Atty. Dkt. No.650053.01002 USE OF IMMUNOGENIC T CELL EPITOPES FOR LYME DISEASE VACCINATION AND DIAGNOSIS CROSS-REFERENCE TO RELATED APPLICATIONS [0001] This application claims priority to U.S. application no. 63/403,451 filed on September 2, 2022, and to U.S. application no.63/501,445 filed on May 11, 2023. The entire contents of each of the aforementioned applications is incorporated by reference herein. STATEMENT REGARDING FEDERALLY SPONSORED RESEARCH OR DEVELOPMENT [0002] This invention was made with government support under R21AI148982 awarded by the National Institute of Allergy and Infectious Disease. The government has certain rights in the invention. SEQUENCE LISTING [0003] A Sequence Listing accompanies this application and is submitted as an XML file of the sequence listing named “650053_01002_SL” which is 1,137,000 bytes in size and was created on August 28, 2023. The sequence listing is electronically submitted via Patent Center with the application and is incorporated herein by reference in its entirety. BACKGROUND [0004] Lyme disease is the most common vector-borne disease in the United States. Lyme disease is caused by the bacterium Borrelia burgdorferi, Borrelia garinii, Borrelia afzelii, Borrelia bavariensis, Borrelia mayonii and others. It is transmitted to humans through the bite of infected blacklegged ixodes ticks. Typical symptoms include fever, headache, fatigue, and a characteristic skin rash called erythema migrans. If left untreated, infection can spread to joints, the heart, and the nervous system. Lyme disease is diagnosed based on symptoms, physical findings (e.g., rash), and the possibility of exposure to infected ticks. SUMMARY [0005] Disclosed herein are compositions and methods for the treatment and/or preventative treatment of Lyme disease in a subject. Also disclosed are methods for detecting Lyme disease in a subject in need thereof, or detecting exposure to Borrelia spp. [0006] In certain embodiments, disclosed herein are polypeptides comprising or consisting of fragments of BB0680 (MCP4) or variants thereof. In some embodiments, the polypeptides comprise or consist of one or more of the polypeptides presented in Tables 1 and 2. In some QB\650053.01002\84442353.1 Page 1 of 153 Atty. Dkt. No.650053.01002 embodiments, the polypeptide comprises or consists of SEQ ID NO: 1, or a polypeptide at least about 90% identical to SEQ ID NO: 1. [0007] Also disclosed herein are compositions comprising the polypeptides of the present disclosure. In some embodiments, the composition comprises a polypeptide comprising or consisting of SEQ ID NO: 1, and optionally an adjuvant. In some embodiments, the composition comprises one or more additional polypeptides, such as OspA, OspC, or one or more polypeptides listed in Tables 1 and 2. [0008] In various embodiments, disclosed herein are polypeptides comprising or consisting of fragments of BB0838 (LptD) or variants thereof. In some embodiments, the polypeptides comprise or consist of one or more of the polypeptides presented in Tables 3 and 4. In some embodiments, the polypeptide comprises or consists of SEQ ID NO: 2, or a polypeptide at least about 90% identical to SEQ ID NO: 2. [0009] Also disclosed herein are compositions comprising the polypeptides of the present disclosure. In some embodiments, the composition comprises a polypeptide comprising or consisting of SEQ ID NO: 2, and optionally an adjuvant. In some embodiments, the composition comprises one or more additional polypeptides, such as OspA, OspC, or one or more polypeptides in listed in Tables 3 and 4. [0010] In certain embodiments, the compositions disclosed herein can include one or more polypeptides disclosed herein, such as a polypeptide comprising or consisting of SEQ ID NO:1, a polypeptide at least about 90% identical to SEQ ID NO: 1, a polypeptide comprising or consisting of SEQ ID NO: 2, a polypeptide at least about 90% identical to SEQ ID NO: 2, one or more polypeptides listed in Tables 1, 2, 3, 4, and 5, or a combination thereof. [0011] In various embodiments, the composition disclosed herein can include one or more of: a polypeptide at least 90% or 95% identical to SEQ ID NO: 1, a polypeptide at least 90% or 95% identical to SEQ ID NO: 2, a polypeptide at least 90% or 95% identical to SEQ ID NO: 3, or a polypeptide at least 90% or 95% identical to SEQ ID NO: 4. [0012] Also disclosed herein are methods of treating Lyme disease, or a method for the preventative treatment of Lyme disease, the method comprising: administering to a subject the polypeptide or composition as disclosed herein. In some embodiments, the subject is asymptomatic for Lyme disease, but may have come in contact with a blacklegged tick selected from Ixodes scapularis or Ixodes pacificus. In some embodiments, the subject is asymptomatic. In some embodiments the subject is symptomatic, and exhibits one or more of the following symptoms: erythema migrans, facial palsy, and arthritis; and/or the subject tests positive for Lyme disease in standard two-tier test (STT). QB\650053.01002\84442353.1 Page 2 of 153 Atty. Dkt. No.650053.01002 [0013] Also disclosed herein are methods for testing a subject for exposure to Lyme disease, the method comprising: contacting a subject sample to one or more polypeptides disclosed herein. In some embodiments, the one or more polypeptides comprise or consist of SEQ ID NO:1, a polypeptide at least about 90% identical to SEQ ID NO: 1, a polypeptide comprising or consisting of SEQ ID NO: 2, a polypeptide at least about 90% identical to SEQ ID NO: 2, or a combination thereof. In some embodiments, the one or more polypeptides is linked to a solid support. [0014] Also disclosed herein are kits comprising one or more polypeptides as disclosed herein, and optionally instructions for use of the kit. In some embodiments, the one or more polypeptides is linked to a solid support, and comprise or consist of SEQ ID NO:1, a polypeptide at least about 90% identical to SEQ ID NO: 1, a polypeptide comprising or consisting of SEQ ID NO: 2, a polypeptide at least about 90% identical to SEQ ID NO: 2, or a combination thereof. BRIEF DESCRIPTION OF THE FIGURES [0015] FIG.1. Overview of methodology used to identify immunogenic MHC II peptides in mice infected with Borrelia burgdorferi. [0016] FIG. 2A-2B. Predicted structure of BB0680 (MCP4), with MCP442-462 epitope (Peptide 1) highlighted within the methyl-accepting transducer domain. [0017] FIG.3. Percent identify of MCP4 protein in various Borrelia strains, including Bb sensu stricto, Bb sensu lato, and non-Lyme disease spirochete Borrelia hermsii, a relapsing fever spirochete. [0018] FIG.4A-4B. CD4+ T cell epitope MCP442-462 (Peptide 1) is immunogenic in mice infected with B. burgdorferi. Lymphocytes from mice infected with B. Burgdorferi for 4 weeks were stained with a proliferation dye (Cell-Trace Violet) and stimulated with Peptide 1 or OVA peptide as a negative control and incubated for 5 days. (A) Flow cytometric analysis of CD4+ T cells identified a population of activated, proliferating CD4+ T cells in lymphocytes stimulated with Peptide 1, but not with OVA peptide. (B) Analysis of CD4- lymphocytes, which include CD8+ T cells and B cells, also identified a population of activated lymphocytes. Representative of 2 biological replicates. [0019] FIG. 5. CLUSTAL O(1.2.4) multiple sequence alignment of BB0680 (MCP4). B.hermsii is a relapsing fever Borrelia. B. afzelii, B. garinii, B. garinii-barariensis, and B. mayonii are Bb sensu lato strains. JD1, N40, B31, and ZS7 are isolates representing Bb sensu stricto strains. Peptide 1 is highlighted in bold. FIG. 5 includes SEQ ID NOS 1309-1317, respectively, in order of appearance from top to bottom. QB\650053.01002\84442353.1 Page 3 of 153 Atty. Dkt. No.650053.01002 [0020] FIG. 6. Table showing MHC class II peptides derived from Borrelia burgdorferi identified by LC/MS/MS. FIG.6 discloses SEQ ID NOS 1324-1325, and 3-4, respectively, in order of appearance. [0021] FIG.7. Structure of LptD (BB0838) based on Phyre2 modeling. LptD _923-934 is at the interface between the central β-barrel and C-terminal β-barrel/plug domains. According to this model, LptD _923-934 (magenta) is localized to the cell surface, within the outer membrane (OM)- spanning β-barrel. The LptD N-terminal periplasmic domain consists of a β-jellyroll domain with an unresolved N-terminal sequence (cyan). The central domain of LptD consists of a β- barrel that is predicted to span the OM (green). The C-terminal domain, which includes LptD _923-934 , consists of a β-barrel and an unresolved C-terminal sequence, possibly a plug (yellow). [0022] FIG.8. Sequence alignment and phylogenic analysis of LptD across Lyme disease spirochetes. ClustalW as used to align LptD protein sequences from Borrelia burgdorferi, Borrelia califorensis, Borrelia mayonii, Borrelia garinii, Borrelia afzelii, Borrelia baveriensis. The alignment and amino acid conservation of the 50 amino acids downstream from the LptD923-934 epitope (underlined) is shown. Brackets indicate promiscuous core epitopes that are predicted to bind to a large number of HLA-DRB1 alleles (see FIGS.11 and 12 for complete list). LptD sequence from relapsing fever spirochete Borrelia hermsii was used as an outgroup in generation of a phylogenetic relationship tree (below the alignment), with numbers indicating the Baysian distance from the consensus sequence. FIG. 8 discloses SEQ ID NOS 1318-1323, respectively, in order of appearance from top to bottom. [0023] FIG.9. Is a schematic depiction of a proposed use of T cell vaccine components for use in a novel Lyme disease vaccine. DETAILED DESCRIPTION [0024] Lyme disease affects nearly 500,000 individuals in the U.S. annually and is caused by infection with the tick-borne spirochete Borrelia burgdorferi. Although most patients are effectively treated with antibiotic therapy, ~10% of patients with Lyme disease have persistent symptoms that continue for months to years following antibiotic therapy and apparent spirochetal killing, called post-treatment Lyme disease syndrome (PTLDS), sometimes referred to as “chronic Lyme disease.” Unfortunately, there are critical gaps in diagnostic and therapeutic tools available to clinicians to treat patients suffering from Lyme disease, particularly following antibiotic therapy. Therefore, novel diagnostic tools and effective vaccines are urgently needed. QB\650053.01002\84442353.1 Page 4 of 153 Atty. Dkt. No.650053.01002 [0025] T helper cells, also called CD4+ T cells, are the “generals” of the adaptive immune system. They regulate all aspects of immune responses to pathogens by directing other components of the immune system to find, neutralize, and kill pathogens during infection, and promote immune resolution and tissue repair post-infection. Dysregulated CD4+ T cell responses can also drive numerous chronic inflammatory, arthritic, neurodegenerative, and fibrotic diseases. B. burgdorferi has evolved mechanisms to evade CD4+ T cell responses during infection. This likely contributes to chronic infection, immune dysregulation, and ongoing tissue damage and fibrosis in Lyme disease patients, particularly the tens of thousands of individuals suffering from chronic Lyme disease/post-treatment Lyme disease syndrome (PTLDS), as well as coinfections. However, very little is known about this part of the adaptive immune system due, in large part, to a shortage of validated T cell immune targets. [0026] Using an immunopeptidomics approach the inventors screened over 10,000 peptides bound to MHC class II molecules expressed on antigen presenting cells from infected mice (Figure 1). One peptide was derived from BB0680 (MCP4 _442-462 ), hereafter Peptide 1 (SEQ ID NO: 1) (see FIG.2A). BB0680 is a methyl-accepting chemotaxis protein that is highly conserved amongst both sensu lato and sensu stricto strains of Lyme disease spirochetes (see FIG.3 and FIG.5). Peptide 1 is highly immunogenic in mice infected with B. burgdorferi (see FIGS. 4A and 4B), validating Peptide 1 as target of CD4+ T cell responses to B. burgdorferi infection. Peptide 1 is one of a number of peptides derived from MCP4 predicted to bind to MHC class II alleles in mice and/or humans (Table 1 below (mouse), Table 2 below (human)). It is anticipated that immunization with Peptide 1 will lead to protective immunity in mice and humans. It is also anticipated that other epitopes derived from MCP4 are immunogenic in mice and humans infected with B. burgdorferi. In some embodiments, and pursuant to the methods disclosed herein, T and B cell reactivity to MCP4 in humans with early and late Lyme disease, and in patients with PTLDS will be measured. [0027] Peptide 1, has the amino acid sequence of SEQ ID NO: 1 and is provided below: [0028] KASLEVASSSQNLSSSALQQA [0029] Another peptide identified in the screen was derived from BB0838 (LptD923-934), hereinafter Peptide 2 (SEQ ID NO: 2). LptD is an outer membrane protein (FIG. 7) involved in translocation of lipoproteins such as OspA and OspC from the periplasm to the outer membrane and is essential for cell growth. The LptD _923-934 epitope is located at the interface between the central β-barrel domain and the C-terminal β-barrel/plug domain (FIG.7). Based on structure modeling, this epitope is localized at or near the cell surface, within the outer membrane-spanning β-barrel (FIG.7). LptD is highly conserved amongst both sensu lato and QB\650053.01002\84442353.1 Page 5 of 153 Atty. Dkt. No.650053.01002 sensu stricto strains of Lyme disease spirochetes, and the region surrounding the LptD923-934 epitope includes numerous promiscuous epitopes, or peptides predicted to bind to a large number of human HLADRB1 alleles (FIG.8). Peptide 2 is one of a number of peptides derived from LptD predicted to bind to MHC class II alleles in humans (Table 3 and Table 4 below). It is anticipated that immunization with Peptide 2 will lead to protective immunity in humans and mice. It also anticipated that other epitopes derived from LptD are immunogenic in humans and mice infected with B. burgdorferi. In some embodiments, and pursuant to the methods disclosed herein, T and B cell reactivity to LptD in humans with early and late Lyme disease, and in patients with PTLDS will be measured. [0030] Peptide 2, has the amino acid sequence of SEQ ID NO: 2 and is provided below: [0031] NVFDFQFLFAMK [0032] A peptide from BB0559 (Crr) was also identified in the screen (Crr _123-138 ), hereinafter Peptide 3 (SEQ ID NO: 3). Crr is a PTS system glucose-specific component. [0033] Peptide 3, has the amino acid sequence of SEQ ID NO: 3 and is provided below: [0034] HSESVITPVVIANSDE [0035] A peptide from oppAIV was also identified in the screen (oppAIV138-152), herein after Peptide 4 (SEQ ID NO: 4). oppAIV is an oligopeptide ABC transporter. [0036] Peptide 4, has the amino acid sequence of SEQ ID NO: 4 and is provided below: [0037] NAEEYFDGKANESE [0038] Additional immunogenic T cell epitopes are identified and described with respect to Table 5 below in the Examples. To date, no other immunogenic T cell epitopes from mice infected with Borrelia burgdorferi have been identified. The only other known Borrelia burgdorferi T cell epitopes target OspA in vaccinated mice. This is of limited value since OspA is typically not expressed by Borrelia burgdorferi during Lyme borreliosis. Furthermore, current vaccine candidates OspA and OspC and diagnostic marker VLSE are poorly conserved between Lyme disease spirochetes, are not expressed during infection (OspA), are rapidly down-regulated following transmission (OspC), or alter their B cell antigenic targets (VLSE). Additionally, all are poor T cell immunogens, which greatly reduces vaccine efficacy. [0039] Definitions and Terminology [0040] The disclosed compositions and methods for treating, detecting, and diagnosing infection by a Borrelia sp., such as Borrelia burgdorfori, may be further described using definitions and terminology as follows. The definitions and terminology used herein are for the purpose of describing particular embodiments only, and are not intended to be limiting. QB\650053.01002\84442353.1 Page 6 of 153 Atty. Dkt. No.650053.01002 [0041] As used in this specification and the claims, the singular forms “a,” “an,” and “the” include plural forms unless the context clearly dictates otherwise. [0042] As used herein, “about”, “approximately,” “substantially,” and “significantly” will be understood by persons of ordinary skill in the art and will vary to some extent on the context in which they are used. If there are uses of the term which are not clear to persons of ordinary skill in the art given the context in which it is used, “about” and “approximately” will mean up to plus or minus 10% of the particular term and “substantially” and “significantly” will mean more than plus or minus 10% of the particular term. [0043] As used herein, the terms “include” and “including” have the same meaning as the terms “comprise” and “comprising.” The terms “comprise” and “comprising” should be interpreted as being “open” transitional terms that permit the inclusion of additional components further to those components recited in the claims. The terms “consist” and “consisting of” should be interpreted as being “closed” transitional terms that do not permit the inclusion of additional components other than the components recited in the claims. The term “consisting essentially of” should be interpreted to be partially closed and allowing the inclusion only of additional components that do not fundamentally alter the nature of the claimed subject matter. [0044] The phrase “such as” should be interpreted as “for example, including.” Moreover the use of any and all exemplary language, including but not limited to “such as”, is intended merely to better illuminate the invention and does not pose a limitation on the scope of the invention unless otherwise claimed. [0045] Furthermore, in those instances where a convention analogous to “at least one of A, B and C, etc.” is used, in general such a construction is intended in the sense of one having ordinary skill in the art would understand the convention (e.g., “a system having at least one of A, B and C” would include but not be limited to systems that have A alone, B alone, C alone, A and B together, A and C together, B and C together, and/or A, B, and C together.). It will be further understood by those within the art that virtually any disjunctive word and/or phrase presenting two or more alternative terms, whether in the description or figures, should be understood to contemplate the possibilities of including one of the terms, either of the terms, or both terms. For example, the phrase “A or B” will be understood to include the possibilities of “A” or ‘B or “A and B.” [0046] All language such as “up to,” “at least,” “greater than,” “less than,” and the like, include the number recited and refer to ranges which can subsequently be broken down into ranges and subranges. A range includes each individual member. Thus, for example, a group QB\650053.01002\84442353.1 Page 7 of 153 Atty. Dkt. No.650053.01002 having 1-3 members refers to groups having 1, 2, or 3 members. Similarly, a group having 6 members refers to groups having 1, 2, 3, 4, or 6 members, and so forth. [0047] The modal verb “may” refers to the preferred use or selection of one or more options or choices among the several described embodiments or features contained within the same. Where no options or choices are disclosed regarding a particular embodiment or feature contained in the same, the modal verb “may” refers to an affirmative act regarding how to make or use and aspect of a described embodiment or feature contained in the same, or a definitive decision to use a specific skill regarding a described embodiment or feature contained in the same. In this latter context, the modal verb “may” has the same meaning and connotation as the auxiliary verb “can.” [0048] The terms “identical” or percent “identity,” in the context of two or more nucleic acids or polypeptide sequences, refer to two or more sequences or subsequences that are the same or have a specified percentage of amino acid residues or nucleotides that are the same (i.e., 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or more identity over a specified region, e.g., of an entire nucleic acid or polypeptide sequence or individual portions or domains of a nucleic acid or polypeptide), when compared and aligned for maximum correspondence over a comparison window, or designated region as measured using one of the following sequence comparison algorithms or by manual alignment and visual inspection. Such sequences are then said to be “substantially identical.” This definition also refers to the complement of a test sequence, in the context of nucleic acids. By way of example, in embodiments, the identify exists over a region that is about or at least about 5, 10, 15, 20, 50, 100, or 1000, amino acids in length, to about, less than about, or at least about 220, 100 or 1000 amino acids or nucleotides in length. Optionally, the identity exists over a region that is at least about 5, 10, 15, 20, 21 amino acids in length (e.g., with reference to SEQ ID NO: 1) to about 100, about 20 to about 75, about 30 to about 50 amino acids or nucleotides in length. Non-limiting examples of polypeptide sequences provided herein comprise sequences that are substantially identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, or SEQ ID NO: 4. By way of example, polypeptides that are at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% identical to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, or SEQ ID NO: 4 is provided herein. Polypeptides comprising a difference of 1, 2, 3, 4, 5, 6 or 7, 8, 9 or 0 amino acids as compared to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, or SEQ ID NO: 4 are also contemplated herein. [0049] For sequence comparison, typically one sequence acts as a reference sequence, to which test sequences are compared. When using a sequence comparison algorithm, test and QB\650053.01002\84442353.1 Page 8 of 153 Atty. Dkt. No.650053.01002 reference sequences are entered into a computer, subsequence coordinates are designated, if necessary, and sequence algorithm program parameters are designated. Preferably, default program parameters can be used, or alternative parameters can be designated. The sequence comparison algorithm then calculates the percent sequence identities for the test sequences relative to the reference sequence, based on the program parameters. [0050] An example of algorithms suitable for determining percent sequence identity and sequence similarity are the BLAST and BLAST 2.0 algorithms, which are described in Altschul et al., Nuc. Acids Res.25:3389-3402 (1977) and Altschul et al., J. Mol. Biol. 215:403-410 (1990), respectively. As will be appreciated by one of skill in the art, the software for performing BLAST analyses is publicly available through the website of the National Center for Biotechnology Information (NCBI). In embodiments, BLAST and BLAST 2.0 are used, with the parameters described herein, to determine percent sequence identity for the nucleic acids and proteins. In embodiments, a BLAST algorithm involves first identifying high scoring sequence pairs (HSPs) by identifying short words of length W in the query sequence, which either match or satisfy some positive-valued threshold score T when aligned with a word of the same length in a database sequence. In embodiments, T is referred to as the neighborhood word score threshold (Altschul et al., supra). In embodiments, these initial neighborhood word hits act as seeds for initiating searches to find longer HSPs containing them. In embodiments, the word hits are extended in both directions along each sequence for as far as the cumulative alignment score can be increased. In embodiments, cumulative scores are calculated using, for nucleotide sequences, the parameters M (reward score for a pair of matching residues; always >0) and N (penalty score for mismatching residues; always <0). In embodiments, for amino acid sequences, a scoring matrix is used to calculate the cumulative score. In embodiments, extension of the word hits in each direction are halted when: the cumulative alignment score falls off by the quantity X from its maximum achieved value; the cumulative score goes to zero or below, due to the accumulation of one or more negative-scoring residue alignments; or the end of either sequence is reached. In embodiments, the BLAST algorithm parameters W, T, and X determine the sensitivity and speed of the alignment. In embodiments, the NCBI BLASTN or BLASTP program is used to align sequences. In embodiments, the BLASTN or BLASTP program uses the defaults used by the NCBI. In embodiments, the BLASTN program (for nucleotide sequences) uses as defaults: a word size (W) of 28; an expectation threshold (E) of 10; max matches in a query range set to 0; match/mismatch scores of 1, −2; linear gap costs; the filter for low complexity regions used; and mask for lookup table only used. In embodiments, the BLASTP program (for amino acid sequences) uses as defaults: a word size QB\650053.01002\84442353.1 Page 9 of 153 Atty. Dkt. No.650053.01002 (W) of 3; an expectation threshold (E) of 10; max matches in a query range set to 0; the BLOSUM62 matrix (see Henikoff & Henikoff, Proc. Natl. Acad. Sci. USA 89:10915 (1992)); gap costs of existence: 11 and extension: 1; and conditional compositional score matrix adjustment. [0051] The terms “polypeptide,” “peptide” and “protein” are used interchangeably herein to refer to a polymer of amino acid residues. The terms apply to amino acid polymers in which one or more amino acid residue is an artificial chemical mimetic of a corresponding naturally occurring amino acid, as well as to naturally occurring amino acid polymers and non-naturally occurring amino acid polymer. [0052] The term “amino acid” refers to naturally occurring and synthetic amino acids, as well as amino acid analogs and amino acid mimetics that function in a manner similar to the naturally occurring amino acids. Naturally occurring amino acids are those encoded by the genetic code, as well as those amino acids that are later modified, e.g., hydroxyproline, γ- carboxyglutamate, and O-phosphoserine. Amino acid analogs refers to compounds that have the same basic chemical structure as a naturally occurring amino acid, i.e., an a carbon that is bound to a hydrogen, a carboxyl group, an amino group, and an R group, e.g., homoserine, norleucine, methionine sulfoxide, methionine methyl sulfonium. Such analogs have modified R groups (e.g., norleucine) or modified peptide backbones, but retain the same basic chemical structure as a naturally occurring amino acid. Amino acid mimetics refers to chemical compounds that have a structure that is different from the general chemical structure of an amino acid, but that functions in a manner similar to a naturally occurring amino acid. [0053] Amino acids may be referred to herein by either their commonly known three letter symbols or by the one-letter symbols recommended by the IUPAC-IUB Biochemical Nomenclature Commission. Nucleotides, likewise, may be referred to by their commonly accepted single-letter codes. [0054] “Conservatively modified variants” applies to both amino acid and nucleic acid sequences. With respect to particular nucleic acid sequences, conservatively modified variants refers to those nucleic acids which encode identical or essentially identical amino acid sequences, or where the nucleic acid does not encode an amino acid sequence, to essentially identical sequences. Because of the degeneracy of the genetic code, a large number of functionally identical nucleic acids encode any given protein. For instance, the codons GCA, GCC, GCG and GCU all encode the amino acid alanine. Thus, at every position where an alanine is specified by a codon, the codon can be altered to any of the corresponding codons described without altering the encoded polypeptide. Such nucleic acid variations are “silent QB\650053.01002\84442353.1 Page 10 of 153 Atty. Dkt. No.650053.01002 variations,” which are one species of conservatively modified variations. Every nucleic acid sequence herein which encodes a polypeptide also describes every possible silent variation of the nucleic acid. One of skill will recognize that each codon in a nucleic acid (except AUG, which is ordinarily the only codon for methionine, and TGG, which is ordinarily the only codon for tryptophan) can be modified to yield a functionally identical molecule. Accordingly, each silent variation of a nucleic acid which encodes a polypeptide is implicit in each described sequence with respect to the expression product, but not with respect to actual probe sequences. [0055] As to amino acid sequences, one of skill will recognize that individual substitutions to a peptide, polypeptide, or protein sequence which alters a single amino acid is a “conservatively modified variant” where the alteration results in the substitution of an amino acid with a chemically similar amino acid. Conservative substitution tables providing functionally similar amino acids are well known in the art. Such conservatively modified variants are in addition to and do not exclude polymorphic variants, interspecies homologs, and alleles. [0056] The following eight groups each contain amino acids that are conservative substitutions for one another: 1) Alanine (A), Glycine (G); 2) Aspartic acid (D), Glutamic acid (E); 3) Asparagine (N), Glutamine (Q); 4) Arginine (R), Lysine (K); 5) Isoleucine (I), Leucine (L), Methionine (M), Valine (V); 6) Phenylalanine (F), Tyrosine (Y), Tryptophan (W); 7) Serine (S), Threonine (T); and 8) Cysteine (C), Methionine (M) (see, e.g., Creighton, Proteins (1984)). [0057] "Lyme disease" as used herein refers to an infection by a Borrelia bacterium, which is also known as Borreliosis. At least nine species of Borrelia are known to cause Lyme disease, including Borrelia afzelii, Borrelia bissettiae, Borrelia burgdorferi, Borrelia garinii, B. hermsii, Borrelia lusitaniae, Borrelia mayonii, Borrelia spielmanii, and Borrelia valaisiana. Additional Borrelia strains include, without limitation, B.burgdorferi-JD1, B.burgdorferi-N40, B.burgdorferi-B31, B.burgdorferi-ZS7, and B.garinii-bavariensis. Lyme disease is commonly caused by the transfer of Borrelia bacteria to mammalian hosts by certain hard ticks of the Ixodidae family. In the U.S., Lyme disease is most commonly the result of the transfer of Borrelia burgdorferi bacteria by the blacklegged tick, also known as a deer tick (Ixodes scapularis or Ixodes pacificus). Outside the U.S., Ixodes ricinus and Ixodes persulcatus act as Borreliosis vectors. Without early detection and treatment, the bacteria travel through the bloodstream and affect various tissues in the host. The infection may develop into an inflammatory condition that affects multiple systems, starting with skin, joints, and nervous system and moving to organs. QB\650053.01002\84442353.1 Page 11 of 153 Atty. Dkt. No.650053.01002 Symptoms can include one or more of fever, chills, headache, fatigue, muscle pain, joint pain, swollen lymph nodes, a bullseye rash, termed erythema migrans, facial palsy, and arthritis. [0058] The term “subject” may be used interchangeably with the terms “individual” and “patient” and includes human and non-human subjects. In some embodiments, subjects may be any animal that can be infected with a bacterium, such as Borrelia burgdorferi. In some embodiments, the subject is a mammal, such as a human, dog, cat, or livestock, such as cattle, pigs, or sheep. In some embodiments, a subject may include a wild, domesticated, or captive population of animals such as deer, elk, bison, etc. In some embodiments, a subject may include one or more wild or domesticated bird species, such as chickens, ducks, or turkeys. [0059] In some embodiments, the methods include detecting the presence of Borrelia burgdorferi in a subject. In some embodiments, the methods include detecting the presence of Borrelia afzelii, Borrelia burgdorferi, Borrelia garinii, or Borrelia mayonii in a subject. [0060] As used herein, the terms “treat” or “treatment” encompass both “preventative” and “curative” treatment. “Preventative” treatment is meant to indicate a postponement of development of a disease, a symptom of a disease, or medical condition, suppressing symptoms that may appear, or reducing the risk of developing or recurrence of a disease or symptom. “Curative” treatment includes reducing the severity of or suppressing the worsening of an existing disease, symptom, or condition. Thus, treatment includes ameliorating or preventing the worsening of existing disease symptoms, preventing additional symptoms from occurring, ameliorating or preventing the underlying systemic causes of symptoms, inhibiting the disorder or disease, e.g., arresting the development of the disorder or disease, relieving the disorder or disease, causing regression of the disorder or disease, relieving a condition caused by the disease or disorder, or stopping the symptoms of the disease or disorder. [0061] A non-limiting example of a treatment for a subject diagnosed with Lyme disease includes, but is not limited to, administration of a composition comprising a polypeptide of SEQ ID NO: 1, a polypeptide at least 90% identical to SEQ ID NO: 1, a polypeptide of SEQ ID NO: 2, or a polypeptide at least 90% identical to SEQ ID NO: 2, or a combination thereof. In some embodiments, the composition comprises an adjuvant. In some embodiments, the composition comprises a vaccine. [0062] A non-limiting example of a treatment for infection by Borrelia sp. including, but not limited to B. burgdorferi includes, but is not limited to, administration of a composition comprising a polypeptide of SEQ ID NO: 1, a polypeptide at least 90% identical to SEQ ID NO: 1, a polypeptide of SEQ ID NO: 2, or a polypeptide at least 90% identical to SEQ ID NO: QB\650053.01002\84442353.1 Page 12 of 153 Atty. Dkt. No.650053.01002 2, or a combination thereof. In some embodiments, the composition comprises an adjuvant. In some embodiments, the composition comprises a vaccine. [0063] A non-limiting example of a preventative treatment for a subject at risk of exposure to a tick causing Lyme disease includes, but is not limited to, administration of a composition comprising a polypeptide of SEQ ID NO: 1, a polypeptide at least 90% identical to SEQ ID NO: 1, a polypeptide of SEQ ID NO: 2, or a polypeptide at least 90% identical to SEQ ID NO: 2, or a combination thereof. In some embodiments, the composition comprises an adjuvant. In some embodiments, the composition comprises a vaccine. [0064] A non-limiting example of a preventative treatment for a subject at risk for infection by Borrelia sp. including, but not limited to B. burgdorferi includes, but is not limited to, administration of a composition comprising a polypeptide of SEQ ID NO: 1, a polypeptide at least 90% identical to SEQ ID NO: 1, a polypeptide of SEQ ID NO: 2, or a polypeptide at least 90% identical to SEQ ID NO: 2, or a combination thereof. In some embodiments, the composition comprises an adjuvant. In some embodiments, the composition comprises a vaccine. [0065] In some embodiments, a non-limiting treatment or preventative treatment includes vaccination of a subject in need thereof (e.g., a subject diagnosed with Lyme disease, or a subject at risk of exposure to Lyme disease), with a composition comprising one or more of the epitopes presented in the tables provided in Figures 5 and 6. [0066] As used herein, the term "adjuvant" refers to ingredients used in some vaccines to create a stronger immune response in subjects receiving the vaccine. By way of example, but not by way of limitation, adjuvants include aluminum, monophosphoryl lipid A (MPL), MPL + aluminum salt, oil in water emulsion, e.g., composed of squalene, MPL and QS-21, cytosine phosphaguanine (CpG). [0067] As used herein, the term "antibody," or "antibody molecule" (used synonymously herein) refer to naturally occurring immunoglobulin molecules with varying structures. Typically, antibodies are gamma globulin proteins that can be found in blood or other bodily fluids of vertebrates and are used by the immune system to identify foreign materials, such as bacteria, viruses, and toxins. Antibodies bind, by non-covalent interactions, with high affinity to other molecules or structures known as antigens. This binding is specific in the sense that an antibody molecule will only bind to a specific structure with high affinity. The unique part of the antigen recognized by an antibody molecule is called an epitope, or antigenic determinant. The part of the antibody molecule binding to the epitope is sometimes called paratope and resides in the so-called variable domain, or variable region (Fv) of the antibody. The variable QB\650053.01002\84442353.1 Page 13 of 153 Atty. Dkt. No.650053.01002 domain comprises three complementary-determining regions (CDR's) spaced apart by framework regions (FR's). There are at least five major classes of antibodies: IgA, IgD, IgE, IgG, and IgM, and several of these may be further divided into subclasses (isotypes), e.g. , IgGl, IgG2, IgG3, IgG4, IgAl, and IgA2. They are typically made of basic structural units-- each with two large heavy chains and two small light chains--to form, for example, monomers with one unit, dimers with two units or pentamers with five units. Non-limiting examples of antibodies include any known class and/or isotype, such as, e.g., IgA (e.g. IgA1, IgA2, and sIgA), IgD, IgE, IgG (e.g. IgG1, IgG2, IgG3, or IgG4), and IgM. The “class” of an antibody may refer to the type of constant domain or constant region possessed by its heavy chain. For example, heavy chain constant domains may be used to classify different classes of immunoglobulins, such as, e.g., α, γ, δ, ε, and μ. In some embodiments, the antibody is a native human IgG. IgG antibodies are typically heterotetrameric glycoproteins of about 150,000 daltons, composed of two identical light chains and two identical heavy chains that are disulfide bonded. The light chain of an antibody may be assigned to certain types, e.g. kappa and lambda, based on the amino acid sequence of its constant domain. [0068] The terms "epitope" and "antigenic determinant", which can be used interchangeably, refer to the part of a macromolecule, such as a polypeptide, carbohydrate, or a lipid, that is recognized by antigen-binding molecules, such antibodies. Epitopes define the minimum binding site for an antibody molecule, and thus represent the target of specificity of an antibody molecule. In some embodiments, an epitope comprises, or consists of SEQ ID NO: 1, or a polypeptide at least 90% identical to SEQ ID NO: 1, or an epitope provided in Tables 1 and 2. In the same or alternative embodiments, an epitope comprises, or consists of SEQ ID NO: 2, or a polypeptide at least 90% identical to SEQ ID NO: 2, or an epitope provided in Tables 3 and 4. In various embodiments, an epitope comprises or consists of a polypeptide provided in Table 5, or a polypeptide at least 90% identical to one or more of the polypeptides provided in Table 5. [0069] An antibody molecule that can "bind", "bind to", "specifically bind", or "specifically bind to", that "has affinity for" and/or that "has specificity for" a certain epitope, antigen or protein (or for at least one part, fragment or epitope thereof) is said to be "against" or "directed against" said epitope, antigen or protein or is a "binding" molecule with respect to such epitope, antigen or protein. [0070] Generally, the term "specificity" refers to the number of different types of antigens or epitopes to which a particular antigen-binding molecule or antigen-binding protein (such as an immunoglobulin, an antibody, an immunoglobulin single variable domain) can bind. The QB\650053.01002\84442353.1 Page 14 of 153 Atty. Dkt. No.650053.01002 specificity of an antigen-binding protein can be determined based on its affinity and/or avidity. The affinity, represented by the equilibrium constant for the dissociation of an antigen with an antigen-binding protein (KD), is a measure for the binding strength between an epitope and an antigen-binding site on the antigen-binding protein: the lesser the value of the K _D , the stronger the binding strength between an epitope and the antigen-binding molecule (alternatively, the affinity can also be expressed as the affinity constant (K _A ), which is 1/K _D ). As will be clear to the skilled person (for example on the basis of the further disclosure herein), affinity can be determined in a manner known per se, depending on the specific antigen of interest. Avidity is the measure of the strength of binding between an antigen-binding molecule (such as an antibody of the invention) and the pertinent antigen. Avidity is related to both the affinity between an epitope and its antigen binding site on the antigen-binding molecule and the number of pertinent binding sites present on the antigen-binding molecule. [0071] As used herein, the term "panel" refers to a collection of two or more biomolecules (e.g. antigens) wherein the two or more biomolecules are organized such that the two or more biomolecules can be differentiated from each other in a detecting step. This organization can be a spatial arrangement (e.g. biomolecule 1 is in section 1 of the panel, biomolecule 2 is in section 2 of the panel, etc.) or a difference in a detection aspect, such as each biomolecule can be differentiated by a different detectable agent (e.g. biomolecule 1 can be detected with color 1, biomolecule 2 can be detected with color 2, etc.). [0072] As used herein, the term "solid support" refers to any substrate or support matrix to which a molecule (such as a polypeptide, antibody, or antibody- polypeptide complex) can be bound, either reversibly or irreversibly. Non-limiting examples of solid supports include, without limitation, a bead, plate, slide, flow chamber, chip, cartridge, flow cell, etc. The solid support may formed from glass, ceramic, polymers (e.g., plastic, latex, polystyrene, polyacrylamide, polyvinylchloride, polypropylene, polyethylene, polylactic acid), cellulose (e.g., paper). In some embodiments, a polypeptide is immobilized on a solid support. In some embodiments, the polypeptide is SEQ ID NO: 1. In certain embodiments, the polypeptide is SEQ ID NO: 2. In some embodiments, the immobilized polypeptide is bound to the solid support, either reversibly or irreversibly, to form a platform for an antibody binding reaction. In some embodiments, there are two or more polypeptide which are immobilized on the solid support in configuration so as to form a polypeptide panel. [0073] As used herein, the term "bead" refers to a microbead or relatively small bead having a diameter less than about 500 µm, typically with a diameter of less than about 100 µm, 50 µm, or 10 µm. While a bead may vary in shape, typically a bead is substantially spherical, QB\650053.01002\84442353.1 Page 15 of 153 Atty. Dkt. No.650053.01002 e.g. a microsphere. Microbeads are known in the art and can comprise various materials such as, e.g., latex, polystyrene, polyacrylamide, polyvinylchloride, polypropylene, polyethylene, polylactic acid, ceramic, glass, and magnetic compositions. [0074] As used herein, the term "plate" encompasses a solid support comprising a variety of types, including plastic or glass plates. In some embodiments, the plate is a 96-well, 384- well, or 1536-well plastic plate. [0075] As used herein, a "detectable binding agent" refers to a molecule that binds, either directly or indirectly, to a target molecule, and can be detected either directly, or with further chemical or enzymatic reaction. By way of example, but not by way of limitations, a detectable binding agent may comprise an antibody linked to an enzyme, such as horseradish peroxidase (HRP). Addition of an HRP substrate, under enzymatic reaction conditions, will allow detection of the HRP-bound molecule and the target. Other examples of detectable binding agents and include antibodies or MHC class II tetramer reagents (tetramers) linked to detectable labels, such as fluorescent labels. Such constructs are well known in the art and are not intended to limit the scope of the present methods and compositions. [0076] As used herein, a "detectable agent" or "detectable label" refers to an agent or label that can be detected either directly, or with further chemical or enzymatic reaction. By way of example, but not by way of limitations, a detectable agent or label may comprise a fluorescent moiety or an enzyme, such as HRP. Other examples of detectable agents and labels include radioisotope. Such agents and labels are well known in the art and are not intended to limit the scope of the present methods and compositions. [0077] As used herein, the term "buffer" refers to a pH buffering agent that helps maintain the pH of an aqueous solution. Non-limiting examples of pH buffering agents include phosphate buffers (e.g. PBS), Tris, citric acid, histidine, glycine, HEPES, MOPS, and PIPES. [0078] As used herein, the term "stabilizer" refers to an agent that stabilizes a component of a composition, such as a protein, antibody, and/or polypeptide, thereby helping to preserve its stability and integrity. Non-limiting examples of stabilizers include glycerol, polysorbates, polyethylene glycols (PEGs), glycine, histidine, arginine, sugars (e.g. trehalose), and polyols (e.g., mannitol, sorbitol and glycerol). [0079] As used herein, the term "non-specific binding surface blocking agent" refers to an agent that reduces the non-specific binding between antibodies and other molecules. Non- limiting examples of non-specific binding surface blocking agents include milk proteins (e.g. casein) and bovine serum albumin (BSA). QB\650053.01002\84442353.1 Page 16 of 153 Atty. Dkt. No.650053.01002 [0080] As used herein, the term “macromolecular crowding agent” refers to an inert agent that excludes volume in solution from other macromolecules, such as proteins and antibodies. Non-limiting examples of macromolecular crowding agents include polyethylene glycols (PEGs), dextran, and high molecular weight, highly branched polysaccharides. [0081] As used herein, the term "antioxidant" refers to an agent that inhibits oxidation reactions. Non-limiting examples of antioxidants include citrate, EDTA (ethylenediaminetetraacetic acid), methionine, ascorbic acid, and thiols. [0082] As used herein, the term "preservative" refers to an agent that prevents or inhibits microbiological growth. Non-limiting examples of preservatives include CMIT (5-chloro-2- methylisothiazol-3(2H)-one), MIT (2-methylisothiazol-3(2H)-one), and sodium azide. [0083] As used herein, the term "surfactant" refers to an agent that modulates the solubility of another molecule or agent in a solution. Non-limiting examples of surfactants include polysorbate 20, polysorbate 80, Triton X-100, and pluronic F68. [0084] As used herein, the term "cut-off value" refers to a dividing point for a quantitative result of a diagnostic test or screen to be indicative of a positive or negative result based on measurements of the level of a molecular marker(s). This disclosure provides methods of detecting Lyme disease and/or Borrelia infection in a subject comprising the step of comparing a measured level of molecular marker to a predetermined value. In some embodiments, comparing a measured value of an antibody against an epitope (e.g., SEQ ID NO: 1 and/or SEQ ID NO: 2) to a predetermined cut-off value of the antibody may be used to decide whether the method indicates a positive or negative result of Lyme disease and/or Borrelia infection in the subject. As used herein, a "cut-off value" refers to a value above which a measured epitope antibody level in a sample is indicative of the positive presence of a Borrelia infection and/or Lyme disease in the subject from which the sample was derived. [0085] As used herein the term "standard two-tier test" (SST) refers to a decision tree that describes the steps required to currently test for Lyme disease. The first required test is the Enzyme Immunoassay (EIA) or Immunofluorescence Assay (IFA). If this test yields negative results, the provider should consider an alternative diagnosis; or in cases where the patient has had symptoms for less than or equal to 30 days, the provider may treat the patient and follow up with a convalescent serum. If the first test yields positive or equivocal results, two options are available: 1) If the patient has had symptoms for less than or equal to 30 days, an IgM Western Blot is performed; 2) if the patient has had symptoms for more than 30 days, the IgG Western Blot is performed. The IgM should not be used if the patient has been ill for more than 30 days. QB\650053.01002\84442353.1 Page 17 of 153 Atty. Dkt. No.650053.01002 [0086] The STT has several well-known shortcomings. Two of the most notable include low sensitivity and specificity in early infection, and the inability to determine infection status after antibody therapy. Diagnostic compositions and methods disclosed herein e.g., that incorporate Peptide 1 (SEQ ID NO: 1) and/or Peptide 2 (SEQ ID NO: 2), such as ELISpot assays, MCH tetramer assays, and proliferation assays, overcome these limitations. [0087] Compositions [0088] In certain embodiments, T cell immunogens derived from BB0680/MCP4 may be used for novel Lyme disease vaccine targets, either alone or in combination with B cell antigens such as OspA or OspC. Thus, disclosed herein are compositions comprising an epitope of the BB0680/MCP4 peptide, wherein the epitope comprises or consists of SEQ ID NO: 1. In some embodiments, the composition comprises one or more additional antigens, such as outer surface protein A, and outer surface protein C (OspA and OspC, respectively). In some embodiments, the additional antigen is a naturally occurring antigen; in some embodiments, the antigen is recombinant. [0089] OspA sequence is shown below (NCBI: Ref. Seq: WP_075552755.1). 1 mkkyllgigl ilaliackqn vssldeknsv svdlpgeikv lvskekdkdg kyslmatvdk 61 lelkgtsdkn ngsgvlegvk adkskvkltv sddlskttle vlkedgktlv srkvtskdks 121 steekfnekg elaektmtra detrleytei ksdgsgkake vlkgyalegt ltaekttlvv 181 kegtvtlskn isksgevtae lndtdsaaat kktgawnsgt stltitansk ktkdlvftke 241 ntitvqkydt agiklegsav eiktldelkn alk (SEQ ID NO: 5) [0090] OspC sequence is shown below (GenBank: AA88006.1) 1 ilmtlflfis cnnsgkdgnt sansadesvk gpnlteiskk itdsnavlla vkeveallss may be used for novel Lyme disease vaccine targets, either alone or in combination with B cell antigens such as OspA or OspC. Thus, disclosed herein are compositions comprising an epitope of the BB0838/LptD peptide. In certain embodiments, the compositions disclosed herein comprise an epitope of the BB0838/LptD peptide, wherein the epitope comprises or consists of SEQ ID NO: 2. In some embodiments, the composition comprises one or more additional antigens, such as outer surface protein A, and outer surface protein C (OspA and OspC, respectively). In some embodiments, the additional antigen is a naturally occurring antigen; in some embodiments, the antigen is recombinant. QB\650053.01002\84442353.1 Page 18 of 153 Atty. Dkt. No.650053.01002 [0092] In one or more embodiments, the compositions disclosed herein can include an epitope of the BB0838/LptD peptide and an epitope of the BB0680/MCP4 peptide. For instance, in certain embodiments, the compositions disclosed herein can include an epitope of the BB0838/LptD peptide, wherein the epitope comprises or consists of SEQ ID NO: 2, and an epitope of the BB0680/MCP4 peptide, wherein the epitope comprises or consists of SEQ ID NO: 1. In various embodiments, the compositions may also include one or more additional antigens, such as outer surface protein A, and outer surface protein C (OspA and OspC, respectively). In some embodiments, the additional antigen is a naturally occurring antigen; in some embodiments, the antigen is recombinant. [0093] In certain embodiments, the compositions disclosed herein can include an epitope of a BB0559/Crr peptide, e.g., Peptide 3, SEQ ID NO: 3, and/or an epitope of oppAIV, e.g., Peptide 4, SEQ ID NO: 4. [0094] In some embodiments, the compositions disclosed herein comprise an adjuvant. In some embodiments, the compositions disclosed herein are provided in lyophilized form. [0095] Methods [0096] Disclosed herein are methods for the treating and diagnosis/detection of infection with Borrelia sp. [0097] In some embodiments, the methods comprise contacting an antibody-containing sample from a subject with a polypeptide of SEQ ID NO: 1 and/or with a polypeptide of SEQ ID NO: 2. [0098] In some embodiments, the method includes allowing the binding of antibodies in the sample to the polypeptide; contacting the bound antibodies with a detectable binding agent; detecting the detectable binding agent; measuring the level of antibodies bound to the polypeptide; and comparing the measured levels of bound antibody to a value, such as a predetermined cutoff value or a value calculated based on the level of a maker in the sample measured in parallel or a control sample (e.g. a sample from a Borrelia sp. exposure naïve subject). [0099] The level of antibodies bound to the polypeptide can then be compared to a value to inform a diagnosis or treatment decision, such as, a diagnosis of Lyme disease or a Borrelia infection. The level of antibodies bound to the polypeptide can be used to monitor the progression of a treatment for Lyme disease or a Borrelia infection. The level of antibodies bound to the polypeptide, or after a series of measurements over a duration of weeks or months, can be used to estimate when the subject was exposed to Borrelia sp. QB\650053.01002\84442353.1 Page 19 of 153 Atty. Dkt. No.650053.01002 [00100] In some embodiments, if the measured level is greater than a predetermined antibody value for the polypeptide, and the subject is diagnosed as positive for Lyme disease. In some embodiments, if the measured level is less than a predetermined antibody value for the polypeptide, the subject is diagnosed as negative for Lyme disease. [00101] In some embodiments, the method further comprises treating the subject for Lyme disease. [00102] As used herein the terms "predetermined value" and "control value" are used interchangeably. For example, in some embodiments, the predetermined value or control value is a cutoff value based on a naïve control antibody level, either measured independently or measured using the same sample. A suitable cutoff value can be determined using routine techniques known to the skilled worker. In some embodiments, the cutoff value is calculated from a measured naïve control level adjusted by a standard deviation or parameter based on the standard deviation. For example, a cutoff value can be a mean naïve control value + 2 standard deviations. In some embodiments, a subject is tested multiple times, and the control value (or predetermined value) comprises the test value of a previous sample from the same subject (e.g., to determine whether a subject is responding favorably to a treatment). In such an exemplary embodiment, the control value (the predetermined value) is greater than the test value if the subject is responsive to treatment, or the control value (the predetermined value) is equal to or less than the test value if the subject is non-responsive to treatment. While it is understood that in some situations a control value is not a predetermined value per-se, the terms "predetermined value" and "control value" are intended to encompass such situations. For example, if the control sample, (e.g., a known naïve control sample, or a known positive sample) is tested simultaneously with the unknown, test sample, and the control value is determined at the time of test completion, then the "control value" is not necessarily "predetermined." However, it is known in advance of testing that the control sample will have a value indicative of a predetermined infection status (e.g., naïve or positive). [00103] In some embodiments, in addition to SEQ ID NO: 1 and/or SEQ ID NO: 2, multiple different polypeptides are employed in testing. In some embodiments, the one or more polypeptides can be configured on a solid support. [00104] In some embodiments of any of the methods above, the detecting comprises detecting the bound antibodies or antibody-epitope complexes using a detectable binding agent. [00105] In some embodiments of any of the methods above, the sample comprises or consists of a blood sample (e.g. whole blood), plasma sample, and/or serum sample. QB\650053.01002\84442353.1 Page 20 of 153 Atty. Dkt. No.650053.01002 [00106] In some embodiments of any of the methods above, the detecting step comprises immobilizing antibody-epitope complexes to a solid support. [00107] In some embodiments, the solid support comprises or consists of a plate, bead, flow cell, flow chamber, microfluidic chamber, and/or microchip comprising a plurality of microfluidic chambers. [00108] In some embodiments, the detecting step comprises flowing the reagent- composition through a flow-chamber. In some embodiments, the detection comprises a microfluidic chamber, microchip comprising a plurality of microfluidic chambers, or lateral flow assay. [00109] In some embodiments, the subject is human and the detectable binding agent comprises an anti-human IgG comprising a detectable label or conjugated to a detectable agent. In some embodiments, the detectable agent comprises an enzyme, such as a horseradish peroxidase. [00110] In some embodiments, a T cell assay is provided. In some embodiments, the T cell assay is configured as an ELISpot assay, an MHC tetramer assay, or a cell proliferation assay. [00111] As used herein, the term "ELISpot" assay refers to the "enzyme-linked immune absorbent spot" assay. The ELISpot assay is often used to quantitatively measure the frequency of cytokine secretion for a single cell. The ELISpot Assay is also a form of immunostaining since it is classified as a technique that uses antibodies to detect a protein analyte, with the word analyte referring to any biological or chemical substance being identified or measured. [00112] As used herein an "MHC tetramer assay" refers to an assay method that uses tetrameric proteins to detect and quantify T cells that are specific for a given antigen within a blood sample. The tetramers used in the assay are made up of four major histocompatibility complex (MHC) molecules, which are found on the surface of most cells in the body. MHC molecules present peptides to T-cells as a way to communicate the presence of viruses, bacteria, cancerous mutations, or other antigens in a cell. If a T-cell's receptor matches the peptide being presented by an MHC molecule, an immune response is triggered. Thus, MHC tetramers that are bioengineered to present a specific peptide can be used to find T-cells with receptors that match that peptide. The tetramers are labeled with a detectable label, such as a fluorophore, allowing tetramer-bound T-cells to be analyzed with flow cytometry. Quantification and sorting of T-cells by flow cytometry enables researchers to investigate immune response to viral infection and vaccine administration as well as functionality of antigen-specific T-cells. Generally, if a subject's immune system has QB\650053.01002\84442353.1 Page 21 of 153 Atty. Dkt. No.650053.01002 encountered a pathogen, the subject will possess T cells with specificity toward some peptide on that pathogen. Hence, if a tetramer stain specific for a pathogenic peptide results in a positive signal, this may indicate that the subject's immune system has encountered and built a response to that pathogen. [00113] T cell proliferation assays are well known in the art and are often used in conjunction with flow cytometric analysis, e.g., to characterize T cells. [00114] In some embodiments of any of the methods above, the subject previously tested positive for Lyme disease by standard two-tier (STT) testing. [00115] In some embodiments of any of the methods above, the subject exhibits one or more of the following symptoms: erythema migrans, facial palsy, and arthritis; and/or the subject already tested positive for Lyme disease in standard two-tier test (STT). In some embodiments, the subject has exhibited the symptom for 3 months or less, 2 months or less, 1 month or less, 2 weeks or less, 1 week or less, 3 days or less, or 1 day or less. [00116] In some embodiments of any of the methods above, the subject has not previously been treated for Lyme disease. [00117] In some embodiments of any of the methods above, the subject is asymptomatic for Lyme disease, but may have come in contact with a blacklegged tick selected from Ixodes scapularis, Ixodes pacificus, Ixodes ricinus, and Ixodes persulcatus. In some embodiments, the possible contact between the subject and the tick was within 3 months, within 2 months, within 1 month, within 2 weeks, within 1 week, within 3 days, or within 1 day. [00118] In some embodiments of any of the methods above, the subject is asymptomatic for Lyme disease and has previously been treated for Lyme disease. In some embodiments, the subject is asymptomatic for Lyme disease and has not previously been treated for Lyme disease. [00119] In some embodiments of any of the methods above, the subject has previously been treated for Lyme disease and exhibits one or more of the following symptoms: erythema migrans, facial palsy, and arthritis; and/or the subject previously tested positive for Lyme disease in standard two-tier test (STT). In some embodiments, the subject has not received treatment for Lyme disease for at least 1 year, for at least 5 years, for at least 10 years, or for at least 15 years. [00120] In some embodiments of any of the methods above, the method comprises a step of treating the subject for Lyme disease. QB\650053.01002\84442353.1 Page 22 of 153 Atty. Dkt. No.650053.01002 [00121] In some embodiments of any of the methods above, the subject is being treated for Lyme disease. In some further embodiments, the method is used to monitor the progression or the efficacy of the treatment. [00122] Kits [00123] Disclosed herein are kits for the detection of infection with Borrelia sp. In some embodiments, the kit comprises a composition described herein and one additional reagent or device. For example, in some embodiments, the kits include a polypeptide comprising SEQ ID NO: 1, or a polypeptide at least 90% identical to SEQ ID NO: 1, configured on a solid support or in a reagent composition. In certain embodiments, the kits include a polypeptide comprising SEQ ID NO: 2, or a polypeptide at least 90% identical to SEQ ID NO: 2, configured on a solid support or in a reagent composition. In some embodiments, the kits include a polypeptide comprising SEQ ID NO: 1 and/or SEQ ID NO: 2. In one or more embodiments, the kits include a polypeptide at least 90% identical to SEQ ID NO: 1 and/or a polypeptide at least 90% identical to SEQ ID NO: 2. In some embodiments, the additional reagent or device is a flow chamber, bead composition, ELISpot assay reagent and/or platform, ELISA reagent, anti-human IgG antibody, and/or a detectable reagent such as a HRP substrate. In some embodiments, a kit includes reagents and components for an MHC tetramer assay. In some embodiments, the kit comprises instructions for using the components of the kit in the performance of a method described herein. In some embodiments, the kits comprise instructions, and are configured for in-home use. [00124] By way of example but not by way of limitation, the kits and components there may be used to evaluate T and/or B cell responses to the epitope(s), which provide novel diagnostic biomarkers for active infection of B. burgdorferi or post-treatment Lyme disease syndrome (PTLDS). In some embodiments, the kits are configured for ELISpot assays, MCH tetramer assays, and/or T cell proliferation assays, and include SEQ ID NO: 1 and/or SEQ ID NO: 2. [00125] Table 1 below shows the predicted mouse MHCII binding of peptides derived from BB0680 determined using NetMHCIIpan (V 4.0). The prediction outcome for each molecule includes the following columns in the table: Pos Residue number (starting from 0); MHC MHC molecule name; Peptide Amino acid sequence; Of Starting position offset of the optimal binding core (starting from 0); Core Binding core register; Core_Rel Reliability of the binding core, expressed as the fraction of networks in the ensemble selecting the optimal core; Score_EL Eluted ligand prediction score; %Rank_EL Percentile rank of eluted ligand prediction score; BindLevel (SB: strong binder, WB: weak binder). The peptide will be identified as a strong binder if the % Rank is below the 1% threshold for the strong binders. QB\650053.01002\84442353.1 Page 23 of 153 Atty. Dkt. No.650053.01002 The peptide will be identified as a weak binder if the % Rank is above the 1% threshold of the strong binders but below the 5% threshold for the weak binders. Table 1. Predicted mouse MHC II binding peptides derived from BB0680 determined using NetMHCIIpan (V.4.0) Pos MHC SEQ ID Peptide Of SEQ ID Core Core_Rel Score_E %Rank_E BindLe allele NO: NO: L L vel 37 H-2- 27 EDYYKQLTR 3 115 YKQLTR 0.793 0.34351 0.39 <=SB B B B B B B B B B B B QB\650053.01002\84442353.1 Page 24 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_Rel Score_E %Rank_E BindLe allele NO: NO: L L vel 154 H-2- 44 NMDFGHSEA 3 126 FGHSEA 1 0.69859 0.48 <=SB B B B B B B B B B B B B B B B B B QB\650053.01002\84442353.1 Page 25 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_Rel Score_E %Rank_E BindLe allele NO: NO: L L vel 299 H-2- 60 VSVYTIDRIL 3 140 YTIDRIL 0.947 0.04629 4.7 <=WB B B B B B B B B B B B B B B B B B B B B B B B B QB\650053.01002\84442353.1 Page 26 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_Rel Score_E %Rank_E BindLe allele NO: NO: L L vel 508 H-2- 85 EESVIAMQDI 4 162 IAMQDI 0.653 0.22328 2.3 <=WB B B B B B B B B B B B B B B B B B B B B B B B QB\650053.01002\84442353.1 Page 27 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_Rel Score_E %Rank_E BindLe allele NO: NO: L L vel 628 H-2- 105 QVGEVVQSS 4 181 VVQSSA 0.98 0.40878 1.66 <=WB B B B B B Table 2 below shows predicted human MHCII binding of peptides derived from BB0680 determined using NetMHCIIpan (V 4.0). The prediction outcome for each molecule includes the following columns in the table: Pos Residue number (starting from 0); MHC MHC molecule name; Peptide Amino acid sequence; Of Starting position offset of the optimal binding core (starting from 0); Core Binding core register; Core_Rel Reliability of the binding core, expressed as the fraction of networks in the ensemble selecting the optimal core; Score_EL Eluted ligand prediction score; %Rank_EL Percentile rank of eluted ligand prediction score; BindLevel (SB: strong binder, WB: weak binder). The peptide will be identified as a strong binder if the % Rank is below the 1% threshold for the strong binders. The peptide will be identified as a weak binder if the % Rank is above the 1% threshold of the strong binders but below the 5% threshold for the weak binders. Table 2. Predicted human MHC II binding of peptides derived from BB0680 determined using NetMHCIIpan (V.4.0) Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL QB\650053.01002\84442353.1 Page 28 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 36 DRB1_0 190 LEDYYKQLTRA 4 370 YKQLTRA 0.947 0.7822 0.08 <=SB QB\650053.01002\84442353.1 Page 29 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 58 DRB1_0 193 FLDTLHVIINGA 4 373 LHVIINGA 0.973 0.5678 2.15 <=WB QB\650053.01002\84442353.1 Page 30 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 95 DRB1_1 203 ELIDLRKNPKF 4 380 LRKNPKF 0.987 0.5771 1.09 <=WB QB\650053.01002\84442353.1 Page 31 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 102 DRB1_1 206 NPKFVIDSVKV 3 381 FVIDSVK 0.813 0.4121 2.77 <=WB QB\650053.01002\84442353.1 Page 32 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 117 DRB1_1 213 RQYLYNFMAN 3 387 LYNFMA 0.94 0.2883 2.56 <=WB QB\650053.01002\84442353.1 Page 33 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 154 DRB1_0 218 NMDFGHSEAN 3 392 FGHSEAN 0.98 0.4483 3 <=WB QB\650053.01002\84442353.1 Page 34 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 189 DRB1_1 231 SEGISAEVAIRS 3 401 ISAEVAIR 0.993 0.2623 1.6 <=WB QB\650053.01002\84442353.1 Page 35 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 205 DRB1_0 235 KKAFAIIVPVYS 3 405 FAIIVPVY 0.993 0.7631 0.57 <=SB QB\650053.01002\84442353.1 Page 36 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 206 DRB1_0 236 KAFAIIVPVYSP 5 406 IVPVYSPE 0.573 0.4961 1.14 <=WB QB\650053.01002\84442353.1 Page 37 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 248 DRB1_1 244 KRGNFIYVDPN 5 412 IYVDPNNI 0.713 0.5200 0.11 <=SB QB\650053.01002\84442353.1 Page 38 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 250 DRB1_0 246 GNFIYVDPNNI 3 412 IYVDPNNI 0.987 0.7653 0.06 <=SB QB\650053.01002\84442353.1 Page 39 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 276 DRB1_0 253 SKFLNVLKDVF 3 418 LNVLKDV 1 0.9408 0.1 <=SB QB\650053.01002\84442353.1 Page 40 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 299 DRB1_0 259 VSVYTIDRILLS 3 423 YTIDRILL 1 0.4632 0.64 <=SB QB\650053.01002\84442353.1 Page 41 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 340 DRB1_0 270 YKDIYGVISSLR 4 432 YGVISSLR 0.967 0.6404 0.95 <=SB QB\650053.01002\84442353.1 Page 42 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 369 DRB5_0 278 LSIRIDRIISFRL 4 439 IDRIISFRL 0.82 0.2523 4.11 <=WB QB\650053.01002\84442353.1 Page 43 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 397 DRB1_0 290 DKDYALDDDE 3 448 YALDDDE 1 0.6551 1.26 <=WB QB\650053.01002\84442353.1 Page 44 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 421 DRB1_0 299 KMKKAISVAIS 5 453 ISVAISSV 0.807 0.5148 2.07 <=WB QB\650053.01002\84442353.1 Page 45 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 435 DRB1_1 306 RNISYVNKASL 4 457 YVNKASL 0.52 0.3866 4.39 <=WB QB\650053.01002\84442353.1 Page 46 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 491 DRB1_1 315 QIALKTNENSQI 3 465 LKTNENS 0.987 0.4033 2.9 <=WB QB\650053.01002\84442353.1 Page 47 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 524 DRB1_0 326 IEEIARKTNLLA 3 473 IARKTNL 1 0.8408 0.17 <=SB QB\650053.01002\84442353.1 Page 48 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 549 DRB5_0 332 GKGFAVVASEI 3 477 FAVVASE 1 0.9308 0.03 <=SB QB\650053.01002\84442353.1 Page 49 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 565 DRB1_1 340 LSKISALEIGEL 3 483 ISALEIGE 0.987 0.3091 3.98 <=WB QB\650053.01002\84442353.1 Page 50 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 619 DRB1_0 352 IAQFKMALDQV 3 494 FKMALD 1 0.8688 0.24 <=SB QB\650053.01002\84442353.1 Page 51 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 660 DRB1_0 358 SVLFFKIKDSKI 3 499 FFKIKDSK 0.973 0.5755 1.32 <=WB QB\650053.01002\84442353.1 Page 52 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ ID Core Core_ Score_ %Rank_ BindLevel NO: NO: Rel EL EL 721 DRB1_1 365 ESSVRTINKRV 3 507 VRTINKR 0.973 0.5149 0.89 <=SB determined using NetMHCIIpan (V 4.0). The prediction outcome for each molecule includes QB\650053.01002\84442353.1 Page 53 of 153 Atty. Dkt. No.650053.01002 the following columns in the table: Pos Residue number (starting from 22); MHC molecule name; Peptide Amino acid sequence; Of Starting position offset of the optimal binding core (starting from 0); Core Binding core register; Core_Rel Reliability of the binding core, expressed as the fraction of networks in the ensemble selecting the optimal core; Score_EL Eluted ligand prediction score; %Rank_EL Percentile rank of eluted ligand prediction score; BindLevel (SB: strong binder, WB: weak binder). The peptide will be identified as a strong binder if the % Rank is below the 1% threshold for the strong binders. The peptide will be identified as a weak binder if the % Rank is above the 1% threshold of the strong binders but below the 5% threshold for the weak binders. Table 3: Predicted human CD4+ T cell epitopes from B. burgdorferi LptD Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO W B W W B W W W W B W W W W W W W B QB\650053.01002\84442353.1 Page 54 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: B B B W W B B W W W W W W W W W W W W W W W W W B W W W QB\650053.01002\84442353.1 Page 55 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: B W W W B W B W B W B W W W W B W B W W W B W B W W W B QB\650053.01002\84442353.1 Page 56 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W B W W W W W W W W B B W W W W W B W QB\650053.01002\84442353.1 Page 57 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W W B B W W W W W W W B B W W B B QB\650053.01002\84442353.1 Page 58 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W B B W W W B B W W B W W B W B W B W W W W W W W W W QB\650053.01002\84442353.1 Page 59 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W B W B W B B W W W W B W B B W W W W W W W W W W B W B QB\650053.01002\84442353.1 Page 60 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: B W W W W W B W B W W W W W W W W W W W W W W W W B W B QB\650053.01002\84442353.1 Page 61 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W B W W W W B B W W W W W B B W W B QB\650053.01002\84442353.1 Page 62 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: B W W W B B W W W W W W W W W B B W B B W W W B B B B W QB\650053.01002\84442353.1 Page 63 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W B W W B W W W W B B B W W B W W W W W B B B QB\650053.01002\84442353.1 Page 64 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W B W W W B W W B W W W W W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 65 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W W W B W W W W W B W W W W W B W QB\650053.01002\84442353.1 Page 66 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W B W W W W B W B W W W B W W W W W W B W W W W W W QB\650053.01002\84442353.1 Page 67 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W B W W W W W W W B W W W W W W W W W W W W W B W QB\650053.01002\84442353.1 Page 68 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W B W B W B W B W B W W W W W W W W W W W W W W W W W B QB\650053.01002\84442353.1 Page 69 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W B W W W W W W W W W W W W W W W W W W B W B W W QB\650053.01002\84442353.1 Page 70 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: B W B B B W W B W B B B W W B W B W W W W W W W W W W W QB\650053.01002\84442353.1 Page 71 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W B W W W W W W B W W W W W W W W W W W QB\650053.01002\84442353.1 Page 72 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W B W W B W W W W W B B W B W W W W B W B W B W W QB\650053.01002\84442353.1 Page 73 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W B W B B W B B W W W W W W B B W W W W B W B B W B B QB\650053.01002\84442353.1 Page 74 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W B W W W B B B W W B W B B W W W B W W W W W B W B B B QB\650053.01002\84442353.1 Page 75 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: B W B B W W B W W W W B W B B B W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 76 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W B B B W W W W W W W W W W W B B W W W W W B B W W W QB\650053.01002\84442353.1 Page 77 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W B B W W B B W W W W W W W W W W W B W W W W W W W W B QB\650053.01002\84442353.1 Page 78 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: B W W B W W W W W W W W W W B W W W W W W W W W W B B W QB\650053.01002\84442353.1 Page 79 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W B W W W W B W W B W B B W W W W W W W W QB\650053.01002\84442353.1 Page 80 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W W W W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 81 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W W B W B W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 82 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W B W W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 83 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W B W B W W W B W W W W W W B W W W B W W W B W W B W QB\650053.01002\84442353.1 Page 84 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W W W B W B W B W W B W B W W W B QB\650053.01002\84442353.1 Page 85 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W B B W W B W W W W B B B W W B W W W W B B B QB\650053.01002\84442353.1 Page 86 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W B W W W W W W W W W W W W W W W W W W W B W QB\650053.01002\84442353.1 Page 87 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W B W W W W W W W B W W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 88 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W B B B B B B B B W W W W B B W W B B W W B B W W QB\650053.01002\84442353.1 Page 89 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W B W W W W W W W W W W W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 90 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W B B W B W B W B W B B B W W W W W B QB\650053.01002\84442353.1 Page 91 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W B W B W W W B W B W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 92 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W W B W W W W B W W W B W W W B W QB\650053.01002\84442353.1 Page 93 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W B W W W W W W W W B W W W B W W W W W B W W W W QB\650053.01002\84442353.1 Page 94 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: B W W W W W W W B W B W W W W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 95 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W W B W W B W W W B W W W W W W W QB\650053.01002\84442353.1 Page 96 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W W W W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 97 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W W W W W W W B B B W B B W W W W QB\650053.01002\84442353.1 Page 98 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W B B B W B B W W W W W W W W W W W W W B W W B B W W W QB\650053.01002\84442353.1 Page 99 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: B W W W B B W W W B W W W W B W W W B B B B W B W W W W QB\650053.01002\84442353.1 Page 100 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: B B B W W W W W W W W W W W W W W W W W B W W W B W W W QB\650053.01002\84442353.1 Page 101 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W B W W W W W W W W W W W W W W W W W W W W W W W B B QB\650053.01002\84442353.1 Page 102 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: B B W W W W W W W W W W W W B W W B W B B W W W W B W W QB\650053.01002\84442353.1 Page 103 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W B W W W W W W W W W W W B W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 104 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W W B W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 105 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W B B W W W W W W W W B B W W W W W W W W W W QB\650053.01002\84442353.1 Page 106 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W B W W W W W B B W W W W W W W B B QB\650053.01002\84442353.1 Page 107 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W B W W W W B W W W W W B W B W W W B W W W B B W W B B QB\650053.01002\84442353.1 Page 108 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W B B W W W B B W W W W W B W W B W W W W W W W B QB\650053.01002\84442353.1 Page 109 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W B W B W W W W W B B B W W B B W W B B B B B B B W B B QB\650053.01002\84442353.1 Page 110 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: B B B B B B W W W W W W W W W W W W W W W W B W W W W W QB\650053.01002\84442353.1 Page 111 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W B W W W W W W W W W W W W W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 112 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W W W W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 113 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W W W W W W W B W W W W W B B W B QB\650053.01002\84442353.1 Page 114 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W B W B W W W B W W B B W B W B W B W W W B W W B B W W QB\650053.01002\84442353.1 Page 115 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W B W W W W W W W W W W W W W W B W B W W W B W B W W QB\650053.01002\84442353.1 Page 116 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W B B B W W W W W W W W W B B W B W W W W W B W QB\650053.01002\84442353.1 Page 117 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W B W W W W W W W W B W W W B W B W W W W B W W QB\650053.01002\84442353.1 Page 118 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W B W W W B W W B W W W W W W W W W B W B W W B QB\650053.01002\84442353.1 Page 119 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W B W W W W W B W B W W W W B B W W W B B W B W B W W QB\650053.01002\84442353.1 Page 120 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: B B W B W W W W W W W W W W W W W W W W W W B W B W W W QB\650053.01002\84442353.1 Page 121 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W W W W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 122 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W W W W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 123 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W W W W W B W W W W W W W W W W W QB\650053.01002\84442353.1 Page 124 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W B W W W B B W W B W B W W B W B B B W W W W W W W W QB\650053.01002\84442353.1 Page 125 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W W W W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 126 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W B W B W W W W W W W W B B B W B W W B W B W QB\650053.01002\84442353.1 Page 127 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W B B B W B W W W W W W W W W W W W W B W W W W W W W W QB\650053.01002\84442353.1 Page 128 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W B W W W W W B W W W W W W W B W W W W W W W W QB\650053.01002\84442353.1 Page 129 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W B W W W W W W W W B W W W W B B W W W W W W W W B B B QB\650053.01002\84442353.1 Page 130 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W B W W W W W W W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 131 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W B W W W W W W W W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 132 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W W W W W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 133 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W B W W W W W W W W W W W W W W W W W QB\650053.01002\84442353.1 Page 134 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ ID Peptide Of SEQ Core Core_R Identity Score_EL %Rank Bind NO: ID el _EL Level NO: W W W W W W W W W W W B W W W W W W B W W Table 4 below shows predicted human MHCII binding of peptides derived from BB0838 determined using NetMHCIIpan (V 4.0). The prediction outcome for each molecule includes the following columns in the table: Pos Residue number (starting from 923); MHC molecule name; Peptide Amino acid sequence; Of Starting position offset of the optimal binding core (starting from 0); Core Binding core register; Core_Rel Reliability of the binding core, expressed as the fraction of networks in the ensemble selecting the optimal core; Score_EL QB\650053.01002\84442353.1 Page 135 of 153 Atty. Dkt. No.650053.01002 Eluted ligand prediction score; %Rank_EL Percentile rank of eluted ligand prediction score; BindLevel (SB: strong binder, WB: weak binder). The peptide will be identified as a strong binder if the % Rank is below the 1% threshold for the strong binders. The peptide will be identified as a weak binder if the % Rank is above the 1% threshold of the strong binders but below the 5% threshold for the weak binders. Table 4: Predicted human CD4+ T cell epitopes within B. burgdorferi LptD 922-972 Pos MHC SEQ Peptide Of SEQ Core Core_ Identity Score_EL %Rank Bind ID ID Rel _EL Level NO: NO: B B B B B B B B B B B B B B B B B B B B B QB\650053.01002\84442353.1 Page 136 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ Peptide Of SEQ Core Core_ Identity Score_EL %Rank Bind ID ID Rel _EL Level NO: NO: B B B B B B B B B B B B B B B B B B B B B B B B B B B B QB\650053.01002\84442353.1 Page 137 of 153 Atty. Dkt. No.650053.01002 Pos MHC SEQ Peptide Of SEQ Core Core_ Identity Score_EL %Rank Bind ID ID Rel _EL Level NO: NO: B B B B EXAMPLES [00126] The following Examples are illustrative and are not intended to limit the scope of the claimed subject matter. [00127] The technology disclosed and exemplified herein has profound implications for diagnosis and treatment of Lyme disease and post-treatment Lyme disease syndrome (PTLDS). T cell responses to B. burgdorferi can now be tracked during and after antibiotic therapy and the powerful T cell arm of the immune system can now be harnessed to hunt down and destroy any bacterial antigens that are sequestered in immune-privileged sites, such as dense fibrotic tissue, following antibiotic therapy. A similar approach is used to treat other hard-to-treat infectious diseases such as tuberculosis and is now being adopted for new types of cancer therapy. [00128] Example 1 - Identification of highly immunogenic epitope of B. burgdorferi [00129] Using an immunopeptidomics approach we have recently identified and validated a highly immunogenic CD4+ T cell epitope derived from a protein involved in chemotaxis produced during B. burgdorferi infection (Peptide 1 (SEQ ID NO: 1)). FIG. 1. (MCP4 _442-462 ), hereafter Peptide 1 (SEQ ID NO: 1) is a methyl-accepting chemotaxis protein that is highly conserved amongst both sensu lato and sensu stricto strains of Lyme disease spirochetes (FIG. 3, FIG. 5). Peptide 1 is highly immunogenic in mice infected with B. burgdorferi (FIG. 4), validating Peptide 1 as target of CD4+ T cell responses to B. burgdorferi infection. Peptide 1 is one of a number of peptides derived from MCP4 predicted to bind to MHC class II alleles in mice and/or humans (FIG. 5). It is anticipated that immunization with Peptide 1 will lead to protective immunity in mice and humans. It is also anticipated that other epitopes derived from MCP4 are immunogenic in mice and humans infected with B. burgdorferi. [00130] Example 2 - Test the therapeutic potential of generating immune responses to Peptide 1 in mice. QB\650053.01002\84442353.1 Page 138 of 153 Atty. Dkt. No.650053.01002 [00131] Mice will be immunized with one or more of peptide 1 (SEQ ID NO: 1) and/or Peptide 2 (SEQ ID NO: 2) and tested for protection against B. burgdorferi infection. It is anticipated that immunized mice will exhibit fewer or no symptoms of infection compared to unimmunized controls mice. It is further anticipated that mice immunized with a vaccine composition comprising SEQ ID NO: 1 and/or SEQ ID NO: 2, or a polypeptide at least 90% identical to SEQ ID NO: 1 and/or a polypeptide at least 90% identical to SEQ ID NO: 2, will exhibit fewer or no symptoms of infection compared to mice immunized with prior art vaccines. It is further anticipated that mice immunized with a vaccine composition comprising SEQ ID NO: 1 and/or SEQ ID NO: 2, or a polypeptide at least 90% identical to SEQ ID NO: 1 and/or a polypeptide at least 90% identical to SEQ ID NO: 2, will exhibit an increase in CD4+ T-cell population as compared to unimmunized control mice, or mice immunized with prior art vaccines. [00132] Example 3 - Determine immune responses to target antigen in human patients during active infection and in patients with post-treatment Lyme disease syndrome (PTLDS). [00133] Biobanks comprising Lyme disease patient samples will be evaluated to measure adaptive T and B cell responses to the target antigen (SEQ ID NO: 1 and/or SEQ ID NO: 2, or a polypeptide at least 90% identical to SEQ ID NO: 1 and/or a polypeptide at least 90% identical to SEQ ID NO: 2) during early infection, late infection, and post-antibiotics (PTLDS). It is anticipated that strong T cell response will be exhibited against SEQ ID NO: 1 and/or SEQ ID NO: 2 as compared to other antigens evaluated. [00134] Lyme disease patients will be vaccinated with a composition comprising SEQ ID NO: 1 and/or SEQ ID NO: 2, or a polypeptide at least 90% identical to SEQ ID NO: 1 and/or a polypeptide at least 90% identical to SEQ ID NO: 2, and samples will be evaluated to measure adaptive T and B cell responses to the target antigen (SEQ ID NO: 1 and/or SEQ ID NO: 2, or a polypeptide at least 90% identical to SEQ ID NO: 1 and/or a polypeptide at least 90% identical to SEQ ID NO: 2) during early infection, late infection, and post-antibiotics (PTLDS). It is anticipated that strong T cell response will be exhibited against SEQ ID NO: 1 and/or SEQ ID NO: 2 as compared to unvaccinated controls, or as compared to other antigens evaluated. [00135] Example 4 - Develop diagnostic reagents that can be used to measure the evolution of CD4+ T cell responses to B. burgdorferi before and after antibiotic therapy. [00136] A panel of tetramer reagents will be generated that can be used to fluorescently label individual CD4+ T cell responses to the target antigen in a wide range of genetic backgrounds. This set of tools will be used to generate a diagnostic platform to measure T cell responses to QB\650053.01002\84442353.1 Page 139 of 153 Atty. Dkt. No.650053.01002 B. burgdorferi in patients both before and after antibiotic therapy. Exemplary diagnostic reagents include ELISpot assays, MCH tetramer assays, and T cell proliferation assays. [00137] Example 5 - Identification of highly immunogenic epitope of B. burgdorferi [00138] Using an immunopeptidomics approach as described above and in Figure 1 we have recently identified several peptides bound to MHC class II molecules expressed on murine macrophages cocultured with Borrelia burgdorferi (FIG. 6). The most abundant peptide of those listed in FIG.6 is derived from BB0838 (LptD923-934), hereinafter peptide 2 (SEQ ID NO: 2). LptD is an outer membrane protein (FIG.7) involved in translocation of lipoproteins such as OspA and OspC from the periplasm to the outer membrane and is essential for cell growth. The LptD _923-934 epitope is located at the interface between the central β-barrel domain and the C-terminal β-barrel/plug domain (FIG. 7). Based on structure modeling, this epitope is localized at or near the cell surface, within the outer membrane-spanning β-barrel (FIG. 7). LptD is highly conserved amongst both sensu lato and sensu stricto strains of Lyme disease spirochetes, and the region surrounding the LptD _923-934 epitope includes numerous promiscuous epitopes, or peptides predicted to bind to a large number of human HLADRB1 alleles (FIG.8). Peptide 2 is one of a number of peptides derived from LptD predicted to bind to MHC class II alleles in humans (FIG.8 and Table 3). It is anticipated that immunization with Peptide 2 will lead to protective immunity in humans and mice. It also anticipated that other epitopes derived from LptD are immunogenic in humans and mice infected with B. burgdorferi. In some embodiments, and pursuant to the methods disclosed herein, T and B cell reactivity to LptD in humans with early and late Lyme disease, and in patients with PTLDS will be measured. [00139] Example 6 – Identification of Bb-derived MHC class II epitopes that are presented by antigen presenting cells (APCs) in mouse lymph nodes during infection, and by human and mouse APCs stimulated with Bb in vitro [00140] There is an urgent and unmet need for a safe and effective Lyme disease (LD) vaccine. Current efforts are underway to generate a next-generation LD vaccine for use in humans. The first-generation vaccine, LYMErix, targeted the Borrelia burgdorferi (Bb) outer surface protein A (OspA) immunogen, and is the basis for a current vaccine in clinical trials. While safe and somewhat effective, LYMErix and the current vaccine candidate targeting OspA share several weaknesses, including rapid down-regulation of the target antigen (OspA) during tick-to-host transmission, poor T-cell-dependent antibody responses to the immunogen, the need for multiple injections, limited cross-protection against different LD serotypes that express antigenically variable OspA types, and a loss of protective immunity ~6-12 months following initial immunization. Our discovery will address these weaknesses by using T-cell- QB\650053.01002\84442353.1 Page 140 of 153 Atty. Dkt. No.650053.01002 directed LD vaccine component directed against conserved and constitutively expressed Bb MHC class II epitopes we have recently identified. When used in conjunction with a B cell vaccine component using OspA or other outer surface proteins (Osps) as immunogens, this component will broaden and strengthen long-term protection against infection with antigenically diverse Bb genospecies (See FIG.9). [00141] Using an immunopeptidomics approach as described above and in Figure 1 we have identified Bb-derived MHC class II epitopes that are presented by antigen presenting cells (APCs) in mouse lymph nodes during infection, and by human and mouse APCs stimulated with Bb in vitro (see Table 5 below). These MHC-II peptides will be synthesized, will be validated using mass spectrometry, and a subset are being tested for CD4+ T cell reactivity in infected and/or immunized mice. A vaccine component will be developed directed at conserved Bb MHC-II epitopes from proteins identified by LC-MS/MS (Table 5 below) to boost T cell, B cell, and antibody responses to humans or dogs immunized with Osp-based vaccines. It is believed that this will result in elevated levels of long-lived memory T cells, memory B cells, and plasma cells; higher-affinity and expanded antibody responses; and cross-protection against Bb sensu stricto (Bbss) and Bb sensu lato (Bbsl) isolates with different OspA serotypes, compared with Osp vaccination alone. Table 5: MHC class II peptides identified by LC-MS/MS New peptides Gene ID SEQ ID Name Peptide Source QB\650053.01002\84442353.1 Page 141 of 153 Atty. Dkt. No.650053.01002 B ^{B_0612 18 ClpX ATTLTEAGYVGEDVE Human} APCs B ^B_RS06830 ₁₉ ^{ERF family} KIESDLILY Human [00143] Pietikäinen A, Backman I, Henningsson AJ, Hytönen J. Clinical performance and analytical accuracy of a C6 peptide-based point-of-care lateral flow immunoassay in Lyme borreliosis serology. Diagn Microbiol Infect Dis. 2022 May;103(1):115657. doi: 10.1016/j.diagmicrobio.2022.115657. Epub 2022 Feb 3. PMID: 35228132. [00144] Camire AC, Hatke AL, King VL, Millership J, Ritter DM, Sobell N, Weber A, Marconi RT. Comparative analysis of antibody responses to outer surface protein (Osp)A and OspC in dogs vaccinated with Lyme disease vaccines. Vet J. 2021 Jul;273:105676. doi: 10.1016/j.tvjl.2021.105676. Epub 2021 Apr 14. PMID: 34148599; PMCID: PMC8254658. [00145] Numbered Clauses [00146] Clause 1. A polypeptide comprising or consisting of a fragment of BB0838 (LptD), or variant thereof. [00147] Clause 2. A composition comprising the polypeptide of clause 1, optionally, wherein the polypeptide comprises SEQ ID NO: 2, or a polypeptide 90% identical to SEQ ID NO: 2, and an adjuvant. [00148] Clause 3. The composition of clause 2, wherein the polypeptide is SEQ ID NO: 2. [00149] Clause 4. The composition any of the previous clauses, comprising at least one additional polypeptide. [00150] Clause 5. The composition of any of the previous clauses, wherein the at least one additional polypeptide comprises OspA or OspC. QB\650053.01002\84442353.1 Page 142 of 153 Atty. Dkt. No.650053.01002 [00151] Clause 6. The composition of any one of clauses 2-5, wherein the composition is in lyophilized form. [00152] Clause 7. A method of treating Lyme disease, or a method for the preventative treatment of Lyme disease, the method comprising: administering to a subject the polypeptide of clause 1, or the composition of any of clauses 2-6. [00153] Clause 8. The method of clause 7, wherein the subject is asymptomatic for Lyme disease, but may have come in contact with a blacklegged tick selected from Ixodes scapularis or Ixodes pacificus. [00154] Clause 9. The method of clause 8, wherein the possible contact was within 3 months. [00155] Clause 10. The method of clause 8, wherein the possible contact was within 2 months. [00156] Clause 11. The method of clause 8, wherein the possible contact was within 1 month. [00157] Clause 12. The method of clause 8, wherein the possible contact was within 2 weeks. [00158] Clause 13. The methods of clause 8, wherein the possible contact was within 1 week. [00159] Clause 14. The method of clause 8, wherein the possible contact was within 3 days. [00160] Clause 15. The method of clause 8, wherein the possible contact was within 1 day. [00161] Clause 16. The method of any one of clauses 7-15, wherein the subject has not previously been treated for Lyme disease. [00162] Clause 17. The method of clause 7, wherein the subject is asymptomatic for Lyme disease and has previously been treated for Lyme disease. [00163] Clause 18. The method of clause 17, wherein the subject previously tested positive for Lyme disease by standard two-tier (STT) testing. [00164] Clause 19. The method of clause 18, wherein the subject has previously been treated for Lyme disease and exhibits one or more of the following symptoms: erythema migrans, facial palsy, and arthritis; and/or the subject tests positive for Lyme disease in standard two-tier test (STT). [00165] Clause 20. The method of clauses 19, wherein the subject has not received treatment for Lyme disease for at least 1 year. [00166] Clause 21. The method of clauses 19, wherein the subject has not received treatment for Lyme disease for at least 5 years. QB\650053.01002\84442353.1 Page 143 of 153 Atty. Dkt. No.650053.01002 [00167] Clause 22. The method of clauses 19, wherein the subject has not received treatment for Lyme disease for at least 10 years. [00168] Clause 23. The method of clauses 19, wherein the subject has not received treatment for Lyme disease for at least 15 years. [00169] Clause 24. The method of clauses 7-23, wherein the Lyme disease is caused by a Borrelia sp. bacteria. [00170] Clause 25. The method of any one of clauses 7-23, wherein the Lyme disease is caused by Borrelia burgdorferi. [00171] Clause 26. A method for testing a subject for the presence of Borrelia sp. bacteria, the method comprising: contacting a subject sample to the polypeptide of clause 1. [00172] Clause 27. The method of clause 26, wherein the polypeptide comprises SEQ ID NO: 2. [00173] Clause 28. The method of clause 27, wherein the polypeptide is SEQ ID NO: 2. [00174] Clause 29. The method of clause 26, wherein the polypeptide is linked to a solid support. [00175] Clause 30. The method of clause 26, wherein the subject sample comprises a blood or serum sample. [00176] Clause 31. A kit comprising the polypeptide of clause 1 linked to a solid support. [00177] Clause 32. A polypeptide comprising or consisting of a fragment of BB0680 (MCP4), or variant thereof. [00178] Clause 33. A composition comprising the polypeptide of clause 32, optionally, wherein the polypeptide comprises SEQ ID NO: 1, or a polypeptide 90% identical to SEQ ID NO: 1, and an adjuvant. [00179] Clause 34. The composition of clause 33, wherein the polypeptide is SEQ ID NO: 1. [00180] Clause 35. The composition clause 33 or 34, comprising at least one additional polypeptide. [00181] Clause 36. The composition of any one of clauses 33-35, wherein the at least one additional polypeptide comprises OspA or OspC. [00182] Clause 37. The composition of any one of clauses 33-36, wherein the composition is in lyophilized form. [00183] Clause 38. A method of treating Lyme disease, or a method for the preventative treatment of Lyme disease, the method comprising: administering to a subject the polypeptide of clause 32, or the composition of any of clauses 33-37. QB\650053.01002\84442353.1 Page 144 of 153 Atty. Dkt. No.650053.01002 [00184] Clause 39. The method of clause 38, wherein the subject is asymptomatic for Lyme disease, but may have come in contact with a blacklegged tick selected from Ixodes scapularis or Ixodes pacificus. [00185] Clause 40. The method of clause 39, wherein the possible contact was within 3 months. [00186] Clause 41. The method of clause 39, wherein the possible contact was within 2 months. [00187] Clause 42. The method of clause 39, wherein the possible contact was within 1 month. [00188] Clause 43. The method of clause 39, wherein the possible contact was within 2 weeks. [00189] Clause 44. The methods of clause 39, wherein the possible contact was within 1 week. [00190] Clause 45. The method of clause 39, wherein the possible contact was within 3 days. [00191] Clause 46. The method of clause 39, wherein the possible contact was within 1 day. [00192] Clause 47. The method of any one of clauses 38-46, wherein the subject has not previously been treated for Lyme disease. [00193] Clause 48. The method of clause 38, wherein the subject is asymptomatic for Lyme disease and has previously been treated for Lyme disease. [00194] Clause 49. The method of clause 48, wherein the subject previously tested positive for Lyme disease by standard two-tier (STT) testing. [00195] Clause 50. The method of clause 49, wherein the subject has previously been treated for Lyme disease and exhibits one or more of the following symptoms: erythema migrans, facial palsy, and arthritis; and/or the subject tests positive for Lyme disease in standard two-tier test (STT). [00196] Clause 51. The method of clauses 49, wherein the subject has not received treatment for Lyme disease for at least 1 year. [00197] Clause 52. The method of clauses 49, wherein the subject has not received treatment for Lyme disease for at least 5 years. [00198] Clause 53. The method of clauses 49, wherein the subject has not received treatment for Lyme disease for at least 10 years. [00199] Clause 54. The method of clauses 49, wherein the subject has not received treatment for Lyme disease for at least 15 years. QB\650053.01002\84442353.1 Page 145 of 153 Atty. Dkt. No.650053.01002 [00200] Clause 55. The method of any one of clauses 38-54, wherein the Lyme disease is caused by a Borrelia sp. bacteria. [00201] Clause 56. The method of any one of clauses 38-54, wherein the Lyme disease is caused by Borrelia burgdorferi. [00202] Clause 57. A method for testing a subject for the presence of Borrelia sp. bacteria, the method comprising: contacting a subject sample to the polypeptide of clause 32. [00203] Clause 58. The method of clause 57, wherein the polypeptide comprises SEQ ID NO: 1. [00204] Clause 59. The method of clause 58, wherein the polypeptide is SEQ ID NO: 1. [00205] Clause 60. The method of clause 57, wherein the polypeptide is linked to a solid support. [00206] Clause 61. The method of clause 57, wherein the subject sample comprises a blood or serum sample. [00207] Clause 62. A kit comprising the polypeptide of clause 32 linked to a solid support. [00208] Clause 63. The composition of clause 4 or 5, wherein the at least one additional polypeptide comprises a polypeptide comprising or consisting of an amino acid sequence of SEQ ID NO: 1, or a polypeptide comprising or consisting of an amino acid sequence having 90% identity to SEQ ID NO: 1. [00209] Clause 64. The composition of clause 4, 5, or 63, wherein the one additional polypeptide comprises: a polypeptide comprising or consisting of an amino acid sequence of SEQ ID NO: 3, or a polypeptide comprising or consisting of an amino acid sequence having 90% identity to SEQ ID NO: 3, a polypeptide comprising or consisting of an amino acid sequence of SEQ ID NO: 4, or a polypeptide comprising or consisting of an amino acid sequence having 90% identity to SEQ ID NO: 4, or a combination thereof. [00210] Clause 65. The composition of clause 35 or 36, wherein the at least one additional polypeptide comprises a polypeptide comprising or consisting of the amino acid sequence of SEQ ID NO: 2, or a polypeptide comprising or consisting of an amino acid sequence having 90% identity to SEQ ID NO: 2. [00211] Clause 66. The composition of clause 35, 36, or 65, wherein the one additional polypeptide comprises: a polypeptide comprising or consisting of an amino acid sequence of SEQ ID NO: 3, or a polypeptide comprising or consisting of an amino acid sequence having 90% identity to SEQ ID NO: 3, a polypeptide comprising or consisting of an amino acid sequence of SEQ ID NO: 4, or a polypeptide comprising or consisting of an amino acid sequence having 90% identity to SEQ ID NO: 4, or a combination thereof. QB\650053.01002\84442353.1 Page 146 of 153 Atty. Dkt. No.650053.01002 [00212] Clause 67. A composition comprising one or more of: a polypeptide at least 90% or 95% identical to SEQ ID NO: 1, a polypeptide at least 90% or 95% identical to SEQ ID NO: 2, a polypeptide at least 90% or 95% identical to SEQ ID NO: 3, or a polypeptide at least 90% or 95% identical to SEQ ID NO: 4. [00213] Clause 68. The composition of clause 67, further comprising an adjuvant. [00214] Clause 69. A method of treating Lyme disease, or a method for the preventative treatment of Lyme disease, the method comprising: administering to a subject the composition of clause 67. [00215] In the foregoing description, it will be readily apparent to one skilled in the art that varying substitutions and modifications may be made to the invention disclosed herein without departing from the scope and spirit of the invention. The invention illustratively described herein suitably may be practiced in the absence of any element or elements, limitation or limitations which is not specifically disclosed herein. The terms and expressions which have been employed are used as terms of description and not of limitation, and there is no intention that in the use of such terms and expressions of excluding any equivalents of the features shown and described or portions thereof, but it is recognized that various modifications are possible within the scope of the invention. Thus, it should be understood that although the present invention has been illustrated by specific embodiments and optional features, modification and/or variation of the concepts herein disclosed may be resorted to by those skilled in the art, and that such modifications and variations are considered to be within the scope of this invention. [00216] All methods described herein can be performed in any suitable order unless otherwise indicated herein or otherwise clearly contradicted by context. The use of any and all examples provided herein, is intended merely to better illuminate the invention and does not pose a limitation on the scope of the invention unless otherwise claimed. No language in the specification should be construed as indicating any non-claimed element as essential to the practice of the invention. [00217] Citations to a number of patent and non-patent references are made herein. The cited references are incorporated by reference herein in their entireties. In the event that there is an inconsistency between a definition of a term in the specification as compared to a definition of the term in a cited reference, the term should be interpreted based on the definition in the specification. QB\650053.01002\84442353.1 Page 147 of 153