 zeta domain, or an immunoreceptor tyrosine-based activation motif (ITAM), or functional variant thereof; and (ii) a CD28 domain, or a 4-1BB domain, or functional variant thereof. In some embodiments, the CAR comprises a (i) a CD3 zeta domain, or an immunoreceptor tyrosine-based activation motif (ITAM), or functional variant thereof; (ii) a CD28 domain or functional variant thereof; and (iii) a 4-1BB domain, or a CD134 domain, or functional variant thereof. In some embodiments, the CAR comprises (i) a CD3 zeta domain, or an immunoreceptor tyrosine-based activation motif (ITAM), or functional variant thereof; (ii) a CD28 domain, or a 4-1BB domain, or functional variant thereof, and/or (iii) a 4-1BB domain, or a CD134 domain, or functional variant thereof. In some embodiments, the CAR comprises a (i) a CD3 zeta domain, or an immunoreceptor tyrosine-based activation motif (ITAM), or functional variant thereof; (ii) a CD28 domain or functional variant thereof; (iii) a 4-1BB domain, or a CD134 domain, or functional variant thereof; and (iv) a cytokine or costimulatory ligand transgene. [0464] In some embodiments, the CAR further comprises one or more spacers, e.g., wherein the spacer is a first spacer between the antigen binding domain and the transmembrane domain. In some embodiments, the first spacer includes at least a portion of an immunoglobulin constant region or variant or modified version thereof. In some embodiments, the spacer is a second spacer between the transmembrane domain and a signaling domain. In some embodiments, the second spacer is an oligopeptide, e.g., wherein the oligopeptide comprises glycine-serine doublets. [0465] In some embodiments the exogenous agent is or comprises a CAR, e.g., a first generation CAR or a nucleic acid encoding a first generation CAR. In some embodiments, a first generation CAR comprises an antigen binding domain, a transmembrane domain, and signaling domain. In some embodiments a signaling domain mediates downstream signaling during T cell activation. [0466] In some embodiments the exogenous agent is or comprises a second generation CAR or a nucleic acid encoding a second generation CAR. In some embodiments a second generation CAR comprises an antigen binding domain, a transmembrane domain, and two signaling domains. In some embodiments a signaling domain mediates downstream signaling during T cell activation. In some embodiments a signaling domain is a costimulatory domain. In some embodiments, a costimulatory domain enhances cytokine production, CAR T cell proliferation, and or CAR T cell persistence during T cell activation. [0467] In some embodiments the exogenous agent is or comprises a third generation CAR or a nucleic acid encoding a third generation CAR. In some embodiments, a third generation CAR comprises an antigen binding domain, a transmembrane domain, and at least three signaling domains. In some embodiments a signaling domain mediates downstream signaling during T cell activation. In some embodiments a signaling domain is a costimulatory domain. In some embodiments, a costimulatory domain enhances cytokine production, CAR T cell proliferation, and or CAR T cell persistence during T cell activation. In some embodiments, a third generation CAR comprises at least two costimulatory domains. In some embodiments, the at least two costimulatory domains are not the same. [0468] In some embodiments the exogenous is or comprises a fourth generation CAR or a nucleic acid encoding a fourth generation CAR. In some embodiments a fourth generation CAR comprises an antigen binding domain, a transmembrane domain, and at least two, three, or four signaling domains. In some embodiments a signaling domain mediates downstream signaling during T cell activation. In some embodiments a signaling domain is a costimulatory domain. In some embodiments, a costimulatory domain enhances cytokine production, CAR T cell proliferation, and or CAR T cell persistence during T cell activation. [0469] In some embodiments, a first, second, third, or fourth generation CAR further comprises a domain which upon successful signaling of the CAR induces expression of a cytokine gene. In some embodiments, a cytokine gene is endogenous or exogenous to a target cell comprising a CAR which comprises a domain which upon successful signaling of the CAR induces expression of a cytokine gene. In some embodiments a cytokine gene encodes a pro- inflammatory cytokine. In some embodiments a cytokine gene encodes IL-1, IL-2, IL-9, IL-12, IL-18, TNF, or IFN-gamma, or functional fragment thereof. In some embodiments a domain which upon successful signaling of the CAR induces expression of a cytokine gene is or comprises a transcription factor or functional domain or fragment thereof. In some embodiments a domain which upon successful signaling of the CAR induces expression of a cytokine gene is or comprises a transcription factor or functional domain or fragment thereof. In some embodiments a transcription factor or functional domain or fragment thereof is or comprises a nuclear factor of activated T cells (NFAT), an NF-kB, or functional domain or fragment thereof. See, e.g., Zhang. C. et al., Engineering CAR-T cells. Biomarker Research. 5:22 (2017); WO 2016126608; Sha, H. et al. Chimaeric antigen receptor T-cell therapy for tumour immunotherapy. Bioscience Reports Jan 27, 2017, 37 (1). [0470] In some embodiments, a CAR antigen binding domain is or comprises an antibody or antigen-binding portion thereof. In some embodiments, a CAR antigen binding domain is or comprises an scFv or Fab. In some embodiments a CAR antigen binding domain comprises an scFv or Fab fragment of a T-cell alpha chain antibody; T-cell b chain antibody; T-cell g chain antibody; T-cell d chain antibody; CCR7 antibody; CD3 antibody; CD4 antibody; CD5 antibody; CD7 antibody; CD8 antibody; CD11b antibody; CD11c antibody; CD16 antibody; CD19 antibody; CD20 antibody; CD21 antibody; CD22 antibody; CD25 antibody; CD28 antibody; CD34 antibody; CD35 antibody; CD40 antibody; CD45RA antibody; CD45RO antibody; CD52 antibody; CD56 antibody; CD62L antibody; CD68 antibody; CD80 antibody; CD95 antibody; CD117 antibody; CD127 antibody; CD133 antibody; CD137 (4-1 BB) antibody; CD163 antibody; F4/80 antibody; IL-4Ra antibody; Sca-1 antibody; CTLA-4 antibody; GITR antibody GARP antibody; LAP antibody; granzyme B antibody; LFA-1 antibody; MR1 antibody; uPAR antibody; or transferrin receptor antibody. [0471] In some embodiments, an antigen binding domain binds to a cell surface antigen of a cell. In some embodiments, a cell surface antigen is characteristic of one type of cell. In some embodiments, a cell surface antigen is characteristic of more than one type of cell. [0472] In some embodiments a CAR antigen binding domain binds a cell surface antigen characteristic of a T cell. In some embodiments, an antigen characteristic of a T cell may be a cell surface receptor, a membrane transport protein (e.g., an active or passive transport protein such as, for example, an ion channel protein, a pore-forming protein, etc.), a transmembrane receptor, a membrane enzyme, and/or a cell adhesion protein characteristic of a T cell. In some embodiments, an antigen characteristic of a T cell may be a G protein-coupled receptor, receptor tyrosine kinase, tyrosine kinase associated receptor, receptor-like tyrosine phosphatase, receptor serine/ threonine kinase, receptor guanylyl cyclase, or histidine kinase associated receptor. [0473] In some embodiments, an antigen characteristic of a T cell may be a T cell receptor. In some embodiments, a T cell receptor may be AKT1; AKT2; AKT3; ATF2; BCL10; CALM1; CD3D (CD3d); CD3E (CD3e); CD3G (CD3g); CD4; CD8; CD28; CD45; CD80 (B7-1); CD86 (B7-2); CD247 (CD3z); CTLA4 (CD152); ELK1; ERK1 (MAPK3); ERK2; FOS; FYN; GRAP2 (GADS); GRB2; HLA-DRA; HLA-DRB1; HLA-DRB3; HLA-DRB4; HLA-DRB5; HRAS; IKBKA (CHUK); IKBKB; IKBKE; IKBKG (NEMO); IL2; ITPR1; ITK; JUN; KRAS2; LAT; LCK; MAP2K1 (MEK1); MAP2K2 (MEK2); MAP2K3 (MKK3); MAP2K4 (MKK4); MAP2K6 (MKK6); MAP2K7 (MKK7); MAP3K1 (MEKK1); MAP3K3; MAP3K4; MAP3K5; MAP3K8; MAP3K14 (NIK); MAPK8 (JNK1); MAPK9 (JNK2); MAPK10 (JNK3); MAPK11 (p38b); MAPK12 (p38g); MAPK13 (p38d); MAPK14 (p38a); NCK; NFAT1; NFAT2; NFKB1; NFKB2; NFKBIA; NRAS; PAK1; PAK2; PAK3; PAK4; PIK3C2B; PIK3C3 (VPS34); PIK3CA; PIK3CB; PIK3CD; PIK3R1; PKCA; PKCB; PKCM; PKCQ; PLCY1; PRF1 (Perforin); PTEN; RAC1; RAF1; RELA; SDF1; SHP2; SLP76; SOS; SRC; TBK1; TCRA; TEC; TRAF6; VAV1; VAV2; or ZAP70. [0474] In some embodiments a CAR comprises a signaling domain which is a costimulatory domain. In some embodiments a CAR comprises a second costimulatory domain. In some embodiments a CAR comprises at least two costimulatory domains. In some embodiments a CAR comprises at least three costimulatory domains. In some embodiments a CAR comprises a costimulatory domain selected from one or more of CD27, CD28, 4-1BB, CD134/OX40, CD30, CD40, PD-1, ICOS, lymphocyte function-associated antigen-1 (LFA-1), CD2, CD7, LIGHT, NKG2C, B7-H3, a ligand that specifically binds with CD83. [0475] In addition to the CARs described herein, various chimeric antigen receptors and nucleotide sequences encoding the same are known in the art and would be suitable for fusosomal delivery and reprogramming of target cells in vivo and in vitro as described herein. See, e.g., WO2013040557; WO2012079000; WO2016030414; Smith T, et al., Nature Nanotechnology. 2017. DOI: 10.1038/NNANO.2017.57, the disclosures of which are herein incorporated by reference. [0476] In some embodiments a non-cell particle comprising a CAR or a nucleic acid encoding a CAR (e.g., a DNA, a gDNA, a cDNA, an RNA, a pre-MRNA, an mRNA, an miRNA, an siRNA, etc.) is delivered to a target cell. In some embodiments the target cell is an effector cell, e.g., a cell of the immune system that expresses one or more Fc receptors and mediates one or more effector functions. In some embodiments, a target cell may include, but may not be limited to, one or more of a monocyte, macrophage, neutrophil, dendritic cell, eosinophil, mast cell, platelet, large granular lymphocyte, Langerhans' cell, natural killer (NK) cell, T lymphocyte (e.g., T cell), a Gamma delta T cell, B lymphocyte (e.g., B cell) and may be from any organism including but not limited to humans, mice, rats, rabbits, and monkeys. C. Small Molecules [0477] In some embodiments, the exogenous agent includes a small molecule, e.g., ions (e.g. Ca 2+ , C1-, Fe 2+ ), carbohydrates, lipids, reactive oxygen species, reactive nitrogen species, isoprenoids, signaling molecules, heme, polypeptide cofactors, electron accepting compounds, electron donating compounds, metabolites, ligands, and any combination thereof. In some embodiments the small molecule is a pharmaceutical that interacts with a target in the cell. In some embodiments the small molecule targets a protein in the cell for degradation. In some embodiments the small molecule targets a protein in the cell for degradation by localizing the protein to the proteasome. In some embodiments that small molecule is a proteolysis targeting chimera molecule (PROTAC). [0478] In some embodiments, the exogenous agent includes a mixture of proteins, nucleic acids, or metabolites, e.g., multiple polypeptides, multiple nucleic acids, multiple small molecules; combinations of nucleic acids, polypeptides, and small molecules; ribonucleoprotein complexes (e.g. Cas9-gRNA complex); multiple transcription factors, multiple epigenetic factors, reprogramming factors (e.g. Oct4, Sox2, cMyc, and Klf4); multiple regulatory RNAs; and any combination thereof. VI. EXEMPLARY FEATURES OF CD24 ASSOCIATED NON-CELL PARTICLES [0479] In some embodiments of any of the aspects described herein, the non-cell particle composition is substantially non-immunogenic. Immunogenicity can be quantified, e.g., as described herein. In some embodiments, the non-cell particle composition comprises elevated levels of an immunosuppressive agent as compared to a reference particle, e.g., an otherwise similar particle but that does not contain exogenous CD24 or a biologically active portion. In some embodiments, the immunosuppressive agent is CD24. In some embodiments, the immunosuppressive agent is CD24 and CD47. In some embodiments, the elevated level is at least 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 2-fold, 3-fold, 5-fold, 10-fold, 20- fold, 50-fold, or 100-fold. In some embodiments, the non-cell particle composition comprises CD24 and CD47 that is absent from the reference particle. [0480] In some embodiments, the non-cell particle composition has a reduction in immunogenicity as measured by a reduction in humoral response following one or more implantation of the non-cell particle derived into an appropriate animal model, e.g., an animal model described herein, compared to a humoral response following one or more implantation of a reference cell, e.g., an unmodified cell otherwise similar to the source cell, into an appropriate animal model, e.g., an animal model described herein. In some embodiments, the reduction in humoral response is measured in a serum sample by an anti-cell antibody titer, e.g., by ELISA. In some embodiments, the serum sample from animals administered the non-cell particle composition has a reduction of 1 %, 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, or more of an anti-cell antibody titer compared to the serum sample from animals administered an unmodified cell. In some embodiments, the serum sample from animals administered the non- cell particle composition has an increased anti-cell antibody titer, e.g., increased by 1%, 2%, 5%, 10%, 20%, 30%, or 40% from baseline, e.g., wherein baseline refers to serum sample from the same animals before administration of the non-cell particle composition. [0481] In some embodiments, immunogenicity of a non-cell particle composition is assayed by a serum inactivation assay (e.g., an assay that detects antibody-mediated neutralization or complement mediated degradation). In some embodiments, non-cell particle are not inactivated by serum or are inactivated at a level below a predetermined value. In some embodiments, serum of a non-cell particle -naive subject (e.g., human or mouse) is contacted with a test non- cell particle composition. In some embodiments, the serum of a subject that has received one or more administrations of non-cell particle, e.g., has received at least two administrations of non- cell particle, is contacted with the test non-cell particle composition. In embodiments, serum- exposed non-cell particles are then tested for ability to deliver a cargo to target cells. In some embodiments, the percent of cells that detectably comprise the cargo after treatment with serum- incubated non-cell particles is at least 50%, 60%, 70%, 80%, 90%, or 95% the percent of cells that detectably comprise the cargo after treatment with positive control non-cell particles not contacted with serum. [0482] In some embodiments, immunogenicity of a non-cell particle composition is assayed by detecting complement activation in response to the non-cell particles. In some embodiments, the non-cell particles do not activate complement, or activate complement at a level below a predetermined value. In some embodiments, serum of a non-cell particle -naive subject (e.g., human or mouse) is contacted with a test non-cell particle composition. In some embodiments, the serum of a subject that has received one or more administrations of non-cell particles, e.g., has received at least two administrations of non-cell particles, is contacted with the test non-cell particle composition. In embodiments, the composition comprising serum and non-cell particles is then tested for an activated complement factor (e.g., C3a), e.g., by ELISA. In some embodiments, a non-cell particle described herein (e.g., elevated levels of a complement regulatory protein compared to a reference cell) undergoes reduced complement activation compared to an otherwise similar non-cell particle that does not contain exogenous CD24 or a biologically active portion, e.g., reduced by at least 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 98%, or 99%. [0483] In some embodiments, the non-cell particles expressing CD24 or a biologically active portion thereof have a longer half-life in vivo compared to otherwise identical non-cell particles that do not express CD24 or a biologically active portion thereof. In some embodiments, the non-cell particles expressing CD24 and CD47 of a biologically active portion thereof have a longer half-life in vivo compared to otherwise identical non-cell particles that do not express CD24 and CD47 or a biologically active portion thereof. [0484] In some embodiments, non-cell particles described herein evade phagocytosis and have a longer half-life when administered to a mammal. In some embodiments, the mammal is a human. [0485] In some embodiments, the non-cell particle evades immune evasion through CD24 interaction with the inhibitory receptor sialic-acid-binding Ig-like lectin 10 (Siglec-10), which is expressed by tumor-associated macrophages. In some embodiments, the non-cell particle comprises immune evasion through CD24 and CD47 interaction with the inhibitory receptor sialic-acid-binding Ig-like lectin 10 (Siglec-10) and SIRPa, respectively. [0486] In some embodiments, the non-cell particle composition has a reduction in macrophage phagocytosis, e.g., a reduction of 1 %, 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, or more in macrophage phagocytosis compared to a reference particle, e.g., an otherwise similar particle but not containing exogenous CD24 or a biologically active porteion, wherein the reduction in macrophage phagocytosis is determined by assaying the phagocytosis index in vitro. [0487] In some embodiments, non-cell particles delivered into the peripheral circulation evade capture and retention by the reticulo-endothelial system (RES) in order to reach target sites with high efficiency. The RES comprises a system of cells, primarily macrophages, which reside in solid organs such as the spleen, lymph nodes and the liver. In some embodiments, the non-cell particle is not captured by the scavenger system in circulation or by Kupffer cells in the sinus of the liver. VII. PHARMACEUTICAL COMPOSITIONS AND METHODS OF MANUFACTURE [0488] The present disclosure also provides, in some aspects, a pharmaceutical composition comprising the non-cell particle composition described herein and pharmaceutically acceptable carrier. The pharmaceutical compositions can include any of the described non-cell particles. [0489] In some embodiments, the non-cell particle meets a pharmaceutical or good manufacturing practices (GMP) standard. In some embodiments, the non-cell particle was made according to good manufacturing practices (GMP). In some embodiments, the non-cell particle has a pathogen level below a predetermined reference value, e.g., is substantially free of pathogens. In some embodiments, the non-cell particle has a contaminant level below a predetermined reference value, e.g., is substantially free of contaminants. In some embodiments, the non-cell particle has low immunogenicity. [0490] In some embodiments, provided herein are the use of pharmaceutical compositions of the invention or salts thereof to practice the methods of the invention. Such a pharmaceutical composition may consist of at least one compound or conjugate of the invention or a salt thereof in a form suitable for administration to a subject, or the pharmaceutical composition may comprise at least one compound or conjugate of the invention or a salt thereof, and one or more pharmaceutically acceptable carriers, one or more additional ingredients, or some combination of these. In some embodiments, the compound or conjugate of the invention may be present in the pharmaceutical composition in the form of a physiologically acceptable salt, such as in combination with a physiologically acceptable cation or anion, as is well known in the art. [0491] In some embodiments, the pharmaceutical compositions useful for practicing the methods of the invention may be administered to deliver a dose of between 1 ng/kg/day and 100 mg/kg/day. In another embodiment, the pharmaceutical compositions useful for practicing the invention may be administered to deliver a dose of between 1 ng/kg/day and 500 mg/kg/day. [0492] In some embodiments, the relative amounts of the active ingredient, the pharmaceutically acceptable carrier, and any additional ingredients in a pharmaceutical composition of the invention will vary, depending upon the identity, size, and condition of the subject treated and further depending upon the route by which the composition is to be administered. In some embodiments, the composition may comprise between 0.1% and 100% (w/w) active ingredient. [0493] In some embodiments, pharmaceutical compositions that are useful in the methods of the invention may be suitably developed for oral, rectal, vaginal, parenteral, topical, pulmonary, intranasal, buccal, ophthalmic, or another route of administration. In some embodiments, a composition useful within the methods of the invention may be directly administered to the skin, vagina or any other tissue of a mammal. In some embodiments, formulations include liposomal preparations, resealed erythrocytes containing the active ingredient, and immunologically based formulations. In some embodiments, the route(s) of administration will be readily apparent to the skilled artisan and will depend upon any number of factors including the type and severity of the disease being treated, the type and age of the veterinary or human subject being treated, and the like. [0494] In some embodiments, formulations of the pharmaceutical compositions described herein may be prepared by any method known or hereafter developed in the art of pharmacology. In some embodiments, preparatory methods include the step of bringing the active ingredient into association with a carrier or one or more other accessory ingredients, and then, if necessary or desirable, shaping or packaging the product into a desired single- or multi- dose unit. [0495] In some embodiments, a “unit dose” is a discrete amount of the pharmaceutical composition comprising a predetermined amount of the active ingredient. In some embodiments, the amount of the active ingredient is generally equal to the dosage of the active ingredient that would be administered to a subject or a convenient fraction of such a dosage such as, for example, one-half or one-third of such a dosage. In some embodiments, the unit dosage form may be for a single daily dose or one of multiple daily doses (e.g., about 1 to 4 or more times per day). In some embodiments, when multiple daily doses are used, the unit dosage form may be the same or different for each dose. [0496] In some embodiments, although the descriptions of pharmaceutical compositions provided herein are principally directed to pharmaceutical compositions that are suitable for ethical administration to humans, it will be understood by the skilled artisan that such compositions are generally suitable for administration to animals of all sorts. In some embodiments, modification of pharmaceutical compositions suitable for administration to humans in order to render the compositions suitable for administration to various animals is well understood, and the ordinarily skilled veterinary pharmacologist may design and perform such modification with merely ordinary, if any, experimentation. In some embodiments, subjects to which administration of the pharmaceutical compositions of the invention is contemplated include humans and other primates, mammals including commercially relevant mammals such as cattle, pigs, horses, sheep, cats, and dogs. [0497] In some of any embodiments, the compositions of the invention are formulated using one or more pharmaceutically acceptable excipients or carriers. In one embodiment, the pharmaceutical compositions of the invention comprise a therapeutically effective amount of a compound or conjugate of the invention and a pharmaceutically acceptable carrier. In some embodiments, pharmaceutically acceptable carriers that are useful, include, but are not limited to, glycerol, water, saline, ethanol and other pharmaceutically acceptable salt solutions such as phosphates and salts of organic acids. Examples of these and other pharmaceutically acceptable carriers are described in Remington's Pharmaceutical Sciences (1991, Mack Publication Co., New Jersey). [0498] In some embodiments, the carrier may be a solvent or dispersion medium containing, for example, water, ethanol, polyol (for example, glycerol, propylene glycol, and liquid polyethylene glycol, and the like), suitable mixtures thereof, and vegetable oils. In some embodiments, the proper fluidity may be maintained, for example, by the use of a coating such as lecithin, by the maintenance of the required particle size in the case of dispersion and by the use of surfactants. In some embodiments, prevention of the action of microorganisms may be achieved by various antibacterial and antifungal agents, for example, parabens, chlorobutanol, phenol, ascorbic acid, thimerosal, and the like. In some embodiments, it is preferable to include isotonic agents, for example, sugars, sodium chloride, or polyalcohols such as mannitol and sorbitol, in the composition. In some embodiments, prolonged absorption of the injectable compositions may be brought about by including in the composition an agent that delays absorption, for example, aluminum monostearate or gelatin. In one embodiment, the pharmaceutically acceptable carrier is not DMSO alone. [0499] In some embodiments, formulations may be employed in admixtures with conventional excipients, i.e., pharmaceutically acceptable organic or inorganic carrier substances suitable for oral, vaginal, parenteral, nasal, intravenous, subcutaneous, enteral, or any other suitable mode of administration, known to the art. In some embodiments, the pharmaceutical preparations may be sterilized and if desired mixed with auxiliary agents, e.g., lubricants, preservatives, stabilizers, wetting agents, emulsifiers, salts for influencing osmotic pressure buffers, coloring, flavoring and/or aromatic substances and the like. In some embodiments, pharmaceutical preparations may also be combined where desired with other active agents, e.g., other analgesic agents. [0500] In some embodiments, “additional ingredients” include, but are not limited to, one or more of the following: excipients; surface active agents; dispersing agents; inert diluents; granulating and disintegrating agents; binding agents; lubricating agents; sweetening agents; flavoring agents; coloring agents; preservatives; physiologically degradable compositions such as gelatin; aqueous vehicles and solvents; oily vehicles and solvents; suspending agents; dispersing or wetting agents; emulsifying agents, demulcents; buffers; salts; thickening agents; fillers; emulsifying agents; antioxidants; antibiotics; antifungal agents; stabilizing agents; and pharmaceutically acceptable polymeric or hydrophobic materials. In some embodiments, “additional ingredients” that may be included in the pharmaceutical compositions of the invention are known in the art and described, for example in Genaro, ed. (1985, Remington's Pharmaceutical Sciences, Mack Publishing Co., Easton, Pa.), which is incorporated herein by reference. [0501] In some embodiments, the composition of the invention may comprise a preservative from about 0.005% to 2.0% by total weight of the composition. In some embodiments, the preservative is used to prevent spoilage in the case of exposure to contaminants in the environment. In some embodiments, examples of preservatives useful in accordance with the invention included but are not limited to those selected from the group consisting of benzyl alcohol, sorbic acid, parabens, imidurea and combinations thereof. In some embodiments, a particularly preferred preservative is a combination of about 0.5% to 2.0% benzyl alcohol and 0.05% to 0.5% sorbic acid. [0502] In some embodiments, the composition preferably includes an anti-oxidant and a chelating agent that inhibits the degradation of the compound. In some embodiments, antioxidants for some compounds are BHT, BHA, alpha-tocopherol and ascorbic acid in the preferred range of about 0.01% to 0.3% and more preferably BHT in the range of 0.03% to 0.1% by weight by total weight of the composition. In some embodiments, the chelating agent is present in an amount of from 0.01% to 0.5% by weight by total weight of the composition. Particularly preferred chelating agents include edetate salts (e.g. disodium edetate) and citric acid in the weight range of about 0.01% to 0.20% and more preferably in the range of 0.02% to 0.10% by weight by total weight of the composition. In some embodiments, the chelating agent is useful for chelating metal ions in the composition that may be detrimental to the shelf life of the formulation. In some embodiments, other suitable and equivalent antioxidants and chelating agents may be substituted therefore as would be known to those skilled in the art. [0503] In some embodiments, liquid suspensions may be prepared using conventional methods to achieve suspension of the active ingredient in an aqueous or oily vehicle. In some embodiments, aqueous vehicles include, for example, water, and isotonic saline. In some embodiments, oily vehicles include, for example, almond oil, oily esters, ethyl alcohol, vegetable oils such as arachis, olive, sesame, or coconut oil, fractionated vegetable oils, and mineral oils such as liquid paraffin. In some embodiments, liquid suspensions may further comprise one or more additional ingredients including, but not limited to, suspending agents, dispersing or wetting agents, emulsifying agents, demulcents, preservatives, buffers, salts, flavorings, coloring agents, and sweetening agents. In some embodiments, oily suspensions may further comprise a thickening agent. In some embodiments, suspending agents include, but are not limited to, sorbitol syrup, hydrogenated edible fats, sodium alginate, polyvinylpyrrolidone, gum tragacanth, gum acacia, and cellulose derivatives such as sodium carboxymethylcellulose, methylcellulose, hydroxypropylmethylcellulose. In some embodiments, dispersing or wetting agents include, but are not limited to, naturally-occurring phosphatides such as lecithin, condensation products of an alkylene oxide with a fatty acid, with a long chain aliphatic alcohol, with a partial ester derived from a fatty acid and a hexitol, or with a partial ester derived from a fatty acid and a hexitol anhydride (e.g., polyoxyethylene stearate, heptadecaethyleneoxycetanol, polyoxyethylene sorbitol monooleate, and polyoxyethylene sorbitan monooleate, respectively). Known emulsifying agents include, but are not limited to, lecithin, and acacia. Known preservatives include, but are not limited to, methyl, ethyl, or n-propyl-para-hydroxybenzoates, ascorbic acid, and sorbic acid. Known sweetening agents include, for example, glycerol, propylene glycol, sorbitol, sucrose, and saccharin. Known thickening agents for oily suspensions include, for example, beeswax, hard paraffin, and cetyl alcohol. [0504] In some embodiments, liquid solutions of the active ingredient in aqueous or oily solvents may be prepared in substantially the same manner as liquid suspensions, the primary difference being that the active ingredient is dissolved, rather than suspended in the solvent. As used herein, an “oily” liquid is one which comprises a carbon-containing liquid molecule and which exhibits a less polar character than water. In some embodiments, liquid solutions of the pharmaceutical composition of the invention may comprise each of the components described with regard to liquid suspensions, it being understood that suspending agents will not necessarily aid dissolution of the active ingredient in the solvent. In some embodiments, aqueous solvents include, for example, water, and isotonic saline. In some embodiments, oily solvents include, for example, almond oil, oily esters, ethyl alcohol, vegetable oils such as arachis, olive, sesame, or coconut oil, fractionated vegetable oils, and mineral oils such as liquid paraffin. [0505] In some embodiments, powdered and granular formulations of a pharmaceutical preparation of the invention may be prepared using known methods. In some embodiments, formulations may be administered directly to a subject, used, for example, to form tablets, to fill capsules, or to prepare an aqueous or oily suspension or solution by addition of an aqueous or oily vehicle thereto. In some of any embodiments, formulations may further comprise one or more of dispersing or wetting agent, a suspending agent, and a preservative. Additional excipients, such as fillers and sweetening, flavoring, or coloring agents, may also be included in these formulations. [0506] In some embodiments, a pharmaceutical composition of the invention may also be prepared, packaged, or sold in the form of oil-in-water emulsion or a water-in-oil emulsion. In some embodiments, the oily phase may be a vegetable oil such as olive or arachis oil, a mineral oil such as liquid paraffin, or a combination of these. In some embodiments, compositions further comprise one or more emulsifying agents such as naturally occurring gums such as gum acacia or gum tragacanth, naturally-occurring phosphatides such as soybean or lecithin phosphatide, esters or partial esters derived from combinations of fatty acids and hexitol anhydrides such as sorbitan monooleate, and condensation products of such partial esters with ethylene oxide such as polyoxyethylene sorbitan monooleate. In some embodiments, emulsions may also contain additional ingredients including, for example, sweetening or flavoring agents. VIII. METHODS OF DELIVERY AND TREATMENT [0507] In some embodiments, the CD24-associated non-cell particles provided herein, e.g. retroviral particles, other non-cell particles, or fusosomes thereof, is capable of delivering (e.g., delivers) an exogenous agent to a target cell.The exogenous agent can be a protein, nucleic acid (e.g., mRNA), or small molecule. Exemplary exogenous agents that can be contained in a non- cell particle herein for delivery are described in Section V. Among provided methods herein are methods that comprise delivering an agent to a target cell. In some embodiments, the exogenous agent is an agent that is entirely heterologous or not produced or normally expressed by the target cell. In some embodiments, delivery of the exogenous agent to the target cell can provide a therapeutic effect to treat a disease or condition in the subject. The therapeutic effect may be by targeting, modulating or altering an antigen or protein present or expressed by the target cell that is associated with or involved in a disease or condition. The therapeutic effect may be by providing an exogenous agent in which the exogenous agent is a protein (or a nucleic acid encoding the protein, e.g., an mRNA encoding the protein) which is absent, mutant, or at a lower level than wild-type in the target cell. In some embodiments, the target cell is from a subject having a genetic disease, e.g., a monogenic disease, e.g., a monogenic intracellular protein disease. [0508] The non-cell particles, e.g., fusosomes, retroviral vectors, VLPs, or pharmaceutical compositions, described herein can be administered to a subject, e.g., a mammal, e.g., a human. In such embodiments, the subject may be at risk of, may have a symptom of, or may be diagnosed with or identified as having, a particular disease or condition (e.g., a disease or condition described herein). In some embodiments, the disease or condition may be one that is treated by delivery of the exogenous agent contained in the administered non-cell particle to a target cell in the subject. [0509] This disclosure also provides, in certain aspects, a method of administering a non-cell particle composition to a subject (e.g., a human subject), a target tissue, or a cell, comprising administering to the subject, or contacting the target tissue or the cell with a non-cell particle composition comprising a plurality of non-cell particles described herein, a non-cell particle composition described herein, or a pharmaceutical composition described herein, thereby administering the non-cell particle composition to the subject [0510] This disclosure also provides, in certain aspects, a method of delivering an exogenous agent, for instance a therapeutic agent (e.g., a polypeptide, a nucleic acid, a metabolite, an organelle, or a subcellular structure), to a subject, a target tissue, or a cell, comprising administering to the subject, or contacting the target tissue or the cell with, a plurality of non-cell particles described herein, a non-cell particle composition comprising a plurality of non-cell particles described herein, a non-cell particle composition described herein, or a pharmaceutical composition described herein, wherein the non-cell particle composition is administered in an amount and/or time such that the therapeutic agent is delivered. Exemplary exogenous agents that can be contained in a non-cell particle herein for delivery to a subject are described in Section V. [0511] This disclosure also provides, in certain aspects, a method of delivering a function to a subject, a target tissue, or a cell, comprising administering to the subject, or contacting the target tissue or the cell with, a plurality of non-cell particles described herein, a non-cell particle composition comprising a plurality of non-cell particles described herein, a non-cell particle composition described herein, or a pharmaceutical composition described herein, wherein the non-cell particle composition is administered in an amount and/or time such that the function is delivered via delivery by the non-cell particle composition of an exogenous agent (e.g., therapeutic agent) to the target tissue or the cell. [0512] Target cells from mammalian (e.g., human) tissue include cells from epithelial, connective, muscular, or nervous tissue or cells, and combinations thereof. Target mammalian (e.g., human) cells and organ systems include the cardiovascular system (heart, vasculature); digestive system (esophagus, stomach, liver, gallbladder, pancreas, intestines, colon, rectum and anus); endocrine system (hypothalamus, pituitary gland, pineal body or pineal gland, thyroid, parathyroids, adrenal glands); excretory system (kidneys, ureters, bladder); lymphatic system (lymph, lymph nodes, lymph vessels, tonsils, adenoids, thymus, spleen); integumentary system (skin, hair, nails); muscular system (e.g., skeletal muscle); nervous system (brain, spinal cord, nerves)’; reproductive system (ovaries, uterus, mammary glands, testes, vas deferens, seminal vesicles, prostate); respiratory system (pharynx, larynx, trachea, bronchi, lungs, diaphragm); skeletal system (bone, cartilage), and combinations thereof. In some embodiments, a non-target cells or organ system is chosen from the cardiovascular system (heart, vasculature); digestive system (esophagus, stomach, liver, gallbladder, pancreas, intestines, colon, rectum and anus); endocrine system (hypothalamus, pituitary gland, pineal body or pineal gland, thyroid, parathyroids, adrenal glands); excretory system (kidneys, ureters, bladder); lymphatic system (lymph, lymph nodes, lymph vessels, tonsils, adenoids, thymus, spleen); integumentary system (skin, hair, nails); muscular system (e.g., skeletal muscle); nervous system (brain, spinal cord, nerves)’; reproductive system (ovaries, uterus, mammary glands, testes, vas deferens, seminal vesicles, prostate); respiratory system (pharynx, larynx, trachea, bronchi, lungs, diaphragm); skeletal system (bone, cartilage), and combinations thereof. [0513] In some embodiments, the target cell or tissue is any such listed in any of WO 2020/102499, WO 2020/102485, WO 2019/222403, WO 2020/014209, and WO 2020/102503, each of which is hereby incorporated by reference in its entirety. In some embodiments, the target cell is a T cell. In some embodiments, the target cell is any of a CD4+ T cell, a CD8+ T cell, an alpha beta T cell, a gamma delta T cell, a naive T cell, an effector T cell, a cytotoxic T cell (e.g., a CD8+ cytotoxic T cell), a regulatory T cell (e.g., a thymus-derived regulatory T cell, a peripherally derived regulatory T cell, a CD4+Foxp3+ regulatory T cell, or a CD4+FoxP3- type 1 regulatory T (Trl) cell), a helper T cell (e.g., a CD4+ helper T cell, a Thl cell, a Th2 cell, a Th3 cell, a Th9 cell, a Thl7 cell, a Th22 cell, or a T follicular helper (Tfh) cell), a memory T cell (e.g., a stem cell memory T cell, a central memory T cell, or an effector memory T cell), a NKT cell, and a Mucosal associated invariant T (MAIT) cell. A. Delivery [0514] In some embodiments, the non-cell particle delivers the exogenous agent to at least 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99% of the number of cells in the target cell population. In some embodiments, the non-cell particle delivers at least 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99% of the exogenous agent to the target cell population. [0515] In some embodiments, the non-cell particle delivers at least 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99% more of the exogenous agent to the target cell population compared to a non-target cell population. In some embodiments, the non-cell particle delivers more exogenous agent to the target cell population based on the non-cell particle comprising a fusogen or re-target fusogen that facilitates binding to the target cell population, but not the non-target cell population. The non-cell particle can comprise any of the exemplary fusogens and re-targeted fusogens described in Section IV herein. In some embodiments, when the plurality of non-cell particles are contacted with a cell population comprising target cells and non-target cells, the exogenous agent is present in at least 10-fold more target cells than non-target cells. In some embodiments, when the plurality of non- cell particles are contacted with a cell population comprising target cells and non-target cells, the exogenous agent is present at least 2-fold, 5-fold, 10-fold, 20-fold, or 50-fold higher in target cells than non-target cells and/or the exogenous agent is present at least 2-fold, 5-fold, 10-fold, 20-fold, or 50-fold higher in target cells than non-target cells. In some embodiments, the non- cell particles of the plurality fuse at a higher rate with a target cell than with a non-target cell by at least 50%. [0516] In some embodiments, the non-cell particle, when contacted with a target cell population, delivers the exogenous agent to a target cell location other than an endosome or lysosome. In embodiments, less 50%, 40%, 30%, 20%, or 10% of the exogenous agent is delivered to an endosome or lysosome. In some embodiments, less than 10% of exogenous agent enters the cell by endocytosis. In some embodiments, the non-cell particle is capable of delivering (e.g., delivers) an exogenous agent, e.g., a protein, to the cytosol of a target cell. [0517] In some embodiments, the non-cell particle is capable of delivering (e.g., delivers) an exogenous agent, e.g., a protein, to the cell membrane of a target cell. Similarly, in some embodiments, a method herein comprises delivering an exogenous agent to the cell membrane of a target cell. In some embodiments, delivering the protein comprises delivering a nucleic acid (e.g., mRNA) encoding the protein to the target cell such that the target cell produces the protein and localizes it to the membrane. In some embodiments, the non-cell particle comprises, or the method further comprises delivering, the protein, and fusion of the non-cell particle with the target cell transfers the protein to the cell membrane of the target cell. In some embodiments, the exogenous agent comprises a cell surface ligand or an antibody that binds a cell surface receptor. [0518] In some embodiments, the non-cell particle further comprises, or the method further comprises delivering, a second exogenous agent that comprises or encodes a second cell surface ligand or antibody that binds a cell surface receptor, and optionally further comprising or encoding one or more additional cell surface ligands or antibodies that bind a cell surface receptor (e.g., 1, 2, 3, 4, 5, 10, 20, 50, or more). In some embodiments, the first exogenous agent and the second exogenous agent form a complex, wherein optionally the complex further comprises one or more additional cell surface ligands. In some embodiments, the exogenous agent comprises or encodes a cell surface receptor, e.g., an exogenous cell surface receptor. In some embodiments, the non-cell particle further comprises, or the method further comprises delivering, a second exogenous agent that comprises or encodes a second cell surface receptor, and optionally further comprises or encodes one or more additional cell surface receptors (e.g., 1, 2, 3, 4, 5, 10, 20, 50, or more cell surface receptors). [0519] In some embodiments, the non-cell particle is capable of delivering (e.g., delivers) one or more cell surface receptors to a target cell (e.g., an immune cell). Similarly, in some embodiments, a method herein comprises delivering one or more cell surface receptors to a target cell. In some embodiments, the first exogenous agent and the second exogenous agent form a complex, wherein optionally the complex further comprises one or more additional cell surface receptors. In some embodiments, the exogenous agent comprises or encodes an antigen or an antigen presenting protein. [0520] In some embodiments, the non-cell particle is capable of causing (e.g., causes) a target cell to secrete a protein, e.g., a therapeutic protein. In some embodiments, the non-cell particle is capable of delivering (e.g., delivers) a secreted exogenous agent, e.g., a secreted protein to a target site (e.g., an extracellular region), e.g., by delivering a nucleic acid (e.g., mRNA) encoding the protein to the target cell under conditions that allow the target cell to produce and secrete the protein. Similarly, in some embodiments, a method herein comprises delivering a secreted exogenous agent as described herein. In embodiments, the secreted protein comprises a protein therapeutic, e.g., an antibody molecule, a cytokine, or an enzyme. In embodiments, the secreted protein comprises an autocrine signalling molecule or a paracrine signalling molecule. In embodiments, the secreted exogenous agent comprises a secretory granule. [0521] In some embodiments, the non-cell particle is capable of secreting (e.g., secretes) an exogenous agent, e.g., a protein. In some embodiments, the exogenous agent, e.g., secreted agent, is delivered to a target site in a subject. In some embodiments, the exogenous agent is a protein that cannot be made recombinantly or is difficult to make recombinantly. In some embodiments, the non-cell particle that secretes a protein is from a source cell selected from an MSC or a chondrocyte. [0522] In some embodiments, the non-cell particle is capable of reprogramming (e.g., reprograms) a target cell (e.g., an immune cell), e.g., by delivering an exogenous agent selected from a transcription factor, a nucleic acid encoding a transcription factor, mRNA, or a plurality of said exogenous agents. Similarly, in some embodiments, a method herein comprises reprogramming a target cell. In embodiments, reprogramming comprises inducing a pancreatic endocrine cell to take on one or more characteristics of a pancreatic beta cell, by inducing a non- dopaminergic neuron to take on one or more characteristics of a dopaminergic neuron, or by inducing an exhausted T cell to take on one or more characteristics of a nonexhausted T cell, e.g., a killer T cell. In some embodiments, the exogenous agent comprises an antigen. In some embodiments, the non-cell particle comprises a first exogenous agent comprising an antigen and a second exogenous agent comprising an antigen presenting protein. [0523] In some embodiments, a non-cell particle is capable of modifying, e.g., modifies, a target tumor cell, for instance by delivering an exogenous agent (protein or nucleic acid) or a nucleic encoding an exogenous agent. Similarly, in some embodiments, a method herein comprises modifying a target tumor cell. In embodiments, the non-cell particle delivers an mRNA encoding an immunostimulatory ligand, an antigen presenting protein, a tumor suppressor protein, or a pro-apoptotic protein. In some embodiments, the non-cell particle delivers an miRNA capable of reducing levels in a target cell of an immunosuppressive ligand, a mitogenic signal, or a growth factor. [0524] In some embodiments, a non-cell particle delivers an exogenous agent that is immunomodulatory, e.g., immuno stimulatory. [0525] In some embodiments, a non-cell particle is capable of causing (e.g., causes) the target cell to present an antigen, for instance by delivering an exogenous agent comprising an antigen or a nucleic acid encoding the antigen. Similarly, in some embodiments, a method herein comprises presenting an antigen on a target cell. In some embodiments, the non-cell particle promotes regeneration in a target tissue. Similarly, in some embodiments, a method herein comprises promoting regeneration in a target tissue. In embodiments, the target cell is a cardiac cell, e.g., a cardiomyocyte (e.g., a quiescent cardiomyocyte), a hepatoblast (e.g., a bile duct hepatoblast), an epithelial cell, a naive T cell, a macrophage (e.g., a tumor infiltrating macrophage), or a fibroblast (e.g., a cardiac fibroblast). In embodiments, the source cell is a T cell (e.g., a Treg), a macrophage, or a cardiac myocyte. [0526] In some embodiments, the non-cell particle is capable of delivering (e.g., delivers) a nucleic acid to a target cell, e.g., to stably modify the genome of the target cell, e.g., for gene therapy. Similarly, in some embodiments, a method herein comprises delivering a nucleic acid to a target cell. In some embodiments, the target cell has an enzyme deficiency, e.g., comprises a mutation in an enzyme leading to reduced activity (e.g., no activity) of the enzyme. [0527] In some embodiments, the non-cell particle is capable of delivering (e.g., delivers) a reagent that mediates a sequence specific modification to DNA (e.g., Cas9, ZFN, or TALEN) in the target cell. Similarly, in some embodiments, a method herein comprises delivering the reagent to the target cell. In embodiments, the target cell is a CNS cell. [0528] In some embodiments, the non-cell particle is capable of delivering (e.g., delivers) a nucleic acid to a target cell, e.g., to transiently modify gene expression in the target cell. [0529] In some embodiments, the non-cell particle is capable of delivering (e.g., delivers) a protein to a target cell, e.g., to transiently rescue a protein deficiency. Similarly, in some embodiments, a method herein comprises delivering a protein to a target cell. In embodiments, the protein is a membrane protein (e.g., a membrane transporter protein), a cytoplasmic protein (e.g., an enzyme), or a secreted protein (e.g., an immunosuppressive protein). [0530] In some embodiments, the non-cell particle is capable of intracellular molecular delivery, e.g., delivers a protein exogenous agent to a target cell. Similarly, in some embodiments, a method herein comprises delivering a molecule to an intracellular region of a target cell. In embodiments, the protein exogenous agent is an inhibitor. In some embodiments, the protein exogenous agent comprises a nanobody, scFv, camelid antibody, peptide, macrocycle, or small molecule. [0531] In some embodiments, the non-cell particle comprises on its membrane one or more cell surface ligands (e.g., 1, 2, 3, 4, 5, 10, 20, 50, or more cell surface ligands), said cell surface ligands to be presented by the non-cell particle to a target cell. Similarly, in some embodiments, a method herein comprises presenting one or more cell surface ligands to a target cell. In some embodiments, the non-cell particle having a cell surface ligand is from a source cell chosen from a neutrophil (e.g., and the target cell is a tumor-infiltrating lymphocyte), dendritic cell (e.g., and the target cell is a naive T cell), or neutrophil (e.g., and the target is a tumor cell or virus- infected cell). In some embodiments the non-cell particle comprises a membrane complex, e.g., a complex comprising at least 2, 3, 4, or 5 proteins, e.g., a homodimer, heterodimer, homotrimer, heterotrimer, homotetramer, or heterotetramer. In some embodiments, the non-cell particle comprises an antibody, e.g., a toxic antibody, e.g., the non-cell particle is capable of delivering the antibody to the target site, e.g., by homing to a target site. In some embodiments, the source cell is an NK cell or neutrophil. [0532] In some embodiments, a method herein comprises causing ligand presentation on the surface of a target cell by presenting cell surface ligands on the non-cell particle. In some embodiments, the non-cell particle is capable of causing cell death of the target cell. In some embodiments, the non-cell particle is from a NK source cell. [0533] In some embodiments, a non-cell particle or target cell is capable of phagocytosis (e.g., of a pathogen). Similarly, in some embodiments, a method herein comprises causing phagocytosis. [0534] In some embodiments, a non-cell particle senses and responds to its local environment. In some embodiments, the non-cell particle is capable of sensing level of a metabolite, interleukin, or antigen. [0535] In embodiments, a non-cell particle is capable of chemotaxis, extravasation, or one or more metabolic activities. In embodiments, the metabolic activity is selected from kyneurinine, gluconeogenesis, prostaglandin fatty acid oxidation, adenosine metabolism, urea cycle, and thermogenic respiration. In some embodiments, the source cell is a neutrophil and the non-cell particle is capable of homing to a site of injury. In some embodiments, the source cell is a macrophage and the non-cell particle is capable of phagocytosis. In some embodiments, the source cell is a brown adipose tissue cell and the non-cell particle is capable of lipolysis. [0536] In some embodiments, the non-cell particle comprises (e.g., is capable of delivering to the target cell) a plurality of exogenous agents (e.g., at least 2, 3, 4, 5, 10, 20, or 50 exogenous agents) or nucleic acids encoding a plurality of exogenous agents. In embodiments, the non-cell particle comprises an inhibitory nucleic acid (e.g., siRNA or miRNA) and an mRNA. [0537] In some embodiments, the non-cell particle comprises (e.g., is capable of delivering to the target cell) a membrane protein or a nucleic acid encoding the membrane protein. In embodiments, the non-cell particle is capable of reprogramming or transdifferentiating a target cell, e.g., the non-cell particle comprises one or more agents that induce reprogramming or transdifferentiation of a target cell. [0538] In some embodiments, the non-cell particle, e.g., fusosome, fuses at a higher rate with a target cell than with a non-target cell based on the non-cell particle comprising a fusogen or re-target fusogen that facilitates binding to the target cell, but not the non-target cell. The non- cell particle can comprise any of the exemplary fusogens and re-targeted fusogens described in Section IV. In some embodiments, the non-cell particle, e.g., fusosome, fuses at a higher rate with a target cell than with a non-target cell, e.g., by at least at least 1%, 2%, 3%, 4%, 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 2-fold, 3-fold, 4-fold, 5-fold, 10-fold, 20-fold, 50- fold, or 100-fold. In some embodiments, the non-cell particle, e.g., fusosome, fuses at a higher rate with a target cell than with other non-cell particles, e.g., by at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, or 90%. In some embodiments, the non-cell particle, e.g., fusosome, fuses with target cells at a rate such that an exogenous agent or nucleic acid encoding an exogenous agent in the non-cell particle is delivered to at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, or 90%, of target cells after 24, 48, or 72 hours. In embodiments, the amount of targeted fusion is about 30%-70%, 35%-65%, 40%-60%, 45%-55%, or 45%-50%. In embodiments, the amount of targeted fusion is about 20%-40%, 25%-35%, or 30%-35%. [0539] In some embodiments, the fusogen is present at a copy number of at least, or no more than, 10, 50, 100, 500, 1,000, 2,000, 5,000, 10,000, 20,000, 50,000, 100,000, 200,000, 500,000, 1,000,000, 5,000,000, 10,000,000, 50,000,000, 100,000,000, 500,000,000, or 1,000,000,000 copies. In some embodiments, at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 96%, 97%, 98%, or 99% of the fusogen comprised by the non-cell particle is disposed in the cell membrane. In embodiments, the non-cell particle also comprises fusogen internally, e.g., in the cytoplasm or an organelle. In some embodiments, the fusogen comprises (or is identified as comprising) about 0.1%, 0.2%, 0.3%, 0.4%, 0.5%, 0.6%, 0.7%, 0.8%, 0.9%, 1%, 5%, 10%, 11%, 12%, 13%, 14%, 15%, 20%, or more, or about 1-30%, 5- 20%, 10-15%, 12-15%, 13-14%, or 13.6% of the total protein in a non-cell particle, e.g., as determined by a mass spectrometry assay. In embodiments, the fusogen comprises (or is identified as comprising) about 13.6% of the total protein in the non-cell particle. In some embodiments, the fusogen is (or is identified as being) more or less abundant than one or more additional proteins of interest. In an embodiment, the fusogen has (or is identified as having) a ratio to EGFP of about 140, 145, 150, 151, 152, 153, 154, 155, 156, 157 (e.g., 156.9), 158, 159, 160, 165, or 170. In another embodiment, the fusogen has (or is identified as having) a ratio to CD63 of about 2700, 2800, 2900, 2910 (e.g., 2912), 2920, 2930, 2940, 2950, 2960, 2970, 2980, 2990, or 3000, or about 1000-5000, 2000- 4000, 2500-3500, 2900-2930, 2910-2915, or 2912.0, e.g., by a mass spectrometry assay. In an embodiment, the fusogen has (or is identified as having) a ratio to ARRDC1 of about 600, 610, 620, 630, 640, 650, 660 (e.g., 664.9), 670, 680, 690, or 700. In another embodiment, the fusogen has (or is identified as having) a ratio to GAPDH of about 50, 55, 60, 65, 70 (e.g., 69), 75, 80, or 85, or about 1-30%, 5-20%, 10-15%, 12-15%, 13-14%, or 13.6%. In another embodiment, the fusogen has (or is identified as having) a ratio to CNX of about 500, 510, 520, 530, 540, 550, 560 (e.g., 558.4), 570, 580, 590, or 600, or about 300-800, 400-700, 500-600, 520-590, 530-580, 540-570, 550-560, or 558.4, e.g., by a mass spectrometry assay. [0540] In some embodiments, the non-cell particle comprises a therapeutic agent at a copy number of at least, or no more than, 10, 50, 100, 500, 1,000, 2,000, 5,000, 10,000, 20,000, 50,000, 100,000, 200,000, 500,000, 1,000,000, 5,000,000, 10,000,000, 50,000,000, 100,000,000, 500,000,000, or 1,000,000,000 copies. In some embodiments, the non-cell particle comprises a protein therapeutic agent at a copy number of at least 10, 50, 100, 500, 1,000, 2,000, 5,000, 10,000, 20,000, 50,000, 100,000, 200,000, 500,000, 1,000,000, 5,000,000, 10,000,000, 50,000,000, 100,000,000, 500,000,000, or 1,000,000,000 copies. In some embodiments, the non- cell particle comprises a nucleic acid therapeutic agent at a copy number of at least 10, 50, 100, 500, 1,000, 2,000, 5,000, 10,000, 20,000, 50,000, 100,000, 200,000, 500,000, 1,000,000, 5,000,000, 10,000,000, 50,000,000, 100,000,000, 500,000,000, or 1,000,000,000 copies. In some embodiments, the non-cell particle comprises a DNA therapeutic agent at a copy number of at least 10, 50, 100, 500, 1,000, 2,000, 5,000, 10,000, 20,000, 50,000, 100,000, 200,000, 500,000, 1,000,000, 5,000,000, 10,000,000, 50,000,000, 100,000,000, 500,000,000, or 1,000,000,000 copies. In some embodiments, the non-cell particle comprises an RNA therapeutic agent at a copy number of at least 10, 50, 100, 500, 1,000, 2,000, 5,000, 10,000, 20,000, 50,000, 100,000, 200,000, 500,000, 1,000,000, 5,000,000, 10,000,000, 50,000,000, 100,000,000, 500,000,000, or 1,000,000,000 copies. In some embodiments, the non-cell particle comprises a nucleic acid encoding an exogenous protein, e.g. a therapeutic agent at a copy number of at least 10, 50, 100, 500, 1,000, 2,000, 5,000, 10,000, 20,000, 50,000, 100,000, 200,000, 500,000, 1,000,000, 5,000,000, 10,000,000, 50,000,000, 100,000,000, 500,000,000, or 1,000,000,000 copies. In some embodiments, the non-cell particle comprises an exogenous therapeutic agent at a copy number of at least 10, 50, 100, 500, 1,000, 2,000, 5,000, 10,000, 20,000, 50,000, 100,000, 200,000, 500,000, 1,000,000, 5,000,000, 10,000,000, 50,000,000, 100,000,000, 500,000,000, or 1,000,000,000 copies. In some embodiments, the non-cell particle comprises an exogenous protein therapeutic agent at a copy number of at least 10, 50, 100, 500, 1,000, 2,000, 5,000, 10,000, 20,000, 50,000, 100,000, 200,000, 500,000, 1,000,000, 5,000,000, 10,000,000, 50,000,000, 100,000,000, 500,000,000, or 1,000,000,000 copies. In some embodiments, the non-cell particle comprises an exogenous nucleic acid (e.g., DNA or RNA) therapeutic agent at a copy number of at least 10, 50, 100, 500, 1,000, 2,000, 5,000, 10,000, 20,000, 50,000, 100,000, 200,000, 500,000, 1,000,000, 5,000,000, 10,000,000, 50,000,000, 100,000,000, 500,000,000, or 1,000,000,000 copies. In some embodiments, the ratio of the copy number of the fusogen to the copy number of the therapeutic agent is between 1,000,000:1 and 100,000:1, 100,000:1 and 10,000:1, 10,000:1 and 1,000:1, 1,000:1 and 100:1, 100:1 and 50:1, 50:1 and 20:1, 20:1 and 10:1, 10:1 and 5:1, 5:1 and 2:1, 2:1 and 1:1, 1:1 and 1:2, 1:2 and 1:5, 1:5 and 1:10, 1:10 and 1:20, 1:20 and 1:50, 1:50 and 1:100, 1:100 and 1:1,000, 1:1,000 and 1:10,000, 1:10,000 and 1:100,000, or 1:100,000 and 1:1,000,000 [0541] In some embodiments, the non-cell particle delivers to a target cell at least 10, 50, 100, 500, 1,000, 2,000, 5,000, 10,000, 20,000, 50,000, 100,000, 200,000, 500,000, 1,000,000, 5,000,000, 10,000,000, 50,000,000, 100,000,000, 500,000,000, or 1,000,000,000 copies of a exogenous agent. In some embodiments, the non-cell particle delivers to a target cell at least 10, 50, 100, 500, 1,000, 2,000, 5,000, 10,000, 20,000, 50,000, 100,000, 200,000, 500,000, 1,000,000, 5,000,000, 10,000,000, 50,000,000, 100,000,000, 500,000,000, or 1,000,000,000 copies of a therapeutic agent. In some embodiments, the non-cell particle delivers to a target cell at least 10, 50, 100, 500, 1,000, 2,000, 5,000, 10,000, 20,000, 50,000, 100,000, 200,000, 500,000, 1,000,000, 5,000,000, 10,000,000, 50,000,000, 100,000,000, 500,000,000, or 1,000,000,000 copies of a protein therapeutic agent. In some embodiments, the non-cell particle delivers to a target cell at least 10, 50, 100, 500, 1,000, 2,000, 5,000, 10,000, 20,000, 50,000, 100,000, 200,000, 500,000, 1,000,000, 5,000,000, 10,000,000, 50,000,000, 100,000,000, 500,000,000, or 1,000,000,000 copies of a nucleic acid therapeutic agent. In some embodiments, the non-cell particle delivers to a target cell at least 10, 50, 100, 500, 1,000, 2,000, 5,000, 10,000, 20,000, 50,000, 100,000, 200,000, 500,000, 1,000,000, 5,000,000, 10,000,000, 50,000,000, 100,000,000, 500,000,000, or 1,000,000,000 copies of an RNA therapeutic agent. In some embodiments, the non-cell particle delivers to a target cell at least 10, 50, 100, 500, 1,000, 2,000, 5,000, 10,000, 20,000, 50,000, 100,000, 200,000, 500,000, 1,000,000, 5,000,000, 10,000,000, 50,000,000, 100,000,000, 500,000,000, or 1,000,000,000 copies of a DNA therapeutic agent. [0542] In some embodiments, the non-cell particle delivers to a target cell at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 96%, 97%, 98%, or 99% of the cargo (e.g., a therapeutic agent, e.g., an exogenous therapeutic agent) comprised by the non-cell particle. In some embodiments, the non-cell particles, e.g., fusosomes, that fuse with the target cell(s) deliver to the target cell an average of at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 96%, 97%, 98%, or 99% of the cargo (e.g., a therapeutic agent, e.g., an exogenous therapeutic agent) comprised by the non-cell particles that fuse with the target cell(s). In some embodiments, the non-cell particle composition delivers to a target tissue at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 96%, 97%, 98%, or 99% of the cargo (e.g., a therapeutic agent, e.g., an exogenous therapeutic agent) comprised by the non-cell particle composition. [0543] In some embodiments, the non-cell particle comprises 0.00000001 mg fusogen to 1 mg fusogen per mg of total protein in non-cell particle, e.g., 0.00000001 - 0.0000001, 0.0000001 - 0.000001, 0.000001 - 0.00001, 0.00001 - 0.0001, 0.0001 - 0.001, 0.001 - 0.01, 0.01 - 0.1, or 0.1 - 1 mg fusogen per mg of total protein in non-cell particle. In some embodiments, the non- cell particle comprises 0.00000001 mg fusogen to 5 mg fusogen per mg of lipid in non-cell particle, e.g., 0.00000001 - 0.0000001, 0.0000001 - 0.000001, 0.000001 - 0.00001, 0.00001 - 0.0001, 0.0001 - 0.001, 0.001 - 0.01, 0.01 - 0.1, 0.1 - 1, or 1-5 mg fusogen per mg of lipid in non-cell particle. B. Treatment and Uses [0544] In some embodiments, the CD24-associated non-cell particles provided herein, e.g. non-cell particle, e.g. retroviral particles other non-cell particles or fusosomes thereof, or pharmaceutical compositions thereof as described herein can be administered to a subject, e.g. a mammal, e.g. a human. In some embodiments, the administration delivers the non-cell particles to a target cell in the subject. In such embodiments, the subject may be at risk of, may have a symptom of, or may be diagnosed with or identified as having, a particular disease or condition. In some embodiments, the methods thereby treat the disease or condition or disorder in the subject In one embodiment the subject has cancer In one embodiment the subject has an infectious disease. In some embodiments, the non-cell particle, e.g. retroviral particles other non-cell particles or fusosomes thereof, contains nucleic acid sequences encoding an exogenous agent for treating the disease or condition in the subject. For example, the exogenous agent is one that targets or is specific for a protein of a neoplastic cells and the non-cell particle, e.g. retroviral particles other non-cell particles or fusosomes thereof, is administered to a subject for treating a tumor or cancer in the subject. In another example, the exogenous agent is an inflammatory mediator or immune molecule, such as a cytokine, and the non-cell particle, e.g. retroviral particles other non-cell particles or fusosomes thereof, is administered to a subject for treating any condition in which it is desired to modulate (e.g. increase) the immune response, such as a cancer or infectious disease. In some embodiments, the CD24-associated non-cell particle, e.g. retroviral particles other non-cell particles or fusosomes thereof, is administered in an effective amount or dose to effect treatment of the disease, condition or disorder. [0545] Provided herein are uses of any of the provided CD24-associated non-cell particles, e.g. retroviral particles other non-cell particles or fusosomes thereof, in such methods and treatments, and in the preparation of a medicament in order to carry out such therapeutic methods. In some embodiments, the methods are carried out by administering the non-cell particle, e.g. retroviral particles other non-cell particles or fusosomes thereof, or compositions comprising the same, to the subject having, having had, or suspected of having the disease or condition or disorder. In some embodiments, the methods thereby treat the disease or condition or disorder in the subject. Also provided herein are uses of any of the compositions, such as pharmaceutical compositions provided herein, for the treatment of a disease, condition or disorder associated with a particular gene or protein targeted by or provided by the exogenous agent. [0546] In some embodiments, the provided methods or uses involve administration of a pharmaceutical composition comprising oral, inhaled, transdermal or parenteral (including intravenous, intratumoral, intraperitoneal, intramuscular, intracavity, and subcutaneous) administration. In some embodiments, the non-cell particles may be administered alone or formulated as a pharmaceutical composition. In some embodiments, the non-cell particles or pharmaceutical compositions described herein can be administered to a subject, e.g., a mammal, e.g., a human. In some of any embodiments, the subject may be at risk of, may have a symptom of, or may be diagnosed with or identified as having, a particular disease or condition (e.g., a disease or condition described herein). In some embodiments, the disease is a disease or disorder. [0547] In some embodiments, the non-cell particles may be administered in the form of a unit-dose composition, such as a unit dose oral, parenteral, transdermal or inhaled composition. In some embodiments, the compositions are prepared by admixture and are adapted for oral, inhaled, transdermal or parenteral administration, and as such may be in the form of tablets, capsules, oral liquid preparations, powders, granules, lozenges, reconstitutable powders, injectable and infusable solutions or suspensions or suppositories or aerosols. [0548] In some embodiments, the regimen of administration may affect what constitutes an effective amount. In some embodiments, the therapeutic formulations may be administered to the subject either prior to or after a diagnosis of disease. In some embodiments, several divided dosages, as well as staggered dosages may be administered daily or sequentially, or the dose may be continuously infused, or may be a bolus injection. In some embodiments, the dosages of the therapeutic formulations may be proportionally increased or decreased as indicated by the exigencies of the therapeutic or prophylactic situation. [0549] In some embodiments, the administration of the compositions of the present invention to a subject, preferably a mammal, more preferably a human, may be carried out using known procedures, at dosages and for periods of time effective to prevent or treat disease. In some embodiments, an effective amount of the therapeutic compound necessary to achieve a therapeutic effect may vary according to factors such as the activity of the particular compound employed; the time of administration; the rate of excretion of the compound; the duration of the treatment; other drugs, compounds or materials used in combination with the compound; the state of the disease or disorder, age, sex, weight, condition, general health and prior medical history of the subject being treated, and like factors well-known in the medical arts. In some embodiments, the dosage regimens may be adjusted to provide the optimum therapeutic response. In some embodiments, several divided doses may be administered daily or the dose may be proportionally reduced as indicated by the exigencies of the therapeutic situation. In some embodiments, the effective dose range for a therapeutic compound of the invention is from about 1 and 5,000 mg/kg of body weight/per day. One of ordinary skill in the art would be able to study the relevant factors and make the determination regarding the effective amount of the therapeutic compound without undue experimentation. [0550] In some embodiments, the compound may be administered to a subject as frequently as several times daily, or it may be administered less frequently, such as once a day, once a week, once every two weeks, once a month, or even less frequently, such as once every several months or even once a year or less. In some embodiments, the amount of compound dosed per day may be administered, in non-limiting examples, every day, every other day, every 2 days, every 3 days, every 4 days, or every 5 days. In some embodiments, with every other day administration, a 5 mg per day dose may be initiated on Monday with a first subsequent 5 mg per day dose administered on Wednesday, a second subsequent 5 mg per day dose administered on Friday, and so on. The frequency of the dose will be readily apparent to the skilled artisan and will depend upon any number of factors, such as, but not limited to, the type and severity of the disease being treated, the type and age of the animal, etc. [0551] In some embodiments, dosage levels of the active ingredients in the pharmaceutical compositions of this invention may be varied so as to obtain an amount of the active ingredient that is effective to achieve the desired therapeutic response for a particular subject, composition, and mode of administration, without being toxic to the subject. [0552] A medical doctor, e.g., physician or veterinarian, having ordinary skill in the art may readily determine and prescribe the effective amount of the pharmaceutical composition required. In some embodiments, the physician or veterinarian could start doses of the compounds of the invention employed in the pharmaceutical composition at levels lower than that required in order to achieve the desired therapeutic effect and gradually increase the dosage until the desired effect is achieved. [0553] In some embodiments, it is especially advantageous to formulate the compound in dosage unit form for ease of administration and uniformity of dosage. In some embodiments, dosage unit form as used herein refers to physically discrete units suited as unitary dosages for the subjects to be treated; each unit containing a predetermined quantity of therapeutic compound calculated to produce the desired therapeutic effect in association with the required pharmaceutical vehicle. In some embodiments, the dosage unit forms of the invention are dictated by and directly dependent on (a) the unique characteristics of the therapeutic compound and the particular therapeutic effect to be achieved, and (b) the limitations inherent in the art of compounding/formulating such a therapeutic compound for the treatment of a disease in a subject. [0554] In some embodiments, the compositions provided herein containing a provided non- cell particle such as any of the viral vectors or virus-based particles described herein,can be formulated in dosage units of genome copies (GC). Suitable method for determining GC have been described and include, e.g., qPCR or digital droplet PCR (ddPCR) as described in, e.g., M. Lock et al, Hu Gene Therapy Methods, Hum Gene Ther Methods 25(2):115-25. 2014, which is incorporated herein by reference. In some embodiments, the dosage of administration of a viral vector or virus-like particle is from about 10 4 to about 10 10 GC units, inclusive. In some embodiments, the dosage of administration of a viral vector or virus-like particle is from about 10 9 to about 10 15 GC units, inclusive. In some embodiments, the dosage of administration of a viral vector or virus-like particle is from about 10 5 to about 10 9 GC units, inclusive. In some embodiments, the dosage of administration of a viral vector or virus-like particle is from about 10 6 to about 10 9 GC units, inclusive. In some embodiments, the dosage of administration of a viral vector or virus-like particle is from about 10 12 to about 10 14 GC units, inclusive. In some embodiments, the dosage of administration is 1.0×10 9 GC units, 5.0×10 9 GC units, 1.0×10 10 GC units, 5.0×10 10 GC units, 1.0×10 11 GC units, 5.0×10 11 GC units, 1.0×10 12 GC units, 5.0×10 12 GC units, or 1.0×10 13 GC units, 5.0×10 13 GC units, 1.0×10 14 GC units, 5.0×10 14 GC units, or 1.0×10 15 GC units. [0555] In some embodiments, the dosage of administration of a viral vector or virus-like particle is from about 10 4 to about 10 10 infectious units, inclusive. In some embodiments, the dosage of administration of a viral vector or virus-like particle is from about 10 9 to about 10 15 infectious units, inclusive In some embodiments, the dosage of administration of a viral vector or virus-like particle is from about 10 5 to about 10 9 infectious units. In some embodiments, the dosage of administration of a viral vector or virus-like particle is from about 10 6 to about 10 9 infectious units. In some embodiments, the dosage of administration of a viral vector or virus-like particle is from about 10 12 to about 10 14 infectious units, inclusive. In some embodiments, the dosage of administration is 1.0×10 9 infectious units, 5.0×10 9 infectious units, 1.0×10 10 infectious units, 5.0×10 10 infectious units, 1.0×10 11 infectious units, 5.0×10 11 infectious units, 1.0×10 12 infectious units, 5.0×10 12 infectious units, or 1.0×10 13 infectious units, 5.0×10 13 infectious units, 1.0×10 14 infectious units, 5.0×10 14 infectious units, or 1.0×10 15 infectious units. The techniques available for quantifing infectious units are routine in the art and include viral particle number determination, fluorescence microscopy, and titer by plaque assay. For example, the number of adenovirus particles can be determined by measuring the absorbance at A260. Similarly, infectious units can also be determined by quantitative immunofluorescence of vector specific proteins using monoclonal antibodes or by plaque assay. [0556] In some embodiments, methods that calculate the infectious units include the plaque assay, in which titrations of the virus are grown on cell monolayers and the number of plaques is counted after several days to several weeks. For example, the infectious titer is determined, such as by plaque assay, for example an assay to assess cytopathic effects (CPE). In some embodiments, a CPE assay is performed by serially diluting virus on monolayers of cells, such as HFF cells, that are overlaid with agarose. After incubation for a time period to achieve a cytopathic effect, such as for about 3 to 28 days, generally 7 to 10 days, the cells can be fixed and foci of absent cells visualized as plaques are determined. In some embodiments, infectious units can be determined using an endpoint dilution (TCID50) method, which determines the dilution of virus at which 50% of the cell cultures are infected and hence, generally, can determine the titer within a certain range, such as one log. [0557] In some embodiments, the dosage of administration of a viral vector or virus-like particle is from about 10 4 to about 10 10 plaque forming units (pfu), inclusive. In some embodiments, the dosage of administration of a viral vector or virus-like particle is from about 10 9 to about 10 15 pfu, inclusive In some embodiments, the dosage of administration of a viral vector or virus-like particle is from about 10 5 to about 10 9 pfu. In some embodiments, the dosage of administration of a viral vector or virus-like particle is from about 10 6 to about 10 9 pfu. In some embodiments, the dosage of administration of a viral vector or virus-like particle is from about 10 12 to about 10 14 pfu, inclusive. In some embodiments, the dosage of administration is 1.0×10 9 pfu, 5.0×10 9 pfu, 1.0×10 10 pfu, 5.0×10 10 pfu, 1.0×10 11 pfu, 5.0×10 11 pfu, 1.0×10 12 pfu, 5.0×10 12 pfu, or 1.0×10 13 pfu, 5.0×10 13 pfu, 1.0×10 14 pfu, 5.0×10 14 pfu, or 1.0×10 15 pfu. [0558] In some aspects, the dosage of administration of a vehicle within the pharmaceutical compositions provided herein varies depending on a subject’s body weight. For example, a composition may be formulated as GC/kg, infectious units/kg, pfu/kg, etc. In some aspects, the dosage at which a therapeutic effect is obtained is from at or about 10 8 GC/kg to at or about 10 14 GC/kg of the subject’s body weight, inclusive. In some aspects, the dosage at which a therapeutic effect is obtained is at or about 10 8 GC/kg of the subject’s body weight (GC/kg). [0559] In some of any embodiments, the compositions of the invention are administered to the subject in dosages that range from one to five times per day or more. In another embodiment, the compositions of the invention are administered to the subject in range of dosages that include, but are not limited to, once every day, every two, days, every three days to once a week, and once every two weeks. It will be readily apparent to one skilled in the art that the frequency of administration of the various combination compositions of the invention will vary from subject to subject depending on many factors including, but not limited to, age, disease or disorder to be treated, gender, overall health, and other factors [0560] In some embodiments, compounds for administration may be in the range of from about 1 mg to about 10,000 mg, about 20 mg to about 9,500 mg, about 40 mg to about 9,000 mg, about 75 mg to about 8,500 mg, about 150 mg to about 7,500 mg, about 200 mg to about 7,000 mg, about 3050 mg to about 6,000 mg, about 500 mg to about 5,000 mg, about 750 mg to about 4,000 mg, about 1 mg to about 3,000 mg, about 10 mg to about 2,500 mg, about 20 mg to about 2,000 mg, about 25 mg to about 1,500 mg, about 50 mg to about 1,000 mg, about 75 mg to about 900 mg, about 100 mg to about 800 mg, about 250 mg to about 750 mg, about 300 mg to about 600 mg, about 400 mg to about 500 mg, and any and all whole or partial increments there between. [0561] In some embodiments, the dose of a compound is from about 1 mg and about 2,500 mg. In some embodiments, a dose of a compound used in compositions described herein is less than about 10,000 mg, or less than about 8,000 mg, or less than about 6,000 mg, or less than about 5,000 mg, or less than about 3,000 mg, or less than about 2,000 mg, or less than about 1,000 mg, or less than about 500 mg, or less than about 200 mg, or less than about 50 mg. Similarly, in some embodiments, a dose of a second compound (i.e., a drug used for treating the same or another disease as that treated by the compositions of the invention) as described herein is less than about 1,000 mg, or less than about 800 mg, or less than about 600 mg, or less than about 500 mg, or less than about 400 mg, or less than about 300 mg, or less than about 200 mg, or less than about 100 mg, or less than about 50 mg, or less than about 40 mg, or less than about 30 mg, or less than about 25 mg, or less than about 20 mg, or less than about 15 mg, or less than about 10 mg, or less than about 5 mg, or less than about 2 mg, or less than about 1 mg, or less than about 0.5 mg, and any and all whole or partial increments thereof. [0562] In some of any embodiments, the present disclosure is directed to a packaged pharmaceutical composition comprising a container holding a therapeutically effective amount of a compound or conjugate of the invention, alone or in combination with a second pharmaceutical agent; and instructions for using the compound or conjugate to treat, prevent, or reduce one or more symptoms of a disease in a subject. [0563] In some embodiments, the term “container” includes any receptacle for holding the pharmaceutical composition. In some embodiments, the container is the packaging that contains the pharmaceutical composition. In other embodiments, the container is not the packaging that contains the pharmaceutical composition, i.e., the container is a receptacle, such as a box or vial that contains the packaged pharmaceutical composition or unpackaged pharmaceutical composition and the instructions for use of the pharmaceutical composition. It should be understood that the instructions for use of the pharmaceutical composition may be contained on the packaging containing the pharmaceutical composition, and as such the instructions form an increased functional relationship to the packaged product. In some embodiments, instructions may contain information pertaining to the compound's ability to perform its intended function, e.g., treating or preventing a disease in a subject, or delivering an imaging or diagnostic agent to a subject. [0564] In some embodiments, routes of administration of any of the compositions disclosed herein include oral, nasal, rectal, parenteral, sublingual, transdermal, transmucosal (e.g., sublingual, lingual, (trans)buccal, (trans)urethral, vaginal (e.g., trans- and perivaginally), (intra)nasal, and (trans)rectal), intravesical, intrapulmonary, intraduodenal, intragastrical, intrathecal, subcutaneous, intramuscular, intradermal, intra-arterial, intravenous, intrabronchial, inhalation, and topical administration. [0565] In some of any embodiments, suitable compositions and dosage forms include, for example, tablets, capsules, caplets, pills, gel caps, troches, dispersions, suspensions, solutions, syrups, granules, beads, transdermal patches, gels, powders, pellets, magmas, lozenges, creams, pastes, plasters, lotions, discs, suppositories, liquid sprays for nasal or oral administration, dry powder or aerosolized formulations for inhalation, compositions and formulations for intravesical administration and the like. [0566] In some embodiments, delivery of a non-cell particle composition described herein may induce or block cellular differentiation, de-differentiation, or trans-differentiation. In some embodiments, the target mammalian cell may be a precursor cell. In some embodiments, the target mammalian cell may be a differentiated cell, and the cell fate alteration includes driving de -differentiation into a pluripotent precursor cell, or blocking such de-differentiation. In some embodiments, the effective amounts of a non-cell particle described herein encoding a cell fate inductive molecule or signal is introduced into a target cell under conditions such that an alteration in cell fate is induced. In some embodiments, a non-cell particle described herein is useful to reprogram a subpopulation of cells from a first phenotype to a second phenotype. In some embodiments, reprogramming may be temporary or permanent. In some embodiments, the reprogramming induces a target cell to adopt an intermediate phenotype. [0567] Provided herein are methods of reducing cellular differentiation in a target cell population. In some embodiments, a target cell population containing one or more precursor cell types is contacted with a non-cell particles composition described herein, under conditions such that the composition reduces the differentiation of the precursor cell. In certain embodiments, the target cell population contains injured tissue in a mammalian subject or tissue affected by a surgical procedure. The precursor cell is, e.g., a stromal precursor cell, a neural precursor cell, or a mesenchymal precursor cell. [0568] In some embodiments, the non-cell particle composition comprising a cargo, may be used to deliver such cargo to a cell tissue or subject. In some embodiments, delivery of a cargo by administration of a non-cell particle composition described herein may modify cellular protein expression levels. In certain embodiments, the administered composition directs upregulation of (via expression in the cell, delivery in the cell, or induction within the cell) of one or more cargo (e.g., a polypeptide or mRNA) that provide a functional activity which is substantially absent or reduced in the cell in which the polypeptide is delivered. In some embodiments, the missing functional activity may be enzymatic, structural, or regulatory in nature. In some embodiments, the administered composition directs up-regulation of one or more polypeptides that increases (e.g., synergistically) a functional activity which is present but substantially deficient in the cell in which the polypeptide is upregulated. In some of any embodiments, the administered composition directs downregulation of (via expression in the cell, delivery in the cell, or induction within the cell) of one or more cargo (e.g., a polypeptide, siRNA, or miRNA) that repress a functional activity which is present or upregulated in the cell in which the polypeptide, siRNA, or miRNA is delivered. In some of any embodiments, the upregulated functional activity may be enzymatic, structural, or regulatory in nature. In some embodiments, the administered composition directs down-regulation of one or more polypeptides that decreases (e.g., synergistically) a functional activity which is present or upregulated in the cell in which the polypeptide is downregulated. In some embodiments, the administered composition directs upregulation of certain functional activities and downregulation of other functional activities. [0569] In some of any embodiments, the non-cell particle composition (e.g., one comprising mitochondria or DNA) mediates an effect on a target cell, and the effect lasts for at least 1, 2, 3, 4, 5, 6, or 7 days, 2, 3, or 4 weeks, or 1, 2, 3, 6, or 12 months. In some embodiments (e.g., wherein the non-cell particle composition comprises an exogenous protein), the effect lasts for less than 1, 2, 3, 4, 5, 6, or 7 days, 2, 3, or 4 weeks, or 1, 2, 3, 6, or 12 months. [0570] In some of any embodiments, the non-cell particle composition described herein is delivered ex-vivo to a cell or tissue, e.g., a human cell or tissue. In embodiments, the composition improves function of a cell or tissue ex-vivo, e.g., improves cell viability, respiration, or other function (e.g., another function described herein). [0571] In some embodiments, the composition is delivered to an ex vivo tissue that is in an injured state (e.g., from trauma, disease, hypoxia, ischemia or other damage). [0572] In some embodiments, the composition is delivered to an ex-vivo transplant (e.g., a tissue explant or tissue for transplantation, e.g., a human vein, a musculoskeletal graft such as bone or tendon, cornea, skin, heart valves, nerves; or an isolated or cultured organ, e.g., an organ to be transplanted into a human, e.g., a human heart, liver, lung, kidney, pancreas, intestine, thymus, eye). In some embodiments, the composition is delivered to the tissue or organ before, during and/or after transplantation. [0573] In some embodiments, the composition is delivered, administered or contacted with a cell, e.g., a cell preparation. In some embodiments, the cell preparation may be a cell therapy preparation (a cell preparation intended for administration to a human subject). In embodiments, the cell preparation comprises cells expressing a chimeric antigen receptor (CAR), e.g., expressing a recombinant CAR. The cells expressing the CAR may be, e.g., T cells, Natural Killer (NK) cells, cytotoxic T lymphocytes (CTL), regulatory T cells. In embodiments, the cell preparation is a neural stem cell preparation. In embodiments, the cell preparation is a mesenchymal stem cell (MSC) preparation. In embodiments, the cell preparation is a hematopoietic stem cell (HSC) preparation. In embodiments, the cell preparation is an islet cell preparation. [0574] In some embodiments, the non-cell particle compositions described herein can be administered to a subject, e.g., a mammal, e.g., a human. In such embodiments, the subject may be at risk of, may have a symptom of, or may be diagnosed with or identified as having, a particular disease or condition (e.g., a disease or condition described herein). [0575] In some embodiments, the source of non-cell particles are from the same subject that is administered a non-cell particle composition. In other embodiments, they are different. In some embodiments, the source of non-cell particles and recipient tissue may be autologous (from the same subject) or heterologous (from different subjects). In some embodiments, the donor tissue for non-cell particle compositions described herein may be a different tissue type than the recipient tissue. In some embodiments, the donor tissue may be muscular tissue and the recipient tissue may be connective tissue (e.g., adipose tissue). In other embodiments, the donor tissue and recipient tissue may be of the same or different type, but from different organ systems. [0576] In some embodiments, the non-cell particle composition described herein may be administered to a subject having a cancer, an autoimmune disease, an infectious disease, a metabolic disease, a neurodegenerative disease, or a genetic disease (e.g., enzyme deficiency). In some embodiments, the subject is in need of regeneration. [0577] In some embodiments, the non-cell particle is co-administered with an inhibitor of a protein that inhibits membrane fusion. For example, Suppressyn is a human protein that inhibits cell-cell fusion (Sugimoto et al., "A novel human endogenous retroviral protein inhibits cell-cell fusion" Scientific Reports 3: 1462 DOI: 10.1038/srep01462). In some embodiments, the non-cell particles is co-administered with an inhibitor of sypressyn, e.g., a siRNA or inhibitory antibody. IX. EXEMPLARY EMBODIMENTS [0578] Among the provided embodiments are: 1. A non-cell particle comprising CD24 or a biologically active portion thereof on an exposed surface of the particle, wherein the non-cell particle is 1 µm or smaller. 2. The non-cell particle of embodiment 1, wherein the CD24 or the biologically active portion thereof binds Siglec-10. 3. The non-cell particle of embodiment 1 or embodiment 2, wherein the CD24 or biologically active portion thereof is human. 4. The non-cell particle of any of embodiments 1-3, wherein the CD24 or biologically active portion thereof: (i) comprises the sequence set forth in SEQ ID NO: 2; (ii) an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:2 that binds Siglec-10; or (iii) a binding portion of (i) or (ii) that binds to Siglec-10. 5. The non-cell particle of any of embodiments 1-4, wherein the CD24 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:2. 6. The non-cell particle of any of embodiments 1-5, wherein the CD24 or biologically active portion is displayed on an exposed surface of the particle via a Glycosylphosphatidylinositol (GPI) membrane anchor. 7. The non-cell particle of any of embodiments 1-6, wherein the CD24 or the biologically active portion thereof is encoded by a nucleic molecule encoding the sequence set forth in SEQ ID NO:3 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:3 that binds Siglec-10. 8. The non-cell particle of any of embodiments 1-6, wherein the CD24 or the biologically active portion thereof is encoded by a nucleic molecule encoding the sequence set forth in SEQ ID NO:15 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:15 that binds Siglec-10. 9. The non-cell particle of any of embodiments 1-5, wherein the CD24 or biologically active portion is displayed on an exposed surface of the particle via a transmembrane domain. 10. The non-cell particle of any of embodiments 1-9, wherein the CD24 or biologically active portion is a glycoprotein 11. The non-cell particle of any of embodiments 1-10, wherein the CD24 or biologically active portion is sialylated. 12. The non-cell particle of any of embodiments 1-11, wherein the CD24 or biologically active portion comprises an a2-3-linked sialoside and/or an a2-6-linked sialoside. 13. The non-cell particle of any of embodiments 1-12, wherein the CD24 or biologically active portion has a molecular weight of between at or about 35 kDa and at or about 45 kDa. 14. The non-cell particle of any of embodiments 1-13, wherein the non-cell particle further comprises a CD47 or a biologically active portion thereof on an exposed surface of the non-cell particle. 15. The non-cell particle of embodiment 14, wherein the CD47 or biologically active portion binds to SIRPa. 16. The non-cell particle of embodiment 14 or embodiment 15, wherein the CD47 or biologically active portion is human. 17. The non-cell particle of any one of embodiments 14-16, wherein the CD47 or biologically active portion comprises the extracellular domain or CD47 or a binding portion thereof that binds to SIRPa. 18. The non-cell particle of any of embodiments 14-17, wherein the CD47 or biologically active portion thereof: (i) comprises the sequence set forth in SEQ ID NO: 7; (ii) an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:7 that binds to SIRPa; or (iii) a binding portion of (i) or (ii) that binds to SIRPa. 19. The non-cell particle of any of embodiments 14-18, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:7. 20. The non-cell particle of any of embodiments 14-18, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:11. 21. The non-cell particle of any of embodiments 14-18 and 20, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:9. 22. The non-cell particle of any of embodiments 14-18 and 20, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:10. 23. The non-cell particle of any of embodiments 14-18 and 20, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:12. 24. The non-cell particle of any of embodiments 14-23, wherein the CD47 or biologically active portion is displayed on an exposed surface of the particle via a transmembrane domain. 25. The non-cell particle of any of embodiments 14-19 and 24, wherein the CD47 or biologically active portion comprises SEQ ID NO: 8 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% identity to SEQ ID NO:8 that binds to SIRPa. 26. The non-cell particle of any of embodiments 14-19, 24 and 25, wherein the CD47 or the biologically active portion thereof is encoded by a nucleic molecule encoding the sequence set forth in SEQ ID NO:5 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:5 that binds to SIRPa. 27. The non-cell particle of any of embodiments 1-26, wherein the non-cell particle is a synthetic particle, a viral particle or a cell-derived particle. 28. The non-cell particle of any of embodiments 1-17, wherein further comprising a nucleic acid comprising a payload gene encoding an exogenous agent. 29. The non-cell particle of any of embodiments 1-28, wherein the non-cell particle is a synthetic particle selected from the group consisting of a liposome, a microparticle, a nanoparticle, a nanogel, a dendrimer and a dendrisome. 30. The non-cell particle of any of embodiments 1-28, wherein the exposed surface is a lipid bilayer and the non-cell particle further comprises a lumen comprising a cytosol, wherein the lumen is surrounded by the lipid bilayer. 31. The non-cell particle of embodiment 30, wherein the lumen further comprises a nucleic acid comprising a payload gene encoding an exogenous agent. 32. The non-cell particle of embodiment 30 or embodiment 31, wherein the non-cell particle is a fusosome and the lipid bilayer further comprises a fusogen. 33. The non-cell particle of any of embodiments 1-28 and 30-32, wherein the non- cell particle is derived from a source cell. 34. The non-cell particle of any of embodiments 1-33, wherein the non-cell particle does not comprise a nucleus. 35. The non-cell particle of any of embodiments 1-28 and 30-32, wherein the non- cell particle is a virus particle or a virus-like particle (VLP). 36. The non-cell particle of embodiments 35, wherein the virus particle or virus-like particle is a retroviral particle or retrovirus-like particle. 37. The non-cell particle of embodiment 36, wherein the retroviral particle or retrovirus-like particle is a lentiviral particle or a lentiviral-like particle. 38. The non-cell particle of any of embodiments 35-37, comprising a fusogen that is a viral fusogen selected from a Class I viral membrane fusion protein, a Class II viral membrane protein, a Class II viral membrane fusion protein, a viral membrane glycoprotein, or a viral envelope protein. 39. The non-cell particle of embodiment 38, wherein the fusogen is endogenous to the virus. 40. The non-cell particle of embodiment 38, wherein the fusogen is a pseudotyped fusogen. 41. The non-cell particle of any of embodiments 32-40, wherein the fusogen is a re- targeted fusogen that binds to a target cell. 42. The non-cell particle of embodiment 41, wherein the fusogen comprises a targeting moiety that binds to the target cell. 43. The non-cell particle of any of embodiments 35-42, wherein the virus or virus- like particle further comprising a lumen comprising a nucleic acid. 44. The non-cell particle of embodiment 43, wherein the nucleic acid comprises a viral nucleic acid comprising one or more of (e.g., all of) the following nucleic acid sequences: 5’ LTR (e.g., comprising U5 and lacking a functional U3 domain), Psi packaging element (Psi), Central polypurine tract (cPPT)/central termination sequence (CTS) (e.g. DNA flap), Poly A tail sequence, a posttranscriptional regulatory element (e.g. WPRE), a Rev response element (RRE), and 3’ LTR (e.g., comprising U5 and lacking a functional U3). 45. The non-cell particle of any of embodiments 35-44, wherein the non-cell particle is a virus-like particle (e.g. retrovirus-like particle) that is a replication defective. 46. A pseudotyped lentivirus or lentiviral-like particle comprising CD24 or a biologically active portion thereof on an exposed surface of the lentiviral particle. 47. The pseudotyped lentivirus or lentiviral-like particle of embodiment 46, wherein the particle is pseudotyped with a vesicular stomatitis virus envelope glycoprotein (VSV-G). 48. The pseudotyped lentivirus or lentiviral particle of embodiment 46, wherein the lentiviral particle is pseudotyped with a protein derrived from an envelope glycoprotein of a virus of the Paramyxovirus family. 49. The pseudotyped lentivirus or lentiviral-like particle of embodiment 46, wherein the particle is pseudotyped with a cell targeting fusion protein comprising a protein derived from a Paramyxoviridae envelope protein G or H or a biologically active portion thereof and at least one cell targeting domain. 50. The pseudotyped lentivirus or lentiviral particle of embodiment 48 or embodiment 49, wherein the virus of the Paramyxovirus family is a Henipavirus or is a Morbillivirus. 51. The pseudotyped lentivirus or lentiviral particle of any of embodiments 48-50, wherein the envelope glycoprotein is an envelope glycoprotein G or H or a biologically active portion thereof. 52. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 48- 51, wherein the envelope glycoprotein is Nipah virus G (Niv-G) protein or a biologically active portion thereof. 53. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 48- 51, wherein the envelope glycoprotein is a Hendra virus G protein or a biologically active portion thereof. 54. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 48- 51, wherein the envelope glycoprotein is a measles virus glycoprotein or a biologically active portion thereof. 55. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 48- 54, wherein said protein derived from an envelope glycoprotein G or H of a virus of the Paramyxoviridae family is at least partially unable to bind at least one natural receptor of said envelope glycoprotein G or H. 56. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 48- 55, furtehr comprising an F protein molecule or a biologically active portion thereof from a Paramyxovirus. 57. The pseudotyped lentivirus or lentiviral-like particle of embodiment 56, wherein the Paramyxovirus is a Henipavirus. 58. The pseudotyped lentivirus or lentiviral-like particle of embodiment 56 or embodiment 57, wherein the protein protein molecule or a biologically active portion is a NiV-F protein or a biologically active portion. 59. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 46- 58, wherein the CD24 or biologically active portion thereof: (i) comprises the sequence set forth in SEQ ID NO: 2; (ii) an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:2 that binds to Siglec-10; or (iii) a binding portion of (i) or (ii) that binds to Siglec-10. 60. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 46- 59, wherein the CD24 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:2. 61. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 46- 60, wherein the CD24 or biologically active portion is displayed on an exposed surface of the particle via a Glycosylphosphatidylinositol (GPI) membrane anchor. 62. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 46- 61, wherein the CD24 or the biologically active portion thereof is encoded by a nucleic molecule encoding the sequence set forth in SEQ ID NO:3 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:3 that binds to Siglec- 10. 63. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 46- 62, wherein the CD24 or the biologically active portion thereof is encoded by a nucleic molecule encoding the sequence set forth in SEQ ID NO:15 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:15 that binds to Siglec- 10. 64. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 46- 60, wherein the CD24 or biologically active portion is displayed on an exposed surface of the particle via a transmembrane domain. 65. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 46- 64, wherein the CD24 or biologically active portion is a glycoprotein 66. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 46- 65, wherein the CD24 or biologically active portion is sialylated. 67. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 46- 66, wherein the CD24 or biologically active portion comprises an a2-3-linked sialoside and/or an a2-6-linked sialoside. 68. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 46- 67, wherein the CD24 or biologically active portion has a molecular weight of between at or about 35 kDa and at or about 45 kDa. 69. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 46- 68, wherein the non-cell particle further comprises a CD47 or a biologically active portion thereof on an exposed surface of the non-cell particle. 70. The pseudotyped lentivirus or lentiviral-like particle of embodiment 69, wherein the CD47 or biologically active portion binds to SIRPa. 71. The pseudotyped lentivirus or lentiviral-like particle of embodiment 69 or embodiment 70, wherein the CD47 or biologically active portion is human. 72. The pseudotyped lentivirus or lentiviral-like particle of any one of embodiments 69-71, wherein the CD47 or biologically active portion comprises the extracellular domain or CD47 or a binding portion thereof that binds to SIRPa. 73. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 69- 72, wherein the CD47 or biologically active portion thereof: (i) comprises the sequence set forth in SEQ ID NO: 7; (ii) an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:7 that binds to SIRPa; or (iii) a binding portion of (i) or (ii) that binds to SIRPa. 74. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 69- 73, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:7. 75. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 69- 73, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:11. 76. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 69- 73 and 75, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:9. 77. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 69- 73 and 75, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:10. 78. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 69- 73 and 77, wherein the CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:12. 79. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 69- 78, wherein the CD47 or biologically active portion is displayed on an exposed surface of the particle via a transmembrane domain. 80. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 69- 74 and 79, wherein the CD47 or biologically active portion comprises SEQ ID NO: 8 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% identity to SEQ ID NO:8 that binds to SIRPa. 81. The pseudotyped lentivirus or lentiviral-like particle of any of embodiments 69- 74, 79 and 80, wherein the CD47 or the biologically active portion thereof is encoded by a nucleic molecule encoding the sequence set forth in SEQ ID NO:5 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:5 that binds to SIRPa. 82. The non-cell particle of any of embodiments 1-45 or the pseudotyped lentivirus or lentiviral-like particle of any of embodiments 46-81, further comprising a nucleic acid comprising a payload gene encoding an exogenous agent. 83. The non-cell particle of embodiment 28, embodiment 31 or embodiment 82 or the pseudotyped lentivirus or lentiviral-like particle of embodiment 82, wherein the exogenous agent encodes a therapeutic agent or a diagnostic agent. 84. The non-cell particle of any of embodiments 1-45, 82 and 83 or the pseudotyped lentivirus or lentiviral-like particle of any of embodiments 46-83, wherein phagocytosis of the particle by a phagocytic cells, optionally a macrophage, is reduced compared to a reference particle that is otherwise similar but does not comprise the CD24 or biologically active portion, optionally wherein phagocytosis is reduced by at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, or 90%. 85. The non-cell particle of any of embodiments 1-45 and 82-84 or the pseudotyped lentivirus or lentiviral-like particle of any of embodiments 46-84, wherein the half-life of the particle in vivo is increased compared to a reference particle that is otherwise similar but does not comprise the CD24 or biologically active portion, optionally wherein the half-life is increased by at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, or 90%. 86. A polynucleotide comprising a first nucleic acid sequence encoding CD24 or a biologically active portion and a second nucleic acid encoding CD47 or a biologically active portion. 87. The polynucleotide of embodiment 86, wherein the encoded CD24 or the biologically active portion thereof binds Siglec-10. 88. The polynucleotide of embodiment 86 or embodiment 87, wherein the encoded CD24 or biologically active portion thereof is human. 89. The polynucleotide of any of embodiments 84-88, wherein the encoded CD24 or biologically active portion thereof: (i) comprises the sequence set forth in SEQ ID NO: 2; (ii) an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:2 that binds to Siglec-10; or (iii) a binding portion of (i) or (ii) that binds to Siglec-10. 90. The polynucleotide of any of embodiments 84-89, wherein the encoded CD24 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:2. 91. The polynucleotide of any of embodiments 84-90, wherein the encoded CD24 or biologically active portion is displayed on an exposed surface of the particle via a Glycosylphosphatidylinositol (GPI) membrane anchor. 92. The polynucleotide of any of embodiments 84-91, wherein: the first nucleic acid encoding CD24 or a biologically active portion encodes the sequence set forth in SEQ ID NO:3 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:3 that binds to Siglec-10; or the first nucleic acid encoding CD24 or a biologically active portion encodes the sequence set forth in SEQ ID NO:15 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:15 that binds to Siglec-10. 93. The polynucleotide of any of embodiments 84-92, wherein the first nucleic acid encoding CD24 comprises the sequence set forth in SEQ ID NO:4 or a sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:4; 94. The polynucleotide of any of embodiments 84-93, wherein the encoded CD47 or biologically active portion binds to SIRPa. 95. The polynucleotide of any of embodiments 84-94, wherein the encoded CD47 or biologically active portion is human. 96. The polynucleotide of any of embodiments 84-95, wherein the encoded CD47 or biologically active portion comprises the extracellular domain or CD47 or a binding portion thereof that binds to SIRPa. 97. The polynucleotide of any of embodiments 84-96, wherein the encoded CD47 or biologically active portion thereof: (i) comprises the sequence set forth in SEQ ID NO: 7; (ii) an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:7 that binds to SIRPa; or (iii) a binding portion of (i) or (ii) that binds to SIRPa. 98. The polynucleotide of any of embodiments 84-97, wherein the encoded CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:7. 99. The polynucleotide of any of embodiments 84-97, wherein the encoded CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:11. 100. The polynucleotide of any of embodiments 84-97 and 99, wherein the encoded CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:9 101. The polynucleotide of any of embodiments 84-97 and 99, wherein the encoded CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:10. 102. The polynucleotide of any of embodiments 84-97 and 99, wherein the encoded CD47 or biologically active portion thereof comprises the sequence set forth in SEQ ID NO:12. 103. The polynucleotide of any of embodiments 84-102, wherein the encoded CD47 or biologically active portion comprises a transmembrane domain. 104. The polynucleotide of any of embodiments 84-103, wherein: the second nucleic acid encodes the sequence set forth in SEQ ID NO: 5 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% identity to SEQ ID NO:5 that binds to SIRPa; or the second nucleic acid encodes the sequence set forth in SEQ ID NO: 8 or an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% identity to SEQ ID NO:8 that binds to SIRPa. 105. The polynucleotide of any of embodiments 84-104, wherein the second nucleic acid encoding CD47 comprises the sequence set forth in SEQ ID NO:13 or a sequence having at least at or about 90%, at least at or about 91%, at or about 92%, at least at or about 93%, at least at or about 94%, at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% identity to SEQ ID NO:13. 106. The polynucleotide of any of embodiments 84-105, further comprising at least one promoter that is operatively linked to control expression of the CD24 or biologically active portion and/or the CD47 or biologically active portion. 107. The polynucleotide of any of embodiments 84-106, wherein the first and second nucleic acid are operatively linked to the same promoter. 108. The polynucleotide of any of embodiments 84-106, wherein the first nucleic acid is operatively linked to a first promoter and the second nucleic acid is operatively linked to a second promoter. 109. The polynucleotide of embodiment 108, wherein the first and second promoter are different. 110. The polynucleotide of any of embodiments 106-109, wherein the promoter, or each promoter individually, is a heterologous promoter. 111. The polynucleotide of any of embodiments 106-110, wherein the promoter, or each promoter individually, is an inducible promoter. 112. The polynucleotide of any of embodiments 84-111, further comprising a nucleic acid sequence encoding a linking peptide between the first and second nucleic acid sequences, wherein the linking peptide separates the translation products of the first and second nucleic acid sequences during or after translation. 113. The polynucleotide of embodiment 112, wherein the linking peptide comprises an internal ribosome entry site (IRES), a self-cleaving peptide, or a peptide that causes ribosome skipping, optionally a T2A peptide. 114. A vector, comprising the polynucleotide of any of embodiments 84-112. 115. The vector of embodiment 114, wherein the vector is a mammalian vector, viral vector or artificial chromosome, optionally wherein the artificial chromosome is a bacterial artificial chromosome (BAC). 116. A method of making a non-cell particle comprising CD24 or a biologically active portion, comprising: a) providing a cell that comprises a nucleic acid encoding CD24 or a biologically active portion thereof; b) culturing the cell under conditions that allow for production of a non-cell particle, and c) separating, enriching, or purifying the particle from the cell, thereby making the fusosome. 117. The method of embodiment 116, wherein the cell further comprises a nucleic acid encoding CD47 or a biologically active portion thereof or the nucleic acid further encodes CD47 or a biologically active portion thereof. 118. A method of making a non-cell particle comprising CD24 or a biologically active portion, comprising: a) providing a cell that comprises the polynucleotide of any of embodiments 84-112 or the vector of embodiment 114 or embodiment 115; b) culturing the cell under conditions that allow for production of a non-cell particle, and c) separating, enriching, or purifying the non-cell particle from the cell, thereby making the fusosome. 119. The method of any of embodiments 116-118, wherein the cell is a mammalian cell and the non-cell particle is a vesicle or an exosome, optionally wherein the vesicle is a microvesicle or a nanovesicle. 120. The method of any of embodiments 116-118, wherein the cell is a producer cell and the non-cell particle is a viral particle or a viral-like particle, optionally a retroviral particle or a retroviral-like particle, optionally a lentiviral particle or lentiviral-like particle. 121. The method of any of embodiments 116-120, wherein the cell further comprises an exogenous nucleic acid sequence encoding an exogenous agent. 122. The method of any of embodiments 116-121, wherein the cell further comprises a fusogen. 123. A non-cell particle made by the method of any of embodiments 116-122. 124. A mammalian cell comprising (i) a viral nucleic acid(s) and (ii) nucleic acid encoding an exogenous CD24 or a biologically active portion thereof, optionally wherein the viral nucleic acid(s) are lentiviral nucleic acids. 125. The mammalian cell of embodiment 124, wherein the viral nucleic acid(s) lacks one or more genes involved in viral replication. 126. The mammalian cell of embodiment 124 or embodiment 125, wherein the viral nucleic acid comprises: one or more of (e.g., all of) the following nucleic acid sequences: 5’ LTR (e.g., comprising U5 and lacking a functional U3 domain), Psi packaging element (Psi), Central polypurine tract (cPPT)/central termination sequence (CTS) (e.g. DNA flap), Poly A tail sequence, a posttranscriptional regulatory element (e.g. WPRE), a Rev response element (RRE), and 3’ LTR (e.g., comprising U5 and lacking a functional U3); a nucleic acid encoding a viral envelope protein; and/or a nucleic acid encoding a viral packaging protein selected from one or more of Gag, Pol, Rev and Tat. 127. The mammalian cell of any of embodiments 124-126, wherein the the exogenous CD24 or biologically active portion comprises: (i) the sequence set forth in SEQ ID NO: 2; (ii) an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:2 that binds Siglec-10; or (iii) a binding portion of (i) or (ii) that binds to Siglec-10. 128. The mammalian cell of embodiment 127, wherein the nucleic acid encoding exogenous CD24 further encodes a a Glycosylphosphatidylinositol (GPI) membrane anchor signal sequence or a transmembrane domain. 129. The mammalian cell of any of embodiments 124-128, wherein the cell further comprises a nucleic acid encoding exogenous CD47 or a biologically active portion. 130. The mammalian cell of embodiment 129, wherein the exogenous CD47 or biologically active portion comprises: (i) the sequence set forth in SEQ ID NO: 7; (ii) an amino acid sequence having at least at or about 90%, at least at or about 91%, at least at or about 92%, at least at or about 93%, at least at or about 94%, at least at or about 95%, at least at or about 96%, at least at or about 97%, at least at or about 98%, or at least at or about 99% sequence identity to SEQ ID NO:7 that binds to SIRPa; or (iii) a binding portion of (i) or (ii) that binds to SIRPa. 131. The mammalian cell of embodiment 130, wherein the nucleic acid encoding exogenous CD47 further encodes a Glycosylphosphatidylinositol (GPI) membrane anchor signal sequence or a transmembrane domain. 132. The mammalian cell of any of embodiments 124-131, wherein the nucleic acid encoding the exogenous CD24 or biologically active portion and the nucleic acid encoding the exogenous CD47 or biologically active portion are encoded by the polynucleotide of any of embodiments 84-112. 133. A viral vector particle or viral-like particle produced from the mammalian cell of any of embodiments 124-132. 134. A composition comprising a plurality of non-cell particles of any of embodiments 1-45. 135. A composition comprising a plurality of pseudotyped lentivirus or lentiviral-like particles of any of embodiments 46-81. 136. The composition of embodiment 134 or embodiment 135 further comprising a pharmaceutically acceptable carrier. 137. The pharmaceutical composition of any of embodiments 134-136, wherein the plurality of particles comprise an average diameter of less than 1 µm. 138. A method of delivering an exogenous agent to a subject (e.g., a human subject) , the method comprising administering to the subject the non-cell particle of any of embodiments 1-45 or the pseudotyped lentivirus or lentiviral-like particles of any of embodiments 46-81 or the composition of any of embodiments 134-137. 139. A method of treating a disease or disorder in a subject (e.g., a human subject), the method comprising administering to the subject a non-cell particle of any of embodiments 1-45 or the pseudotyped lentivirus or lentiviral-like particles of any of embodiments 46-81 or the composition of any of embodiments 134-137. 140. A method of evading phagocytosis of a particle by a phagocytic cell, the method comprising contacting a phagocytic cell with a non-cell particle of any of embodiments 1-45 or the pseudotyped lentivirus or lentiviral-like particles of any of embodiments 46-81 or the composition of any of embodiments 134-137, whereby said particles evades phacocytosis by said phagocytic cell. 141. A method of increasing the life of a particle in vivo in a mammal, method comprising administering the non-cell particle of any of embodiments 1-45 or the pseudotyped lentivirus or lentiviral-like particles of any of embodiments 46-81 or the composition of any of embodiments 134-137 to a mammalian subject wherein said administered particles have a longer half-life in said mammal than an otherwise similar particle that does not have CD24 expressed thereon. 142. The non-cell particle of any of embodiments 1-27, 29, 30, and 32-45, further comprising an exogenous agent. 143. The non-cell particle of any of embodiments 28, 31, 82, 83, and 142, wherein the exogenous agent comprises a protein. 144. The non-cell particle of any of embodiments 28, 31, 82, 83, 142, and 143, wherein the exogenous agent comprises a membrane protein. 145. The non-cell particle of any of embodiments 28, 31, 82, 83, and 142-144, wherein the exogenous agent comprises a chimeric antigen receptor (CAR), a T cell receptor, an integrin, an ion channel, a pore forming protein, a Toll-Like Receptor, an interleukin receptor, a cell adhesion protein, or a transport protein. 146. The non-cell particle of any of embodiments 28, 31, 82, 83, and 142-145, wherein the exogenous agent comprises a CAR comprising an antigen binding domain, a transmembrane domain, and one or more signaling domains. 147. The non-cell particle of embodiment 146, wherein the antigen binding domain binds to a surface antigen characteristic of a cell type or a disorder. 148. The non-cell particle of embodiment 146 or 147, wherein the antigen binding domain binds to a surface antigen characteristic of a neoplastic cell, a T cell, an autoimmune or inflammatory disorder, a senescent cell, or an infectious disease. 149. A method of delivering an exogenous agent to a subject (e.g., a human subject), the method comprising administering to a subject the non-cell particle of any of embodiments 28, 31, 82, 83, and 142-148, wherein the payload gene encoding the exogenous agent or the exogenous agent is delivered to a target cell. 150. The method of embodiment 149, wherein the exogenous agent is a CAR. 151. The method of embodiment 149 or embodiment 150, wherein the target cell is a T cell. 152. The method of any of embodiments 149-151, wherein the target cell is any of a CD4+ T cell, a CD8+ T cell, an alpha beta T cell, a gamma delta T cell, a naive T cell, an effector T cell, a cytotoxic T cell (e.g., a CD8+ cytotoxic T cell), a regulatory T cell (e.g., a thymus-derived regulatory T cell, a peripherally derived regulatory T cell, a CD4+Foxp3+ regulatory T cell, or a CD4+FoxP3- type 1 regulatory T (Trl) cell), a helper T cell (e.g., a CD4+ helper T cell, a Thl cell, a Th2 cell, a Th3 cell, a Th9 cell, a Thl7 cell, a Th22 cell, or a T follicular helper (Tfh) cell), a memory T cell (e.g., a stem cell memory T cell, a central memory T cell, or an effector memory T cell), a NKT cell, and a Mucosal associated invariant T (MAIT) cell. X. EXAMPLES [0579] The following examples are included for illustrative purposes only and are not intended to limit the scope of the invention. Example 1: Modification of retroviral vector with CD24 to evade macrophage phagocytosis [0580] This Example describes quantification of the evasion of phagocytosis by a modified retroviral vector. In an embodiment, a modified retroviral vector will evade phagocytosis by macrophages. [0581] Cells engage in phagocytosis, engulfing particles, enabling the sequestration and destruction of foreign invaders, like bacteria or dead cells. In some embodiments, phagocytosis of lentiviral vectors by macrophages would reduce their activity. In some embodiments, phagocytosis of lentiviral vectors is a measure of immunogenicity of retroviral vectors. [0582] Retroviral vectors are produced from cells which lack CD24 (hereinafter NMC, positive control), cells that are transfected with CD24 cDNA (hereinafter NMC-CD47), and cells transfected with an empty vector control (hereinafter NMC-empty vector, negative control). Prior to retroviral vector production, the cells are labeled with CSFE. [0583] Reduction of macrophage mediated immune clearance is determined with a phagocytosis assay according to the following protocol. Macrophages are plated immediately after harvest in confocal glass bottom dishes. Macrophages are incubated in DMEM+10%FBS+1%P/S for 1h to attach. An appropriate number of retroviral vectors produced from NMC, NMC-CD24, NMC-empty vector are added to the macrophages as indicated in the protocol, and are incubated for 2h, substantially as described in tools.thermofisher.com/content/sfs/manuals/mp06694.pdf. [0584] After 2h, the dish is gently washed, and intracellular fluorescence is examined. Intracellular fluorescence emitted by engulfed retroviral particles is imaged by confocal microscopy at 488 excitation. The total fluorescence and/or number of phagocytotic positive macrophage is quantified using imaging software. The data may be expressed as the phagocytic index = (number of macrophages containing engulfed cells/total number of counted macrophages) × 100. [0585] In an embodiment, the phagocytic index will be reduced when macrophages are incubated with retroviral vectors derived from NMC-CD24, versus those derived from NMC, or NMC-empty vector. Example 2: Modification of retroviral vector with CD24 and CD47 to evade macrophage phagocytosis [0586] This Example describes quantification of the evasion of phagocytosis by a modified retroviral vector. In an embodiment, a modified retroviral vector will evade phagocytosis by macrophages. [0587] Cells engage in phagocytosis, engulfing particles, enabling the sequestration and destruction of foreign invaders, like bacteria or dead cells. In some embodiments, phagocytosis of lentiviral vectors by macrophages would reduce their activity. In some embodiments, phagocytosis of lentiviral vectors is a measure of immunogenicity of retroviral vectors. [0588] Retroviral vectors are produced from cells which lack CD24 and CD47 (hereinafter NMC, positive control), cells that are transfected with CD24 and CD47 cDNA (hereinafter NMC-CD24-CD47), and cells transfected with an empty vector control (hereinafter NMC-empty vector, negative control). Prior to retroviral vector production, the cells are labeled with CSFE. [0589] Reduction of macrophage mediated immune clearance is determined with a phagocytosis assay according to the following protocol. Macrophages are plated immediately after harvest in confocal glass bottom dishes. Macrophages are incubated in DMEM+10%FBS+1%P/S for 1h to attach. An appropriate number of retroviral vectors produced from NMC, NMC-CD24-CD47, NMC-empty vector are added to the macrophages as indicated in the protocol, and are incubated for 2h, substantially as described in tools.thermofisher.com/content/sfs/manuals/mp06694.pdf. [0590] After 2h, the dish is gently washed, and intracellular fluorescence is examined. Intracellular fluorescence emitted by engulfed retroviral particles is imaged by confocal microscopy at 488 excitation. The total fluorescence and/or number of phagocytotic positive macrophage is quantified using imaging software. The data may be expressed as the phagocytic index = (number of macrophages containing engulfed cells/total number of counted macrophages) × 100. [0591] In an embodiment, the phagocytic index will be reduced when macrophages are incubated with retroviral vectors derived from NMC-CD24-CD48, versus those derived from NMC, or NMC-empty vector. Example 3: Production of LV particles with human CD24 and/or human CD47 [0592] Laboratory-grade VSV-G-pseudotyped third-generation SIN lentiviral vectors (LVs) are produced by calcium phosphate transient transfection into 293T cells or by LV stable producer cell lines. 293T cells are transfected with a solution containing third generation lentiviral packaging plasmids expressing (i) gag and pol, (ii) rev, and (iii) VSV-G envelope protein, along with the expression plasmids pCMV-hCD47 and/or pCMV-hCD24, and transgene transfer plasmid pLenti-GFP. The amount of human CD47 and human CD24 plasmids are varied to generate LV particles with variable CD47 and/or CD24. Medium is changed 14 to 16 hours after transfection, and supernatant is collected 30 hours after medium change. LV- containing supernatants are sterilized through a 0.22-mm filter and, as necessary is transferred into sterile polyal-lomer tubes and centrifuged at 20,000g for 120 minutes at 20°C (Beckman Optima XL-100 K Ultracentrifuge). LV pellets are dissolved in the appropriate volume of Phosphate Buffered Saline (PBS) to allow 500x to 1000x concentrations. [0593] For LV titration, 1e5293T cells are transduced with serial LV dilutions in the presence of polybrene (8 mg/ml). For LV-GFP, cells are analyzed by flow cytometry 3-7 days after transduction and infectious titer, expressed as transducing units (TU)/mL, is calculated using the formula TU/mL = ((% GFP+ cells/100) x 100,000 x (1/dilution factor)). [0594] LVs are analyzed for CD24 or CD47 expression by immunoblotting. To reduce and denature LV samples, each sample is boiled in sample buffer at 100°C for 5 minutes. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) is used to resolve proteins from LV particles. Resolved gels are transferred to Polyvinylidene difluoride (PVDF) membrane by immersion tank electrophoresis. Antibodies for human CD47, human CD24, and p24 are used to identify amounts of proteins present in LV preparations. Ratios of CD47 and CD24 to p24 provide a qualitative measure of average CD47 or CD24 per LV particle. This can then be related to the plasmid concentration used during LV preparation. [0595] Increased amounts of CD24 and CD47 plasmid during transfection increases LV incorporation of these proteins as detected by immunoblotting. Example 4: Analysis of CD24 and/or CD 47 LV uptake into human macrophages [0596] LVs with CD47 or CD24 are produced as described in Example 3. [0597] Leukocyte reduction system (LRS) chambers from anonymous donors are obtained from local blood banks. Peripheral monocytes are purified through successive density gradients using Ficoll (Sigma Aldrich) and Percoll (GE Healthcare). Monocytes are then differentiated into macrophages by 7-9 days of culture in IMDM + 10% AB human serum .Unless otherwise stated, macrophages used for all in vitro phagocytosis assays are stimulated with 50 ng/mL human TGFb1 and 50 ng/mL human IL-10on Days 3-4 of differentiation until the end of the culture period on Days 7-9. IL-4 stimulation is added at a concentration of 20 ng/mL on Days 3- 4 of differentiation until the end of the culture period on Days 7-9. [0598] In vitro phagocytosis assays are performed by incubating 100,000 donor-derived macrophages with serial dilutions of crude LV preparations (1:2 thru 1:10000 by volumetric ratio) overnight in a humidified, 5% CO 2 incubator at 37°C in ultra-low-attachment 96-well U- bottom plates in serum-free IMDM (Life Technologies). Plates are centrifuged and medium is changed after overnight incubation. Macrophages are incubated for another 3 days to permit lentiviral expression before being harvested for flow cytometry. [0599] Macrophages are harvested by centrifugation at 400 g for 5 minutes at 4°C and stained with A647-labeled anti-CD11b to identify human macrophages. Assays are analyzed by flow cytometry on an LRSFortessa Analyzer (BD Biosciences) using a high-throughput auto- sampler. Phagocytosis is measured as the number of CD11b+, GFP+ macrophages, quantified as a percentage of the total CD11b+ macrophages. [0600] GFP+ macrophages due to LV-mediated transduction/uptake are reduced in CD47 and CD24 expressing LVs and further reduced in LVs with both CD47 and CD24. Moreover, GFP+ macrophage numbers decrease with increasing CD47 and/or CD24 levels on LV particles. Example 5: Reduction of in vivo CD24 and/or CD47 LV uptake into mouse macrophages [0601] LVs with CD47 or CD24 are produced as described in Examples 1 and 3, with the substitution of the use of pCMV-mCD47 and pCMV-mCD24 for transfection. Analysis of CD47 and CD24 incorporation is carried out using immunoblotting with anti-mouse CD47 and anti-mouse CD24 antibodies as is described in Example 3. [0602] Vector administration is carried out in adult (7 to 10 weeks old) wild-type C57BL/6 mice by tail-vein injection. Mice are bled from the retro-orbital plexus using capillary tubes, and blood is collected into 038% sodium citrate buffer (pH 74) Mice are anesthetized with tribromoethanol and euthanized by CO2 inhalation at scheduled times following LV administration. All animal procedures are performed according to protocols approved by the Institutional Animal Care and Use Committee. [0603] LVs are delivered at time zero (T0) to five cohorts of mice (N=5 each). Blood is sampled at 5 minutes, 10 minutes, 30 minutes, 1 hour, 2 hour, 4 hours, 8 hours, 12 hours, 24 hours, 48 hours rotating through the five cohorts to prevent undue blood volume depletion of the mice. [0604] Blood samples are analyzed for viral RNA. RNA extraction is performed using the RNeasy Plus mini Kit (Qiagen) according to manufacturer’s instructions and reverse transcribed using the SuperScript Vilo kit. All q-PCR analyses are performed using TaqMan probes from Applied Biosystems (WPRE: primer fw 5’-GGCTGTTGGGCACTGACAAT-3’; primer rv 5’- ACGTCCCGCGCAGAATC-3’; probe FAM 5’-TTTCCTTGGCTGCTCGCCTGTGT-3’ NGB). Q-PCR is run for 40 cycles using the Viia 7 instrument and raw data (Ct) are analyzed as follows: to determine gene expression, the difference (DCt) between the threshold cycle (Ct) of WPRE and that of the reference gene TAF7 is calculated by applying an equal threshold. The lower the DCt, the higher the gene expression level. [0605] The time course of viral RNA in serum shows a decrease over time. The addition of CD47 and/or CD24 reduces the rate of decrease, indicating an increase in viral vector bioavailability. Increasing levels of CD47 and/or CD24 reduces the rate of decrease in a dose- dependent manner. [0606] The present invention is not intended to be limited in scope to the particular disclosed embodiments, which are provided, for example, to illustrate various aspects of the invention. Various modifications to the compositions and methods described will become apparent from the description and teachings herein. Such variations may be practiced without departing from the true scope and spirit of the disclosure and are intended to fall within the scope of the present disclosure. XI. SEQUENCES
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