Immunoregulatory antigen-presenting vesicles

Abstract

Disclosed herein include methods, compositions, and kits suitable for use in modulating immune responses and treating diseases or disorders. There are provided, in some embodiments, nucleic acid compositions (e.g., mRNA vaccines, DNA vaccines) comprising one or more polynucleotides encoding components of an antigen presentation complex (APC). The APC can comprise an APC-assembly domain, one or more antigen presentation polypeptide(s) and a presenting peptide. A plurality of APCs can be capable of self-assembling into an antigen-presenting vesicle (APV) secreted from a cell in which the APCs are expressed. There are provided, in some embodiments, populations of APVs.

Description

IMMUNOREGULATORY ANTIGEN-PRESENTING VESICLESRELATED APPLICATIONS

[0001] This application claims the benefit under 35 U.S.C. §119(e) of U.S. Provisional Patent Application Ser. No. 63 / 632,954, filed April 11, 2024, and U.S. Provisional Patent Application Ser. No. 63 / 728,287, filed December 5, 2024. The entire contents of these applications are hereby expressly incorporated by reference in their entireties.STATEMENT REGARDING FEDERALLY SPONSORED R&D

[0002] This invention was made with government support under Grant No. W91 INF-19-2-0026 awarded by the Army. The government has certain rights in the invention.REFERENCE TO SEQUENCE LISTING

[0003] The present application is being filed along with a Sequence Listing in electronic format. The Sequence Listing is provided as a file entitled 30KJ-810005- WO SequenceListing, created April 10, 2025, which is 325 kilobytes in size. The information in the electronic format of the Sequence Listing is incorporated herein by reference in its entirety.BACKGROUNDField

[0004] The present disclosure relates generally to the field of immune medicine, in particular, to self-assembling vesicles for treating and regulating immune responses against diseases and disorders.Description of the Related Art

[0005] The release of B cell-derived extracellular vesicles (EVs) with functional peptide:MHC (pMHC) complexes on their surface was first reported about thirty years ago. Since then, EVs that were previously labeled as simple cellular “debris” have been increasingly recognized for their immunoregulatory potential as a simpler, cell-free alternative to cell-based immunotherapies. Naturally occurring pMHC -di splaying antigen-presenting vesicles (APVs) in particular have been demonstrated to orchestrate immune responses either directly or with the aid of antigen-presenting cells. Research teams have ventured to engineer more complex versions of these antigen-presenting vesicles, such as whole mammalian cells conjugated with immunostimulatory molecules, nanoparticles coated with membranes derived from antigen- presenting cells via extrusion or sonication, or engineered extracellular blebs from dendritic cells. These previous approaches demonstrated the therapeutic potential of APVs, but production is often low yield or requires the patient’s own cells to be harvested and processed before treatment can be administered. Significant attention has been given to manufacturing APVs viamicrofluidics, but existing microfluidic vesicles suffer from short half-lives and are susceptible to rupture due to osmotic changes and the turbulent flow of the lymphatic and cardiovascular systems. Polymer-coated iron-oxide nanoparticles conjugated with pMHCI have shown remarkable therapeutic potential for autoimmune diseases such as type 1 diabetes, but the stiff spherical structure of the nanoparticle scaffold reduces the potential surface area for ideal pMHC:T cell receptor (TCR) interactions; additionally, pMHC complexes are rigidly adhered to the nanoparticle surface, limiting pMHC movement and clustering considered important for the formation of a T cell stimulating immunological synapse. Thus, engineered APVs that would ideally recreate the endogenous form of APVs, while maximizing the concentration of proteins that are critical for immunoregulation, are still in need.SUMMARY

[0006] Disclosed herein include compositions. In some embodiments, the composition comprises: a nucleic acid composition comprising one or more polynucleotides encoding components of an antigen presentation complex (APC). In some embodiments, the components of the APC are capable of assembling into an antigen-presenting vesicle (APV) budded from a cell in which the APC components are expressed. In some embodiments, the APV comprises a plurality of APCs. In some embodiments, the APC comprises an APC- assembly domain, one or more antigen presentation polypeptide(s) and a presenting peptide.

[0007] Disclosed herein include compositions. In some embodiments, the composition comprises: a population of an antigen-presenting vesicles (APVs). In some embodiments, each of the APVs comprises a plurality of antigen presentation complexes (APCs). In some embodiments, the APC comprises an APC-assembly domain, one or more antigen presentation polypeptide(s) and a presenting peptide.

[0008] In some embodiments, the APVs are derived from expression of the nucleic acid composition disclosed herein in a cell. In some embodiments, the APC comprises or consists of components of the APC.

[0009] In some embodiments, the APC comprises all or a portion of a major histocompatibility complex (MHC), or a derivative thereof. In some embodiments, the APC comprises all or a portion of MHC class I (MHC-I) or MHC class II (MHC-II). In some embodiments, the MHC comprises human leukocyte antigen (HLA) and / or mouse MHC. In some embodiments, the antigen presentation polypeptide(s) are selected from MHC-I a chain, beta-2 microglobulin (P2M), MHC-II a chain, MHC-II P chain, a classical HLA Class I molecule, a non-classical HLA Class I molecule, a classical HLA Class II molecule, a non- classical HLA Class II molecule, HLA-A, HLA-B, HLA-C, HLA-E, HLA-F, HLA-G, HLA- DRA, HLA-DRB1, HLA-DRB3, HLA-DRB4, HLA-DRB5, HLA-DQA1, HLA-DQB1, HLA-DPA1, HLA-DPB1, HLA-DMA, HLA-DMB, HLA-DOA, HLA-DOB, derivatives thereof, homologs thereof, or any combination thereof. In some embodiments, the HLA class I is selected from an HLA allele selected from HLA-A*01:01, HLA-A*02:01, HLA-A*02:03, HLA- A*02:06, HLA-A*03:01, HLA-A* 11:01, HLA-A*23:01, HLA-A*24:02, HLA-A*26:01, HLA- A*30:01, HLA-A*30:02, HLA-A*31:01, HLA-A*32:01, HLA-A*33:01, HLA-A*68:01, HLA- A*68:02, HLA-B*07:02, HLA-B*08:01, HLA-B*15:01, HLA-B*35:01, HLA-B*40:01, HLA- B*44:02, HLA-B*44:03, HLA-B*51:01, HLA-B*53:01, HLA-B*57:01, and HLA-B*58:01. In some embodiments, the HLA class II is selected from an HLA allele selected from HLA- DRBl*01:01, HLA-DRBl*15:01, HLA-DRB 1*03:01, HLA-DRB 1*04:01, HLA-DRBl*ll:01, HLA-DRBl*13:01, HLA-DRB 1*07:01, HLA-DRB 1*01:01, HLA-DRB 1*01:02, HLA- DRBl*04:02, HLA-DRB 1*04: 05, HLA-DRB 1*04: 07, HLA-DRB 1*04:08, HLA-DRBl*08:04, HLA-DRB 1*09:01, HLA-DRBl*10:01, HLA-DRB1*11:O2, HLA-DRBl*l l:03, HLA- DRB1*11:O4, HLA-DRB1* 15:02, HLA-DRB1* 15:03, HLA-DRB 1*16:01, HLA-DRB 1*16:02, HLA-DRB3 *02:02, HL A-DRB3 *03:01, HLA-DRB5*01:01, HLA-DQAl*01:01 / DQBl*05:01,HLA-DQAl*05:01 / DQBl*02:01, HLA-DQAl*01:02 / DQBl*05:02, HLA-DQA1 *01 :02 / DQB 1*06:02, HLA-DQAl*03:01 / DQBl*03:02, HLA-DQA1 *01 :02 / DQB 1*06:04, HLA-DQAl*05:01 / DQBl*03:01, HLA-DQAl*02:01 / DQB 1*02:02, HLA-DQA1 *03 :01 / DQB 1*03:01, HLA-DQAl*02:01 / DQB 1*03:03, HLA-DQA1 *03 :03 / DQB 1*03:03, HLA-DPAl*01:03 / DPBl*01:01, HLA-DPAl*01:03 / DPBl*02:01, HLA-DPAl*01:03 / DPBl*03:01, HLA-DPAl*01:03 / DPBl*04:01, HLA-DPA1 *01 :03 / DPB 1*04:02, HLA-DPAl*01:03 / DPBl*05:01, HLA-DPAl*02:01 / DPBl*01:01, HLA-DPAl*02:01 / DPBl*02:01, HLA-DPAl*02:01 / DPBl*03:01, HLA-DPAl*02:01 / DPB 1*04:01, HLA-DPAl*02:01 / DPBl*04:02, HLA-DPAl*02:01 / DPBl*05:01, HLA-DPAl*02:01 / DPBl*06:01, HLA-DPAl*02:01 / DPBl*09:01, HLA-DPAl*02:01 / DPBl*l l:01, HLA-DPAl*02:01 / DPBl*13:01, HLA-DPAl*02:01 / DPBl*14:01, HLA-DPAl*02:01 / DPBl*15:01, and HLA-DPA1*O2:O1 / DPB1*17:OL In some embodiments, at least two components of the APC are derived from different species. In some embodiments, the APC comprises at least one mutation at positions equivalent to Y84 and A139 of HLA-A, optionally Y84A and / or A139C.

[0010] In some embodiments, the antigen presentation polypeptide(s) is capable of forming a binding site that binds the presenting peptide. In some embodiments, the presence of the antigen presentation polypeptide(s) does not induce an immune response in a subject, optionally a subject from which the cell was derived. In some embodiments, the presence of the antigen presentation polypeptide(s) induces an immune response in a subject. In some embodiments, the immune response is induced from a subject from which the cell was derived.In some embodiments, the antigen presentation polypeptide(s) comprises an amino acid sequence having at least 65%, 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% sequence identity to an amino acid sequence selected from SEQ ID NOs: 53-54, 57-58, 61-62, 81-86, 112-113, 120-121, 144-145, and 152-153.

[0011] In some embodiments, the cell is: a cell of a subject; an in vivo cell, an ex vivo cell, or an in situ cell; and / or an adherent cell or a suspension cell. In some embodiments, the cell: is not an immune cell; or is an immune cell.

[0012] In some embodiments, the APC-assembly domain recruits one or more endosomal sorting complex required for transport (ESCRT) proteins to the cytoplasmic tail of the APC. In some embodiments, the recruitment of ESCRT proteins via the APC-assembly domain induces the self-assembly and budding of APV. In some embodiments, the cytoplasmic portion of the APC comprises the APC-assembly domain. In some embodiments, the cytoplasmic tail of the APC comprises the APC-assembly domain. In some embodiments, the APC-assembly domain interacts with the ESCRT proteins TSG101, NEDD4, and / or ALIX. In some embodiments, the APC-assembly domain comprises or is derived from: the ESCRT and ALIX binding region (EABR) of the human CEP55 protein, optionally residues 160-217; a nonhuman protein, optionally a nonmammalian protein, further optionally a chicken protein, a mouse protein, a lizard protein, a reptile protein, a hamster protein, or a goldfish protein; Syntenin-1, rat Galectin-3 (rGalectin-3), Hrs, and / or CD2AP; a viral protein, optionally a fragment of a viral protein, further optionally a retroviral protein, herpes simplex viral protein, vaccinia viral protein, hepadnaviral protein, togaviral protein, flaviviral protein, arenaviral protein, coronaviral protein, orthomyxoviral protein, paramyxoviral protein, bunyaviral protein, bornaviral protein, rhabdoviral protein or filoviral protein, optionally a Gag protein, further optionally derived from EIAV, HTLV-1, MLV, or MPMV, optionally EIAV p9 and / or HIV-1 p6; and / or an Ebola protein, optionally EBOV VP40. In some embodiments, the APC-assembly domain comprises an amino acid sequence having at least 65%, 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% sequence identity to an amino acid sequence of SEQ ID NO: 33.

[0013] In some embodiments, the presenting peptide, or a portion thereof, is displayed on the surface of the APV. In some embodiments, the presenting peptide: is about 1 amino acid to about 10000 amino acids in length, optionally 5-20 amino acids in length, further optionally 5, 6, 7, 8, 9, 10, 11, or 12 amino acids in length; comprises or is derived from an antigenic protein associated with a disease or disorder, optionally an immunogenic variant and / or an immunogenic fragment of said antigenic protein; comprises or is derived from a conserved portion of said antigenic protein; and / or comprises or is derived from at least about 0.001 percent, about 0.01 percent, about 0.05 percent, about 0.1 percent, about 0.2 percent,about 0.4 percent, about 0.6 percent, about 0.8 percent, about 1 percent, about 2 percent, about 3 percent, about 4 percent, or about 5 percent of the full length of said antigenic protein.

[0014] In some embodiments, the disease or disorder is an infectious disease or disorder caused by an infectious agent, the presenting peptide comprises or is derived from an antigenic protein of said infectious agent, and the antigenic protein of said infectious agent is a pathogenic antigen. In some embodiments, the disease or disorder is a disease associated with expression of a tumor-associated antigen, and the antigenic protein is a tumor-associated antigen. In some embodiments, the disease or disorder is a disease associated with expression of a cancer-associated antigen, and the antigenic protein is a cancer-associated antigen. In some embodiments, the disease or disorder is an autoimmune disease or disorder, and the antigenic protein is an autoimmune antigen. In some embodiments, the disease or disorder is a metabolic disorder. In some embodiments, the metabolic disorder is diabetes. In some embodiments, the disease or disorder is an allergic disease or disorder, and the antigenic protein is an allergenic antigen.

[0015] In some embodiments, the infectious agent is: a bacterium, a fungus, a virus, or a protist; and / or a coronavirus (CoV). In some embodiments, the CoV comprises an alphacoronavirus, a betacoronavirus, a gammacoronavirus, or a deltacoronavirus. In some embodiments, the infectious agent is selected from Acinetobacter baumannii, Anaplasma genus, Anaplasma phagocytophilum, Ancylostoma braziliense, Ancylostoma duodenale, Arcanobacterium haemolyticum, Ascaris lumbricoides, Aspergillus genus, Astroviridae, Babesia genus, Bacillus anthracis, Bacillus cereus, Bartonella henselae, BK virus, Blastocystis hominis, Blastomyces dermatitidis, Bordetella pertussis, Borrelia burgdorferi, Borrelia genus, Borrelia spp, Brucella genus, Brugia malayi, Bunyaviridae family, Burkholderia cepacia and other Burkholderia species, Burkholderia mallei, Burkholderia pseudomallei, Caliciviridae family, Campylobacter genus, Candida albicans, Candida spp, Chlamydia trachomatis, Chlamydophila pneumoniae, Chlamydophila psittaci, CJD prion, Clonorchis sinensis, Clostridium botulinum, Clostridium difficile, Clostridium perfringens, Clostridium perfringens, Clostridium spp, Clostridium tetani, Coccidioides spp, coronaviruses, Corynebacterium diphtheriae, Coxiella burnetii, Crimean-Congo hemorrhagic fever virus, Cryptococcus neoformans, Cryptosporidium genus, Cytomegalovirus (CMV), Dengue viruses (DEN-1, DEN-2, DEN-3 and DEN-4), Dientamoeba fragilis, Ebolavirus (EBOV), Echinococcus genus, Ehrlichia chaffeensis, Ehrlichia ewingii, Ehrlichia genus, Entamoeba histolytica, Enterococcus genus, Enterovirus genus, Enteroviruses, mainly Coxsackie A virus and Enterovirus 71 (EV71), Epidermophyton spp, Epstein-Barr Virus (EBV), Escherichia coli O157:H7, Ol l i and 0104 :H4, Fasciola hepatica and Fasciolagigantica, FFI prion, Filarioidea superfamily, Filoviruses, Flaviviruses, Francisella tularensis, Fusobacterium genus, Geotrichum candidum, Giardia intestinalis, Gnathostoma spp, GSS prion, Guanarito virus, Haemophilus ducreyi, Haemophilus influenzae, Helicobacter pylori, Henipavirus (Hendra virus Nipah virus), Hepatitis A Virus, Hepatitis B Virus (HBV), Hepatitis C Virus (HCV), Hepatitis D Virus, Hepatitis E Virus, Herpes simplex virus 1 and 2 (HSV-1 and HSV-2), Histoplasma capsulatum, HIV (Human immunodeficiency virus), Hortaea werneckii, Human bocavirus (HBoV), Human herpesvirus 6 (HHV-6) and Human herpesvirus 7 (HHV-7), Human metapneumovirus (hMPV), Human papillomavirus (HPV), Human parainfluenza viruses (HPIV), Japanese encephalitis virus, JC virus, Junin virus, Kingella kingae, Klebsiella granulomatis, Kuru prion, Lassa virus, Legionella pneumophila, Leishmania genus, Leptospira genus, Listeria monocytogenes, Lymphocytic choriomeningitis virus (LCMV), Machupo virus, Malassezia spp, Marburg virus, Measles virus, Metagonimus yokagawai, Microsporidia phylum, Molluscum contagiosum virus (MCV), Mumps virus, Mycobacterium leprae and Mycobacterium lepromatosis, Mycobacterium tuberculosis, Mycobacterium ulcerans, Mycoplasma pneumoniae, Naegleria fowleri, Necator americanus, Neisseria gonorrhoeae, Neisseria meningitidis, Nocardia asteroides, Nocardia spp, Onchocerca volvulus, Orientia tsutsugamushi, Orthomyxoviridae family (Influenza), Paracoccidioides brasiliensis, Paragonimus spp, Paragonimus westermani, Parvovirus Bl 9, Pasteurella genus, Plasmodium genus, Pneumocystis jirovecii, Poliovirus, Rabies virus, Respiratory syncytial virus (RSV), Rhinovirus, rhinoviruses, Rickettsia akari, Rickettsia genus, Rickettsia prowazekii, Rickettsia rickettsii, Rickettsia typhi, Rift Valley fever virus, Rotavirus, Rubella virus, Sabia virus, Salmonella genus, Sarcoptes scabiei, SARS coronavirus, Schistosoma genus, Shigella genus, Sin Nombre virus, Hantavirus, Sporothrix schenckii, Staphylococcus genus, Staphylococcus genus, Streptococcus agalactiae, Streptococcus pneumoniae, Streptococcus pyogenes, Strongyloides stercoralis, Taenia genus, Taenia solium, Tick-borne encephalitis virus (TBEV), Toxocara canis or Toxocara cati, Toxoplasma gondii, Treponema pallidum, Trichinella spiralis, Trichomonas vaginalis, Trichophyton spp, Trichuris trichiura, Trypanosoma brucei, Trypanosoma cruzi, Ureaplasma urealyticum, Varicella zoster virus (VZV), Variola major or Variola minor, vCJD prion, Venezuelan equine encephalitis virus, Vibrio cholerae, West Nile virus, Western equine encephalitis virus, Wuchereria bancrofti, Yellow fever virus, Yersinia enterocolitica, Yersinia pestis, and Yersinia pseudotuberculosis.

[0016] In some embodiments, the presenting peptide is derived from one or more of MART-1; NYESO1; neuropilin (NRP); IGRP; CD19; CD123; CD22; CD30; CD171; CS-1 (also referred to as CD2 subset 1, CRACC, SLAMF7, CD319, and 19A24); C-type lectin-likemolecule-1 (CLL-1 or CLECL1); CD33; epidermal growth factor receptor variant III (EGFRvIII); ganglioside G2 (GD2); ganglioside GD3 (aNeu5Ac(2-8)aNeu5Ac(2-3)bDGalp(l- 4)bDGlcp(l-l)Cer); TNF receptor family member B cell maturation (BCMA); Tn antigen ((Tn Ag) or (GalNAca-Ser / Thr)); prostate-specific membrane antigen (PSMA); Receptor tyrosine kinase-like orphan receptor 1 (R0R1); Fms-Like Tyrosine Kinase 3 (FLT3); Tumor-associated glycoprotein 72 (TAG72); CD38; CD44v6; Carcinoembryonic antigen (CEA); Epithelial cell adhesion molecule (EPCAM); B7H3 (CD276); KIT (CD117); Interleukin- 13 receptor subunit alpha-2 (IL-13Ra2 or CD213A2); Mesothelin; Interleukin 11 receptor alpha (IL-l lRa); prostate stem cell antigen (PSCA); Protease Serine 21 (Testisin or PRSS21); vascular endothelial growth factor receptor 2 (VEGFR2); Lewis(Y) antigen; CD24; Platelet-derived growth factor receptor beta (PDGFR-beta); Stage-specific embryonic antigen-4 (S SEA-4); CD20; Folate receptor alpha; Receptor tyrosine-protein kinase ERBB2 (Her2 / neu); Mucin 1, cell surface associated (MUC1); epidermal growth factor receptor (EGFR); neural cell adhesion molecule (NCAM); Prostase; prostatic acid phosphatase (PAP); elongation factor 2 mutated (ELF2M); Ephrin B2; fibroblast activation protein alpha (FAP); insulin-like growth factor 1 receptor (IGF -I receptor), carbonic anhydrase IX (CAIX); Proteasome (Prosome, Macropain) Subunit, Beta Type, 9 (LMP2); glycoprotein 100 (gplOO); oncogene fusion protein consisting of breakpoint cluster region (BCR) and Abelson murine leukemia viral oncogene homolog 1 (Abl) (bcr-abl); tyrosinase; ephrin type-A receptor 2 (EphA2); Fucosyl GM1; sialyl Lewis adhesion molecule (sLe); ganglioside GM3 (aNeu5Ac(2-3)bDGalp(l-4)bDGlcp(l-l)Cer); transglutaminase 5 (TGS5); high molecular weight-melanoma-associated antigen (HMWMAA); o-acetyl-GD2 ganglioside (OAcGD2); Folate receptor beta; tumor endothelial marker 1 (TEM1 / CD248); tumor endothelial marker 7-related (TEM7R); claudin 6 (CLDN6); thyroid stimulating hormone receptor (TSHR); G protein-coupled receptor class C group 5, member D (GPRC5D); chromosome X open reading frame 61 (CXORF61); CD97; CD179a; anaplastic lymphoma kinase (ALK); Poly sialic acid; placenta-specific 1 (PLAC1); hexasaccharide portion of globoH glycoceramide (GloboH); mammary gland differentiation antigen (NY-BR-1); uroplakin 2 (UPK2); Hepatitis A virus cellular receptor 1 (HAVCR1); adrenoceptor beta 3 (ADRB3); pannexin 3 (PANX3); G protein-coupled receptor 20 (GPR20); lymphocyte antigen 6 complex, locus K 9 (LY6K); Olfactory receptor 51E2 (OR51E2); TCR Gamma Alternate Reading Frame Protein (TARP); Wilms tumor protein (WT1); Cancer / testis antigen 1 (NY-ESO-1); Cancer / testis antigen 2 (LAGE-la); Melanoma-associated antigen 1 (MAGE-A1); ETS translocation-variant gene 6, located on chromosome 12p (ETV6-AML); sperm protein 17 (SPA17); X Antigen Family, Member 1A (XAGE1); angiopoietin-binding cell surface receptor 2 (Tie 2); melanoma cancer testis antigen-1 (MAD-CT-1); melanoma cancer testis antigen-2(MAD-CT-2); Fos-related antigen 1; tumor protein p53 (p53); p53 mutant; prostein; survivin; telomerase; prostate carcinoma tumor antigen- 1 (PCTA-1 or Galectin 8), melanoma antigen recognized by T cells 1 (MelanA or MARTI); Rat sarcoma (Ras) mutant; human Telomerase reverse transcriptase (hTERT); sarcoma translocation breakpoints; melanoma inhibitor of apoptosis (ML-IAP); ERG (transmembrane protease, serine 2 (TMPRSS2) ETS fusion gene); N- Acetyl glucosaminyl-transferase V (NA17); paired box protein Pax-3 (PAX3); Androgen receptor; Cyclin Bl; v-myc avian myelocytomatosis viral oncogene neuroblastoma derived homolog (MYCN); Ras Homolog Family Member C (RhoC); Tyrosinase-related protein 2 (TRP-2); Cytochrome P450 1B1 (CYP1B1); CCCTC-Binding Factor (Zinc Finger Protein)-Like (BORIS or Brother of the Regulator of Imprinted Sites), Squamous Cell Carcinoma Antigen Recognized By T Cells 3 (SART3); Paired box protein Pax-5 (PAX5); proacrosin binding protein sp32 (OY-TES1); lymphocyte-specific protein tyrosine kinase (LCK); A kinase anchor protein 4 (AKAP-4); synovial sarcoma, X breakpoint 2 (SSX2); Receptor for Advanced Glycation Endproducts (RAGE-1); renal ubiquitous 1 (RU1); renal ubiquitous 2 (RU2); legumain; human papilloma virus E6 (HPV E6); human papilloma virus E7 (HPV E7); intestinal carboxyl esterase; heat shock protein 70-2 mutated (mut hsp70-2); CD79a; CD79b; CD72; Leukocyte-associated immunoglobulin-like receptor 1 (LAIR1); Fc fragment of IgA receptor (FCAR or CD89); Leukocyte immunoglobulin-like receptor subfamily A member 2 (LILRA2); CD300 molecule-like family member f (CD300LF); C-type lectin domain family 12 member A (CLEC12A); bone marrow stromal cell antigen 2 (BST2); EGF-like module-containing mucinlike hormone receptor-like 2 (EMR2); lymphocyte antigen 75 (LY75); Glypican-3 (GPC3); Fc receptor-like 5 (FCRL5); and immunoglobulin lambda-like polypeptide 1 (IGLL1).

[0017] In some embodiments, the APC comprises one or more linker(s). In some embodiments, the one or more linker(s): comprise one or more flexible amino acid residue(s), optionally about 1 to about 50 flexible amino acid residues, further optionally the flexible amino acid residues comprise glycine, serine, or a combination thereof; is a glycine-serine (GS) linker, optionally 1-25 amino acids in length; and / or is situated between the APC-assembly domain and the presenting peptide, between the APC-assembly domain and the antigen presentation polypeptide, between the antigen presentation polypeptide and the presenting peptide, and / or between two of the one or more antigen presentation polypeptides. In some embodiments, the linker comprises an amino acid sequence selected from GSGSGSG (SEQ ID NO: 1), GGGGS (SEQ ID NO: 2), GSGSG (SEQ ID NO: 3), GGGG (SEQ ID NO: 4), GGG, GG, GS, GSGS (SEQ ID NO: 8), GGGS (SEQ ID NO: 9), GGS, GTS, GGSGGS (SEQ ID NO: 12), GGG, GGGGGG (SEQ ID NO: 14), GGGGGGGGG (SEQ ID NO: 15), GGGGGGGGGGGG (SEQ ID NO: 16), GGGGGGGGGGGGGGG (SEQ ID NO: 17), GGS, GGSGGS (SEQ ID NO: 19),GGSGGSGGS (SEQ ID NO: 20), GGSGGSGGSGGS (SEQ ID NO: 21), GGSGGSGGSGGSGGS (SEQ ID NO: 22), GSG, GSGGSG (SEQ ID NO: 24), GSGGSGGSG (SEQ ID NO: 25), GSGGSGGSGGSG (SEQ ID NO: 26), GSGGSGGSGGSGGSG (SEQ ID NO: 27), (GGGGS)n (SEQ ID NO: 28), GGGGSGGGGS (SEQ ID NO: 29), GGGGSGGGGSGGGGS (SEQ ID NO: 30), GGGGSGGGGSGGGGSGGGGS (SEQ ID NO: 31), and GGGGSGGGGS GGGGSGGGGSGGGGS (SEQ ID NO: 32). In some embodiments, the linker comprises an amino acid sequence of GGGGS (SEQ ID NO: 2) or GGGS (SEQ ID NO: 9). In some embodiments, the linker comprises n GGGGS (SEQ ID NO: 2) or GGGS (SEQ ID NO: 9), and n is an integer from 1 to 10, optionally n is 3 or 4.

[0018] In some embodiments, the APC comprises a single fusion protein. In some embodiments, the single fusion protein comprises one or more linker(s), the presenting peptide, the antigen presentation polypeptide(s), and the APC-assembly domain. In some embodiments, the antigen presentation polypeptide(s) is covalently connected to the APC-assembly domain and the presenting peptide. In some embodiments, the antigen presentation polypeptide(s) is situated between the APC-assembly domain and the presenting peptide. In some embodiments, at least one of the antigen presentation polypeptide(s) is situated between the APC-assembly domain and the presenting peptide. In some embodiments, the antigen presentation polypeptide(s) comprise two or more antigen presentation polypeptides with the presenting peptide situated between said two or more antigen presentation polypeptides. In some embodiments, the antigen presentation polypeptide(s) comprise MHC-I a chain and beta-2 microglobulin (P2M). In some embodiments, the components of the APC are connected in the order from N-terminus to C-terminus: the presenting peptide, beta-2 microglobulin (P2M), MHC-I a chain and the APC-assembly domain; or the APC-assembly domain, MHC-I a chain, beta-2 microglobulin (P2M) and the presenting peptide. In some embodiments, the antigen presentation polypeptide(s) comprise MHC-II a chain and MHC-II P chain. In some embodiments, the components of the APC are connected in the order from N-terminus to C- terminus: the APC-assembly domain, MHC-II P chain, the presenting peptide and the MHC-II a chain; the APC-assembly domain, MHC-II a chain, the presenting peptide and the MHC-II P chain; the MHC-II a chain, the presenting peptide, MHC-II P chain and the APC-assembly domain; or the MHC-II P chain, the presenting peptide, MHC-II a chain and the APC-assembly domain.

[0019] In some embodiments, the APC comprises two or more separate polypeptides. In some embodiments, the APC comprises two separate polypeptides. In some embodiments, at least two of the two or more separate polypeptides comprise an APC-assembly domain. In some embodiments, at least one of the two or more separate polypeptides is a fusionprotein. In some embodiments, the fusion protein comprises one or more linker(s), the antigen presentation polypeptide(s), and the APC-assembly domain. In some embodiments, the fusion protein comprises (i) a linker, a first antigen presentation polypeptide, and the APC-assembly domain; or (ii) a linker, a second antigen presentation polypeptide, and the presenting peptide. In some embodiments, the first antigen presentation polypeptide is covalently connected to the APC-assembly domain, and the second antigen presentation polypeptide is covalently connected to the presenting peptide, optionally via a peptide bond. In some embodiments, the first antigen presentation polypeptide is capable of binding to the second antigen presentation polypeptide. In some embodiments, the first antigen presentation polypeptide comprises MHC-I a chain and the second antigen presentation polypeptide comprises beta-2 microglobulin (P2M). In some embodiments, the first antigen presentation polypeptide comprises beta-2 microglobulin (P2M) and the second antigen presentation polypeptide comprises MHC-I a chain. In some embodiments, the first antigen presentation polypeptide comprises MHC-II a chain and the second antigen presentation polypeptide comprises MHC-II P chain. In some embodiments, the first antigen presentation polypeptide comprises MHC-II P chain and the second antigen presentation polypeptide comprises MHC-II a chain. In some embodiments, MHC-I a chain is capable of forming a binding site that binds the presenting peptide. In some embodiments, MHC-II a chain and the MHC-II P chain are capable of forming a binding site that binds the presenting peptide.

[0020] In some embodiments, the APC comprises an amino acid sequence having at least 65%, 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% sequence identity to an amino acid sequence selected from SEQ ID NOs: 37-52, 55-56, 59-60, 63-80, 114-119, 122-143, 146-151, and 154-159.

[0021] In some embodiments, the APVs comprise one or more supplemental polypeptide(s) (e.g., immunosuppressive polypeptide(s), immunostimulatory polypeptide(s), costimulatory polypeptide(s), cell adhesion polypeptide(s), anti-phagocytic polypeptide(s), tissue-homing polypeptide(s), or any combination thereof). In some embodiments, the supplemental polypeptide(s) are selected from CD3s, CD3(^, CD4, CD5, CD8a, CD9, CD16, CD22, CD27, CD28, CD33, CD37, CD45, CD64, CD80, CD86, CD 134, CD137, CD152, CD 154, PD1, CARD11, CD2, CD7, CD27, CD28, CD30, CD40, CD54 (ICAM), CD3, CD3y, CD35, CD25, CD39, GITR, LRRC32, Neuropilin-1, CCR6, CD83, CD134 (0X40), CD137 (4- 1BB), CD150 (SLAMF1), CD152 (CTLA4), CD223 (LAG3), CD270 (HVEM), CD273 (PD- L2), CD274 (PD-L1), CD278 (ICOS), DAP10, LAT, NKD2C SLP76, TRIM, ZAP70, CD73, LFA-1, CD47, CCR7, derivatives thereof, or any combination thereof. In some embodiments, the supplemental polypeptide(s) is: (i) associated with an APC-assembly domain; and / or (ii) notassociated with an APC-assembly domain. In some embodiments, the nucleic acid composition comprises one or more second polynucleotide(s) encoding the one or more supplemental polypeptide(s).

[0022] In some embodiments, the APVs comprise a lipid bilayer. In some embodiments, the APVs comprise a lipid bilayer derived from the cell from which the APVs was budded.

[0023] In some embodiments, at least two of the APCs of the plurality of APCs are different from each other with respect to the presenting peptide, and the population of APVs thereby display a plurality of disparate presenting peptides. In some embodiments, the population of APVs comprise: one or more homotypic APVs, wherein the plurality of APCs of a homotypic APV are the same as each other with respect to the presenting peptide, and wherein a homotypic APV thereby does not display a plurality of disparate presenting peptides; one or more heterotypic APVs, wherein at least two of the APCs of a heterotypic APV are different from each other with respect to the presenting peptide, and wherein a heterotypic APV thereby displays a plurality of disparate presenting peptides; a mixture of two or more homotypic APVs that differ from each other with respect to the presenting peptide of the plurality of APCs present in said two or more homotypic APVs, and wherein the population of APVs thereby displays a plurality of disparate presenting peptides; a mixture of two or more heterotypic APVs that differ from each other with respect to the presenting peptide of the plurality of APCs of said two or more heterotypic APVs; and / or a mixture of one or more homotypic APVs and one or more heterotypic APVs, and wherein the population of APVs thereby displays a plurality of disparate presenting peptides. In some embodiments, the plurality of disparate presenting peptides comprises: between about 2 and about 500 antigenic peptides that differ from each other; presenting peptide of a same protein type; and / or presenting peptide of different protein types.

[0024] In some embodiments, less than about 10% of the APVs of the population of APVs have a particle size smaller than about 30 nm; less than about 10% of the APVs of the population of APVs have a particle size exceeding about 100 nm; the average diameter of the APVs of the population of APVs range from about 30 nm to about 250 nm, from about 50 nm to about 125 nm, or from about 60 nm to about 80 nm; and / orthe average diameter of the APVs of the population of APVs is about 50 nm, about 52 nm, about 54 nm, about 56 nm, about 58 nm, about 60 nm, about 62 nm, about 64 nm, about 66 nm, about 68 nm, 70 nm, about 72 nm, about 74 nm, about 76 nm, about 78 nm, about 80 nm, about 82 nm, about 84 nm, about 86 nm, about 88 nm, or about 90 nm. In some embodiments, the average is the mean, median or mode. In some embodiments, the mean is the arithmetic mean, geometric mean, and / or harmonic mean. In some embodiments, the APVs: have a minimum diameter of about 10 nm, about 12 nm, about14 nm, about 16 nm, about 18 nm, about 20 nm, about 22 nm, about 24 nm, about 26 nm, about 28 nm, about 30 nm, about 32 nm, about 34 nm, about 36 nm, about 38 nm, about 40 nm, about 42 nm, about 44 nm, about 46 nm, about 48 nm, or about 50 nm; and / or have a maximum diameter of about 250 nm, about 252 nm, about 254 nm, about 256 nm, about 258 nm, about 260 nm, about 262 nm, about 264 nm, about 266 nm, about 268 nm, about 270 nm, about 272 nm, about 274 nm, about 276 nm, about 278 nm, or about 280 nm.

[0025] In some embodiments, the APV and / or the APC is capable of inducing immunogenic responses against the presenting peptide in a subject without the administration of exogenous antigen presenting cells and / or exogenous antigen presenting components other than the APV and / or the APC.

[0026] In some embodiments, the nucleic acid composition is complexed or associated with one or more lipids or lipid-based carriers, thereby forming liposomes, lipid nanoparticles (LNPs), lipoplexes, and / or nanoliposomes, optionally encapsulating the nucleic acid composition. In some embodiments, the nucleic acid composition is, comprises, or further comprises, one or more vectors. In some embodiments, at least one of the one or more vectors is a viral vector, a plasmid, a transposable element, a naked DNA vector, a lipid nanoparticle (LNP), or any combination thereof. In some embodiments, the viral vector is an AAV vector, a lentivirus vector, a retrovirus vector, an adenovirus vector, a herpesvirus vector, a herpes simplex virus vector, a cytomegalovirus vector, a vaccinia virus vector, a MVA vector, a baculovirus vector, a vesicular stomatitis virus vector, a human papillomavirus vector, an avipox virus vector, a Sindbis virus vector, a VEE vector, a Measles virus vector, an influenza virus vector, a hepatitis B virus vector, an integration-deficient lentivirus (IDLV) vector, or any combination thereof. In some embodiments, the transposable element is piggybac transposon or sleeping beauty transposon. In some embodiments, the polynucleotide(s) encoding components of the APC are comprised in the one or more vectors. In some embodiments, the polynucleotide(s) encoding components of the APC are comprised in the same vector and / or different vectors. In some embodiments, the polynucleotide(s) encoding components of the APC are situated on the same nucleic acid and / or different nucleic acids. In some embodiments, the one or more vectors is a DNA vaccine.

[0027] In some embodiments, the polynucleotide(s) encoding components of the APC are operably linked to one or more promoters capable of inducing transcription of said polynucleotide(s). In some embodiments, the DNA vaccine is a plasmid-based DNA vaccine, a minicircle-based DNA vaccine, a bacmid-based DNA vaccine, a minigene-based DNA vaccine, a ministring DNA (linear covalently closed DNA vector) vaccine, a closed-ended linear duplex DNA (CELiD or ceDNA) vaccine, a doggybone™ DNA vaccine, a dumbbell shaped DNAvaccine, or a minimalistic immunological-defined gene expression (MIDGE)-vector DNA vaccine. In some embodiments, the promoter comprises a ubiquitous promoter, an inducible promoter, a tissue-specific promoter and / or a lineage-specific promoter. In some embodiments, the ubiquitous promoter is selected from a cytomegalovirus (CMV) immediate early promoter, a CMV promoter, a viral simian virus 40 (SV40) (e.g., early or late), a Moloney murine leukemia virus (MoMLV) LTR promoter, a Rous sarcoma virus (RSV) LTR, an RSV promoter, a herpes simplex virus (HSV) (thymidine kinase) promoter, H5, P7.5, and Pl l promoters from vaccinia virus, an elongation factor 1-alpha (EFla) promoter, early growth response 1 (EGR1), ferritin H (FerH), ferritin L (FerL), Glyceraldehyde 3-phosphate dehydrogenase (GAPDH), eukaryotic translation initiation factor 4A1 (EIF4A1), heat shock 70 kDa protein 5 (HSPA5), heat shock protein 90 kDa beta, member 1 (HSP90B1), heat shock protein 70 kDa (HSP70), P-kinesin (P- KIN), the human ROSA 26 locus, a Ubiquitin C promoter (UBC), a phosphoglycerate kinase- 1 (PGK) promoter, 3 -phosphoglycerate kinase promoter, a cytomegalovirus enhancer, human P- actin (HBA) promoter, chicken P-actin (CBA) promoter, a CAG promoter, a CASI promoter, a CBH promoter, or any combination thereof. In some embodiments, the polynucleotide(s) encoding components of the APC are operably linked to a tandem gene expression element. In some embodiments, the tandem gene expression element is an internal ribosomal entry site (IRES), foot-and-mouth disease virus 2A peptide (F2A), equine rhinitis A virus 2A peptide (E2A), porcine teschovirus 2A peptide (P2A) or Thosea asigna virus 2A peptide (T2A), or any combination thereof.

[0028] In some embodiments, the polynucleotide(s) encoding components of the APC comprises a transcript stabilization element. In some embodiments, the transcript stabilization element comprises woodchuck hepatitis post-translational regulatory element (WPRE), bovine growth hormone polyadenylation (bGH-polyA) signal sequence, human growth hormone polyadenylation (hGH-polyA) signal sequence, or any combination thereof.

[0029] In some embodiments, the one or more polynucleotides comprise the nucleotide sequence of any one of SEQ ID NOs: 90-111 and 160-183 or a sequence that is at least 80%, 85%, 90%, 95%, 98%, 99%, or 100% identical to any one of SEQ ID NOs: 90-111 and 160-183.

[0030] In some embodiments, the nucleic acid composition is or comprises mRNA. In some embodiments, the mRNA is formulated in a lipid nanoparticle (LNP). In some embodiments, the mRNA comprises: a 5' untranslated region (UTR), a 3' UTR, and / or a cap; one or more modified nucleotides selected from pseudouridine, N-l-methyl-pseudouridine, 2- aminoadenosine, 2-thiothymidine, inosine, pyrrolo-pyrimidine, 3-methyl adenosine, 5- methylcytidine, C-5 propynyl-cytidine, C-5 propynyl-uridine, 2-aminoadenosine, C5-bromouridine, C5-fluorouridine, C5-iodouridine, C5-propynyl-uridine, C5-propynyl-cytidine, C5-methylcytidine, 2-aminoadenosine, 7-deazaadenosine, 7-deazaguanosine, 8-oxoadenosine, 8- oxoguanosine, 0(6)-methylguanine, and 2-thiocytidine; and / or a modified nucleotide in place of one or more uridines. In some embodiments, the modified nucleoside is selected from pseudouridine (y), N 1-methyl-pseudouridine (m IT), and 5-methyl-uridine (m5U).

[0031] In some embodiments, the LNP comprises: one or more of an ionizable cationic lipid, a non-cationic lipid, a sterol, and a PEG-modified lipid, optionally the noncationic lipid is a neutral lipid; 0.5-15 mol% PEG-modified lipid, 5-25 mol% non-cationic lipid, 25-55 mol% sterol, and 20-60 mol% ionizable cationic lipid; and / or 40-55 mol% ionizable cationic lipid, 5-15 mol% neutral lipid, 35-45 mol% sterol, and 1-5 mol% PEG-modified lipid. In some embodiments, the LNP comprises: 47 mol% ionizable cationic lipid, 11.5 mol% neutral lipid, 38.5 mol% sterol, and 3.0 mol% PEG-modified lipid; 48 mol% ionizable cationic lipid, 11 mol% neutral lipid, 38.5 mol% sterol, and 2.5 mol% PEG-modified lipid; 49 mol% ionizable cationic lipid, 10.5 mol% neutral lipid, 38.5 mol% sterol, and 2.0 mol% PEG-modified lipid; 50 mol% ionizable cationic lipid, 10 mol% neutral lipid, 38.5 mol% sterol, and 1.5 mol% PEG- modified lipid; or 51 mol% ionizable cationic lipid, 9.5 mol% neutral lipid, 38.5 mol% sterol, and 1.0 mol% PEG-modified lipid. In some embodiments, the ionizable cationic lipid is heptadecan-9-yl 8 ((2 hydroxyethyl)(6 oxo 6-(undecyloxy)hexyl)amino)octanoate; the neutral lipid is 1,2 distearoyl sn glycero-3 phosphocholine (DSPC); the sterol is cholesterol; and / or the PEG-modified lipid is l-monomethoxypolyethyleneglycol-2,3-dimyristylglycerol with polyethylene glycol of average molecular weight 2000 (PEG2000 DMG). In some embodiments, the wt / wt ratio of lipid to mRNA is from about 1 : 100 to about 100: 1. In some embodiments, the composition is a lyophilized composition. In some embodiments, the lyophilized composition has a water content of less than about 10%.

[0032] In some embodiments, the composition is formulated or is to be formulated: as a liquid, a solid, or a combination thereof; for infusion; for injection; for intramuscular administration, intranasal administration, transdermal administration, aerosol delivery, nasal delivery, vaginal delivery, rectal delivery, buccal delivery, ocular delivery, local delivery, topical delivery, intraci sternal delivery, intraperitoneal delivery, oral delivery, intramuscular injection, intravenous injection, subcutaneous injection, intranodal injection, intratumoral injection, intraperitoneal injection, intradermal injection; and / or as particles. In some embodiments, the particles are iron oxide particles, liposomes, micelles, polymer complexes, cationic peptide nanoemulsions, virus-like particles (VLPs), lipid nanoparticles (LNP) and / or lipoplex (LPX) particles.

[0033] In some embodiments, the nucleic acid composition and the LNP-formingcomponents are in separate vials. In some embodiments, the composition is a pharmaceutical composition. In some embodiments, the pharmaceutical composition further comprises one or more pharmaceutically acceptable carriers, diluents and / or excipients.

[0034] The composition can further comprises instructions for use of the composition for: stimulating an immune response in a subject in need thereof; treating or preventing a disease or disorder in a subject in need thereof; and / or treating or preventing a cancer or an autoimmune disorder in a subject in need thereof.

[0035] Disclosed herein include kits. In some embodiments, the kit comprises the composition disclosed herein. Disclosed herein include cells. In some embodiments, the cell comprises the nucleic acid composition disclosed herein.

[0036] Disclosed herein include methods of stimulating an immune response in a subject in need thereof. In some embodiments, the method comprises: administering to the subject a therapeutically effective amount of the composition or the cell disclosed herein, thereby stimulating an immune response in the subject.

[0037] Disclosed herein include methods of treating or preventing a disease or disorder in a subject in need thereof. In some embodiments, the method comprises: administering to the subject a therapeutically effective amount of the composition or the cell disclosed herein, thereby treating or preventing the disease or disorder in the subject. In some embodiments, the disease or disorder is a cancer or an autoimmune disorder. Disclosed herein include methods for treating or preventing a cancer or an autoimmune disorder in a subject in need thereof. In some embodiments, the method comprises: administering to the subject a therapeutically effective amount of the composition or the cell disclosed herein, thereby treating or preventing a cancer or the autoimmune disorder in the subject.

[0038] In some embodiments, immunogenic levels of the APC and / or APV are produced in serum of the subject at about 1 hour to about 6 months post administration of the composition. In some embodiments, a cytokine is released in the serum of the subject at about 1 hour to about 6 months post administration of the composition. In some embodiments, the cytokine is IFN-y. In some embodiments, T cells are activated in the subject at about 1 hour to about 6 months post administration of the composition; and / or T cells are induced to change from one type of T cell to another type of T cell, optionally the regulatory T cell type, in the subject at about 1 hour to about 6 months post administration of the composition.

[0039] In some embodiments, the method comprises administering to the subject at least two doses of the composition. In some embodiments, the second dose of the composition is administered to the subject at least 7 days after a first dose of the composition is administered to the subject; the method comprises administering to the subject at least 3, 4, 5, 6, 7, 8, 9, 10, 12,15, 20, or 25, doses of the composition; and / or the method comprises administering a dose of the composion to the subject on a periodic basis, optionally at least once every hour, every two hours, every four hours, every six hours, every eight hours, every ten hours, every 12 hours, every 16 hours, every 24 hours, every 36 hours, every 48 hours, every 72 hours, every 96 hours, every 5 days, every week, every 2 weeks, every 3 weeks, every 4 weeks, every 5 weeks, every 6 weeks, every 8 weeks, every 10 weeks, every 12 weeks, every 15 weeks, every 20 weeks, every 25 weeks, every 30 weeks, every 40 weeks, every year, every 2 years, or every 3 years.

[0040] In some embodiments, the composition elicits an at least 10% higher T cell activation and / or cytokine release as compared to an approach comprising administration of a soluble version of the presenting peptide; or the composition elicits an at least 10% lower T cell activation and / or cytokine release as compared to an approach comprising administration of a soluble version of the presenting peptide. In some embodiments, administration of the composition elicits protective and long-lasting immunity against the disease or disorder associated with the presenting peptide thereof; or administration of the composition elicits protective and long-lasting immunosuppression, optionally associated with the presenting peptide.

[0041] In some embodiments, an at least as low dose of the composition is needed to generate a comparable immune response as compared to an approach comprising administration of a soluble version of the presenting peptide; or an at least as low dose of the composition is needed to generate a comparable immunosuppression as compared to an approach comprising administration of a soluble version of the presenting peptide. In some embodiments, following administration of the composition, the composition induces an at least as potent T cell activation and / or cytokine release against the presenting peptide or variants thereof as compared to an approach comprising administration of a soluble version of the presenting peptide, optionally the composition comprises a population of APVs; or the composition induces an at least as potent immunosuppression, optionally against the presenting peptide or variants thereof, as compared to an approach comprising administration of a soluble version of the presenting peptide, optionally the composition comprises a population of APVs.

[0042] In some embodiments, the subject: is a human subject; is a newborn or infant of an age of not more than 3 years, of not more than 2 years, of not more than 1.5 years, of not more than 1 year (12 months), of not more than 9 months, 6 months or 3 months, or is between 6 months and 2 years; is immunocompromised, has a pulmonary disease, and / or is 65 years of age or older; has a cancer, optionally melanoma, ovarian cancer, esophageal cancer, lung cancer, hepatocellular cancer, prostate cancer, or breast cancer; and / or has an underlying comorbid condition, optionally selected from heart disease, diabetes, and lung disease.

[0043] In some embodiments, the composition is administered in an effective amount to: elicit a robust CD4 and / or CD8 T cell response against the presenting peptide in the subject; and / or elicit a cytokine release against the presenting peptide in the subject, optionally IFN-y release. In some embodiments, the composition is: (i) co-administered with an adjuvant; or (ii) not co-administered with an adjuvant.

[0044] In some embodiments, the disease or disorder is a blood disease, an immune disease, a neurological disease or disorder, a cancer, an infectious disease, a genetic disease, a disorder caused by aberrant mtDNA, a metabolic disease, a disorder caused by aberrant cell cycle, a disorder caused by aberrant angiogenesis, a disorder cause by aberrant DNA damage repair, or any combination thereof, optionally a solid tumor. In some embodiments, the disease is associated with expression of a tumor-associated antigen. In some embodiments, the disease associated with expression of a tumor antigen-associated is selected from a proliferative disease, a precancerous condition, a cancer, and a non-cancer related indication associated with expression of the tumor antigen; the cancer is selected from colon cancer, rectal cancer, renalcell carcinoma, liver cancer, non-small cell carcinoma of the lung, cancer of the small intestine, cancer of the esophagus, melanoma, bone cancer, pancreatic cancer, skin cancer, cancer of the head or neck, cutaneous or intraocular malignant melanoma, uterine cancer, ovarian cancer, rectal cancer, cancer of the anal region, stomach cancer, testicular cancer, uterine cancer, carcinoma of the fallopian tubes, carcinoma of the endometrium, carcinoma of the cervix, carcinoma of the vagina, carcinoma of the vulva, Hodgkin's Disease, non-Hodgkin lymphoma, cancer of the endocrine system, cancer of the thyroid gland, cancer of the parathyroid gland, cancer of the adrenal gland, sarcoma of soft tissue, cancer of the urethra, cancer of the penis, solid tumors of childhood, cancer of the bladder, cancer of the kidney or ureter, carcinoma of the renal pelvis, neoplasm of the central nervous system (CNS), primary CNS lymphoma, tumor angiogenesis, spinal axis tumor, brain stem glioma, pituitary adenoma, Kaposi's sarcoma, epidermoid cancer, squamous cell cancer, T-cell lymphoma, environmentally induced cancers, combinations of said cancers, and metastatic lesions of said cancers; and / or the cancer is a hematologic cancer chosen from one or more of chronic lymphocytic leukemia (CLL), acute leukemias, acute lymphoid leukemia (ALL), B-cell acute lymphoid leukemia (B-ALL), T-cell acute lymphoid leukemia (T-ALL), chronic myelogenous leukemia (CML), B cell prolymphocytic leukemia, blastic plasmacytoid dendritic cell neoplasm, Burkitt's lymphoma, diffuse large B cell lymphoma, follicular lymphoma, hairy cell leukemia, small cell- or a large cell-follicular lymphoma, malignant lymphoproliferative conditions, MALT lymphoma, mantle cell lymphoma, marginal zone lymphoma, multiple myeloma, myelodysplasia and myelodysplastic syndrome, non-Hodgkin's lymphoma, Hodgkin's lymphoma, plasmablasticlymphoma, plasmacytoid dendritic cell neoplasm, Waldenstrom macroglobulinemia, or preleukemia.

[0045] In some embodiments, administering comprises aerosol delivery, nasal delivery, vaginal delivery, rectal delivery, buccal delivery, ocular delivery, local delivery, topical delivery, intraci sternal delivery, intraperitoneal delivery, oral delivery, intramuscular injection, intravenous injection, infusion, subcutaneous injection, intranodal injection, intratumoral injection, intraperitoneal injection, intradermal injection, or any combination thereof. In some embodiments, the composition is administered intramuscularly. In some embodiments, the composition is administered into a deltoid region of an arm.

[0046] Disclosed herein include methods of modulating an immune cell. In some embodiments, the method comprises: contacting the immune cell with the composition disclosed herein. In some embodiments, modulating comprising activating, regulating, stimulating, and / or suppressing. Disclosed herein include method of isolating an immune cell of interest. In some embodiments, the method comprises: contacting a population of cells suspected of comprising of an immune cell of interest with the composition disclosed herein.

[0047] In some embodiments, the contacting step is performed in vitro. In some embodiments, the contacting step is performed in a compartment loaded with the composition disclosed herein, optionally a nanovial. In some embodiments, the contacting step is performed in a cavity of a particle, optionally a nanovial. In some embodiments, the particle comprises at least one opening. In some embodiments, the particle comprises a single opening. In some embodiments, the particle is composed of hydrogel. In some embodiments, a longest dimensional length of the particle is less than about 100 micrometers.

[0048] In some embodiments, the APVs are disposed on the surface of the cavity. In some embodiments, the APVs are disposed on the surface of the cavity through a binding moiety. In some embodiments, the binding moiety comprises an antibody or fragment thereof capable of specifically binding the APV. In some embodiments, the binding moiety comprises an antibody or fragment thereof capable of specifically binding to one or more selected from CD274, CD83, CD80, CD54, MHC, the presenting peptide, the APC-assembly domain, and a fragment thereof. In some embodiments, one or more capture agent(s) are disposed on the surface of the cavity. In some embodiments, the capture agent(s) comprise an antibody or fragment thereof capable of specifically binding to a cytokine. In some embodiments, the capture agent(s) comprise an antibody or fragment thereof capable of specifically binding to one or more selected from IL-2, TNF-a, IFN- y, and fragments thereof. In some embodiments, the immune cell comprises a B cell, a plasmablast, a plasma cell, a T cell, or an NK cell.

[0049] The method can further comprise isolating immune cell(s) of interest. In someembodiments, activation of the immune cell is at least about 1.1 -fold higher as compared to a method of activating the immune cell using the antigen presentation polypeptide and the presenting peptide without forming the APV. In some embodiments, level of cytokine secretion is at least about 1.1 -fold higher as compared to a method of activating the immune cell using the antigen presentation polypeptide(s) and the presenting peptide without forming the APV. In some embodiments, the cytokine is IFN- y. In some embodiments, the presence of the supplemental polypeptide(s) increases the activation of the immune cell and / or the level of cytokine secretion by at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80% or 90%.BRIEF DESCRIPTION OF THE DRAWINGS

[0050] FIG. 1 A-FIG. IF show that EABR addition to the cytoplasmic tail of SCT pMHCI promotes APV budding and release. FIG. 1A shows a schematic of membrane-bound SCT pMHCI proteins on a cell surface containing cytoplasmic tail EABR additions that induced budding of an APV comprising a lipid bilayer with embedded SCT pMHCI proteins. FIG. IB shows a SCT pMHCIZEABR construct. The top panel of FIG. IB shows that the SCT pMHCI protein is composed of a peptide fused to a 3*(Gly4Ser) linker (SEQ ID NO: 30), P2M, a 4*(Gly4Ser) linker (SEQ ID NO: 31), HLA-A*02:01 alpha chain, a GlysSer spacer (SEQ ID NO: 9), and an EABR sequence. The bottom panel of FIG. IB shows the EABR sequence. FIG. 1C displays a schematic showing production and purification of APVs. FIG. ID shows a chromatogram representative of the typical yield of SCT pMHCI APVs from a 100 mL transfection of Expi293F cells. Inset highlights void volume peak. FIG. IE shows the Western blot analysis detecting SCT pMHCI protein from APVs purified by ultracentrifugation on a 20% sucrose cushion from transfected HEK293T cell culture supernatants. Cells were transfected with SCT MART1 / D1, SCT MARTI / DI / EABR, SCT MART1 / D9, SCT MART1 / D9 / EABR, and SARS-CoV-2 spike(S) / EPM / EABR (S / EPM / EABR) constructs. Rabbit anti-HLA-A primary antibody and Alexa488-conjugated anti-rabbit secondary antibody were used to detect SCT pMHCI protein. FIG. IF shows immuno-EM images of SCT MART1 / D1ZEABR APVs purified from transfected Expi293F cell culture supernatants by ultracentrifugation and SEC. Primary rabbit anti-HLA-A antibody identical to primary antibody used in FIG. IE. Secondary 6 nm gold-conjugated anti-rabbit antibody appears as black punctate in image. Left: representative APVs are highlighted in boxes. Scale bar, 100 nm. Right: close up of black-boxed APV. Scale bar, 20 nm.

[0051] FIG. 2 A-FIG. 2G shows that EABR addition to SCT pMHCI promoted budding of the complete, intended pMHCI complex on APVs. FIG. 2 A shows indirect ELISA of APVs purified by ultracentrifugation from transfected HEK293T cells with a primary rabbit anti-HLA-A antibody and secondary HRP-conjugated anti-rabbit antibody. Cells weretransfected with SCT NYESO1 / D1, SCT NYESO1 / D1 / EABR, SCT NYESO1 / D9, SCT NYESO1 / D9 / EABR, SCT MART 1 / D 1, and SCT MART 1 / D 1 / EABR constructs (2 replicates per dilution). FIG. 2B shows sandwich ELISA of APVs purified by ultracentrifugation from transfected HEK293T cells using anti-NYES01 :HLA-A*02:01 (3M4E5) for capture, biotinylated 3M4E5 for detection, and HRP-conjugated streptavidin secondary. Cells were transfected with SCT NYESO1 / D9 / EABR, SCD D9 / EABR and NYESO1 peptide (SCD / EABR + NYESO1)), HC D9 / EABR and NYESO1 / P2M (HC / EABR + NYESO1 / P2M), SCT NYESO1 / D9 (SCT), SCD D9 and NYESO1 peptide (SCD + NYESO1), HC D9 and NYESO1 / P2M (HC + NYESO1 / P2M) constructs (2 replicates per dilution). FIG. 2C shows dynamic light scattering measurement of SCT MART1 / D1 and SCT MART1 / D1ZEABR APVs represented as a probability mass function of the expected diameter values for each sample. Points are connected by a simple interpolating spline. FIG. 2D displays a schematic showing full SCT pMHCIZEABR construct (SCTZEABR) and various alternative constructs used for the ELISA in FIG. 2B: NYESO1 / P2M, HC, and SCD. FIG. 2E-FIG. 2G show immuno-EM micrographs of different EABR vesicles purified from transfected Expi293F cell culture supernatants by ultracentrifugation and SEC, including SARS-CoV2-S / EPM / EABR (FIG. 2E), SCT MART1 / D1 / EABR (FIG. 2F) and SCT MART1 / D1 (FIG. 2G). Samples were stained with a primary rabbit anti-HLA-A antibody and a secondary 6 nm gold-conjugated anti-rabbit antibody that appears as black punctate in image. Scale bars, 100 nm. In FIG. 2E, SARS-CoV2- S / EPM / EABR. Spike protein coronas are visible around the edges of the spherical vesicles. A single gold nanoparticle from a secondary antibody is visible in the middle of the image. In FIG. 2F, SCT MART1 / D1ZEABR gold particles from secondary antibody can be seen as halos of black punctate around deflated vesicles. In FIG. 2G, SCT MART 1 / D 1 scattered gold particles from secondary antibody can be seen as non-specific staining without the presence of vesicles.

[0052] FIG. 3A-FIG. 3B show the generalization of EABR-mediated APV release across SCT pMHCI variants. FIG. 3A shows sandwich ELISA of murine SCT pMHCI of APVs purified by ultracentrifugation from transfected HEK293T cells (2 replicates per dilution). Mouse anti-H-2Kd capture antibody, biotinylated mouse anti-H-2Kd primary antibody, and HRP-conjugated streptavidin secondary antibody. FIG. 3B shows sandwich ELISA of chimeric human / mouse SCT pMHCI protein on APVs purified by ultracentrifugation from transfected HEK293T cell culture supernatants (2 replicates per dilution). Mouse anti-NYES01 :HLA- A*02:01 capture antibody, biotinylated mouse anti-NYES01 :HLA-A*02:01 primary antibody, and HRP-conjugated streptavidin secondary antibody.

[0053] FIG. 4A-FIG. 4C show IFN-y release from their cognate T cells in vitro induced by pMHCIZEABR APVs. FIG. 4A shows quantitative Western blot comparing knownamounts of NYES01 :HLA-A*02:01 tetramer (NYES01 tet.) standards (lanes 1-5) with various dilutions of purified NYES01 / D9 / EABR APVs (NYES01 APVs) (lanes 6-9) to determine pMHCI protein concentrations in APV samples. Mouse anti-P2M primary antibody, Alexa488- conjugated anti-mouse secondary antibody. FIG. 4B shows scans of ELISPOT wells detecting IFN-y release from one replicate test of Donor 3’s T cells after being dosed with serial dilutions of NYES01:HLA-A*02:01 tetramers (NYES01 Tetramer), SCT NYES01 / D9 / EABR APVs, and SCT MART1 / D9 / EABR APVs (top three rows) and scans of ELISPOT wells detecting IFN- y release from T cells dosed with 1.5% PHA as a positive control, wells without cells as a negative control (No cells), and T cells plated without antigen challenge (No antigen) (bottom row). FIG. 4C shows ELISPOT spot forming units for IFN-y from T cells of three different donors dosed with SCT NYES01 / D9 / EABR APVs, SCT MART1 / D9 / EABR APVs, NYES01 :HLA-A*02:01 tetramers (NYES01 Tetramer), or no antigen challenge. Each data point is the response per IxlO6cells. Baseline stimulation (z.e., “No antigen” - plated T cells without stimulation by antigen) was measured in triplicate for each donor and presented as a single mean in each plot with standard deviation. Because the NYES01 :HLA-A*02:01 tetramers generated larger spot sizes on average compared to the APVs, Donor 3’s spot forming units were too numerous to count when dosed with more than 10 ng of NYES01 :HLA-A*02:01 tetramer, preventing direct comparison between antigen conditions at higher concentrations for this donor. Significant differences between conditions linked by vertical lines are indicated by asterisks: ns > 0.05; *p < 0.05; **p < 0.01; ***p < 0.001; ****p < 0.0001.

[0054] FIG. 5 displays additional micrographs of pMHCI / EABR grids prepared by immuno-EM showing APVs. All micrographs show Expi293F cell culture supernatant after transfection with a SCT MART 1 / D 1ZEABR construct and purified by ultracentrifugation and SEC as outlined in FIG. 1C. Panels A-D in FIG. 5 show 50 mL of purified Expi293F cell culture supernatant. Panels E-I in FIG. 5 show 200 mL of purified Expi293F cell culture supernatant further diluted in pH 7.4 PBS after purification. All grids were prepared using the identical protocol as in FIG. IF, FIG. 2C and FIG. 2E-FIG. 2F. Secondary 6 nm gold-conjugated antirabbit antibody bound to primary rabbit anti-HLA-A antibody appears as black punctate in the image. In panel A of FIG. 5, scale bar = 200 nm. In panels B-I of FIG. 5, scale bar = 100 nm.

[0055] FIG. 6A-FIG. 6B show Western blots of purified APVs that were negative for CD81 (FIG. 6A) and CD63 (FIG. 6B), including purified Expi293F SCT DI MART1 / D1 / EABR APVs (XP293F Dl / EABR APVs), Expi293F purified supernatant, HEK293T SCT DI MART1 / D1 / EABR APVs (HEK293T Dl / EABR APVs), HEK293T cell extract, and HEK293T purified supernatant.

[0056] FIG. 7A-FIG. 7B show indirect ELISA of purified Expi293F and HEK293Ttransfection supernatant, suggesting complete pMHCI not required for APV release. Indirect ELISA of purified Expi293F (FIG. 7 A) and HEK293T (FIG. 7B) supernatant transfected with SCT MART1 / D1 / EABR (SCT / EABR), SCD Dl / EABR (SCD / EABR), DI HC-EABR (HCZEABR), and the non-EABR versions of the three constructs: SCT MART1 / D1 (SCT), SCD DI (SCD), and HC DI (HC). The diagrams of SCT, SCD, and HC are in FIG. 2D. All supernatant was purified by ultracentrifugation and re-suspended in pH 7.4 PBS. Polyclonal rabbit anti-HLA-A was used for the primary antibody, and HRP-conjugated goat anti-rabbit was used for the secondary antibody (2 replicate measurements per dilution).

[0057] FIG. 8 displays sandwich ELISA of purified Expi293F transfection supernatant showing non-EABR SCT capable of vesicle formation. Sandwich ELISA of purified Expi293F supernatant transfected with: SCT NYESO1 / D9 / EABR (SCT / EABR); SCD D9 / EABR (SCD / EABR) along with co-transfected NYESO1 peptide; HC-D9 / EABR (HCZEABR) along with co-transfected NYESO1 / P2M; and, the non-EABR versions of the three constructs: SCT NYESO1 / D9 (SCT) and SCD D9 (SCD) with co-transfected NYESO1, and HC-D9 (HC) with co-transfected NYESO1 / P2M. All supernatant was purified by ultracentrifugation and re-suspended in pH 7.4 PBS. Monoclonal human anti -NYESO EHL A- A*02:01 complex was used for the initial capture antibody. Biotinylated monoclonal human anti-NYES01 :HLA-A*02:01 complex was used for the primary detection antibody and secondary strep-HRP was then incubated in each well before developing with HRP substrate. (2 replicate measurements per dilution).

[0058] FIG. 9A-FIG. 9C show scans of ELISPOT plates detecting IFN-y release from donor T cells from Donor 1 (FIG. 9A), Donor 2 (FIG. 9B), and Donor 3 (FIG. 9C), after being dosed with serial dilutions of SCT NY-ESO-1 / D9 / EABR APVs (lanes 4, 7 and 10), SCT MART1 / D9ZEABR APVs (lanes 5, 8 and 11), and NYESO1 :HLA-A2 tetramers (lanes 6, 9 and 12); 1.5% PHA (lane 3, row A of FIG. 9A-FIG. 9C); without cells or antigen challenge (lane 2, rows A of FIG. 9A-FIG. 9C); and cells without antigen challenge (lane 1, rows A-C of FIG. 9A- FIG. 9C).

[0059] FIG. 10A-FIG. 10G shown that EABR addition to pMHCII promoted budding of the complete, intended pMHCII complex on APVs. FIG. 10A displays a schematic showing cartoon representation of naturally-occurring MHCII including the alpha and beta chains that form the full MHCII complex. A MHCII complex is termed a peptide-MHCII (pMHCII) complex when a presenting peptide is bound in the peptide-binding cleft formed by the complexed MHCII alpha and beta chains. FIG. 10B displays a schematic showing a SCT pMHCII / EABR construct (SCT-T & SCT-TZEABR) and various alternative constructs used for the ELISA in FIG. 10C-FIG. 10G. FIG. 10C shows ELISA of purified vesicles from Expi293Fcells that were transfected with various DNA plasmids encoding a murine version of MHCII, I- Ab, presenting the E alpha peptide (Ea) or pMHCII single-chain trimer constructs. FIG. 10D shows ELISA of purified vesicles from HEK293T cells that were transfected with various DNA plasmids encoding a murine version of MHCII, LAb, presenting the E alpha peptide (Ea) or pMHCII single-chain trimer constructs. FIG. 10E shows ELISA of purified vesicles from NMuMG cells that were transfected with various mRNA transcripts encoding a murine version of MHCII, I- Ab, presenting the E alpha peptide or pMHCII single-chain trimer constructs. 10F shows ELISA of purified vesicles from Expi293F cells that were transfected with various DNA plasmids encoding a murine version of MHCII, I- Ab, presenting the multiple-sclerosis-relevant myelin oligodendrocyte peptide or pMOG peptide as well as single-chain trimer pMHCII constructs. FIG. 10G shows ELISA of purified vesicles from HEK293T cells that were transfected with various DNA plasmids encoding a murine version of MHCII, I- Ab, presenting the myelin oligodendrocyte peptide or pMOG peptide as well as single-chain trimer pMHCII constructs.

[0060] FIG. 11A-FIG. 11D show that engineered extracellular vesicles improved single cell capture and T cell activation on hydrogel nanovials compared to functionalizing the hydrogel surface with recombinant protein. FIG. 11A shows a schematic of a plasmid construct containing a membrane protein fused to a Gly3Ser spacer (SEQ ID NO: 9), and an EABR vesicle-forming sequence (top) and a schematic of membrane-bound protein on a cell surface containing cytoplasmic tail EABR additions that induced budding of a vesicle comprising a lipid bilayer with embedded membrane proteins containing the EABR sequence. FIG. 1 IB shows a schematic showing production and purification of the engineered EABR-mediated extracellular vesicles. FIG. 11C shows post-fabrication biotinylation of hydrogel nanovials via gelatin, which were then functionalized with streptavidin, followed by biotinylated capture antibodies. FIG. 11D shows detection of cytokines released by activated cells that were captured within the nanovial, using fluorescent sandwich antibodies.

[0061] FIG. 12A-FIG. 12D show presentation of both HER2 / EABR and CD54 proteins on purified extracellular vesicles present in transfection supernatant after co-expression of HER2 / EABR and CD54. FIG. 12A shows a schematic showing the plasmid construct for HER2 vesicles featuring a G3S spacer (SEQ ID NO: 9) and the EABR vesicle-forming sequence. The plasmid was transfected into HEK293T or Expi293F cells and vesicles were harvested as shown in FIG. 11 A. FIG. 12B shows a schematic showing the plasmid construct for HER.2 + CD54 vesicles. Only HER2 required a vesicle-forming EABR sequence to be appended for both CD54 and HER2 to appear on the harvested vesicles. FIG. 12C shows results of sandwich ELISA of APVs purified by ultracentrifugation from transfected Expi293F cells. Cellswere co-transfected with HER2ZEABR and CD54, HER2ZEABR alone, HER2 / EABR and CD54ZEABR, or HER2 constructs (2 replicates per dilution). In the top panel anti-HER2 antibodies were used for capture, biotinylated anti-HER2 antibodies were used for detection, and HRP-conjugated streptavidin secondary antibodies were used for visualization. In the bottom panel, anti-CD54 antibodies were used for capture, biotinylated anti-HER2 antibodies were used for detection, and HRP-conjugated streptavidin secondary antibodies were used for visualization. FIG. 12D shows immuno-EM image of vesicles purified by ultracentrifugation and size-exclusion chromatography from Expi293F cells co-transfected with HER2 / EABR and CD54 constructs. Primary antibodies used were mouse anti-HER2 and rabbit anti-CD54. Secondary antibodies 12 nm gold-conjugated anti-mouse antibodies for visualization of HER2 appeared as black punctae in image and highlighted by arrows with Secondary 6nm gold- conjugated anti-rabbit antibodies for visualization of CD54 appeared as smaller black punctae in image and highlighted by arrows without Scale bar, 200 nm.

[0062] FIG. 13A-FIG. 13D show that coating hydrogel nanovials with vesicles copresenting HER2 / EABR and CD54 improved cell loading and CAR-T activation compared to coating with recombinant HER2. FIG. 13 A shows immobilization of HER2 eVLP on 35 pm and 50 pm nanovials based on concentration of aHER2 capture antibodies on the nanovials. Maximum capture signal was detected at around 20 pg / mL aHER2 capture antibodies for both 35 pm and 50 pm nanovials. FIG. 13B shows the significantly higher capture rate of CD54 / HER2 eVLP on nanovials compared to the HER2-only eVLP. This signal was comparable to the positive control of nanovials conjugated with 20 pg / mL recombinant HER2 (rHER2). FIG. 13C shows aHER2 CAR cell and control untransfected (UTX) T cell loading in nanovials using both HER2 eVLP and CD54 / HER2 eVLP. FIG. 13D displays flow data showing improvement in nanovial assay using eVLP.

[0063] FIG. 14A-FIG. 14H show that co-expression of SCT pMHCIZEABR and CD274, CD83 or CD80 immunoregulatory proteins allowed for fine-tuned synthesis of known endogenous immunoregulatory extracellular vesicles. FIG. 14A shows a schematic of the assay performed for the top row of FIG. 14C-FIG. 14E. Expression of immunoregulatory membrane proteins CD274, CD83, or CD80 on engineered extracellular vesicles were captured with plated antibody, then co-presented NYES01 / HLA-A*02:01 were detected and quantified with biotinylated anti-NYESO:HLA-A*02:01 and HRP-conjugated streptavidin (strep-HRP). FIG. 14B shows a schematic of the assay performed for the bottom row of FIG. 14C-FIG. 14E. Identical assay was performed in FIG. 14A and FIG. 14B, except that the capture antibody and detection antibody were swapped. FIG. 14C shows results of sandwich ELISA of APVs purified by ultracentrifugation from transfected Expi293F cells using anti-CD274 for capture,biotinylated anti-NYES01 :HLA-A*02:01 (3M4E5) for detection, and HRP-conjugated streptavidin secondary. Cells were co-transfected with SCT NYES01 / D9 / EABR and CD274, SCT NYES01 / D9 / EABR and CD274 / EABR, SCT NYES01 / D9 and CD274 / EABR, or SCT NYES01 / D9 and CD274 constructs (2 replicates per dilution). FIG. 14D shows results of sandwich ELISA of APVs purified by ultracentrifugation from transfected Expi293F cells using anti-CD83 for capture, biotinylated anti-NYES01 :HLA-A*02:01 (3M4E5) for detection, and HRP-conjugated streptavidin secondary. Cells were co-transfected with SCT NYES01 / D9 / EABR and CD83, SCT NYES01 / D9 / EABR and CD83 / EABR, SCT NYES01 / D9 and CD83ZEABR, or SCT NYES01 / D9 and CD83 constructs (2 replicates per dilution). FIG. 14E shows results of sandwich ELISA of APVs purified by ultracentrifugation from transfected HEK293T cells using anti-CD80 for capture, biotinylated anti-NYES01 :HLA-A*02:01 (3M4E5) for detection, and HRP-conjugated streptavidin secondary. Cells were co-transfected with SCT NYES01 / D9 / EABR and CD80, SCT NYES01 / D9 / EABR and CD80 / EABR, SCT NYES01 / D9 and CD80ZEABR, or SCT NYES01 / D9 and CD80 constructs (2 replicates per dilution). FIG. 14F shows results of nano flow cytometry (NanoFCM) of APVs purified by ultracentrifugation from transfected HEK293T cells, and co-stained with APC anti-CD80 and Alexa488 anti-NYES01 :HLA-A*02:01 (3M4E5). In the top-left panel of FIG. 14F, vesicles were purified from HEK293T transfected with the MART1 / D9 / EABR construct were used for gating non-specific signal from irrelevant extracellular vesicles. In the top-right panel of FIG. 14F, vesicles were from HEK293T cells transfected with the NYES01 / D9 / EABR construct. In the bottom-left panel of FIG. 14F, v esicles were from HEK293T cells transfected with NYES01 / D9 / EABR and CD80 constructs. In the bottom-right panel of FIG. 14F, vesicles were from HEK293T cells transfected with NYES01 / D9 / EABR and CD80ZEABR constructs. FIG. 14G shows results of NanoFCM size analysis of vesicles purified by ultracentrifugation from HEK293T cells co-transfected with NYES01 / D9 / EABR and CD80 / EABR constructs. FIG. 14H shows immuno-EM image of vesicles purified by ultracentrifugation and size-exclusion chromatography from Expi293F cells co-transfected with NYES01 / D9 / EABR and CD80 / EABR constructs. Primary antibodies used were human anti-NYES01 :HLA-A*02:01 (3M4E5) antibody and mouse anti-CD80. Secondary 12 nm gold-conjugated anti-mouse antibody appeared as black punctae in image and highlighted by arrow with Secondary 6 nm gold- conjugated anti-human antibody appeared as smaller black punctae in image and highlighted by arrow without Scale bar, 200 nm.

[0064] FIG. 15A-FIG. 151 show that coating hydrogel nanovials with synthetic antigen-presenting vesicles co-presenting pMHCIZEABR and CD80 improved cell loading and T cell activation compared to coating with recombinant pMHCI. FIG. 15A-FIG. 15D show flowcytometry gating strategy for T-cell loaded nanovials and secretion detection. FIG. 15A shows that single nanovials were separated from hydrogel / PEG debris and nanovial “doublets,” which were incorrectly formed during microfluidic fabrication. FIG. 15B shows that live cells were stained positively with Calcein AM. FIG. 15C shows that NGFR+ cells were identified as having been successfully transfected with the 1G4 T cell receptor specific for NYES01 / HLA- A*0201. FIG. 15D shows that nanovials passing the previous flow cytometry gates were then assessed for their anti-IFN-y BV421 signal, which was a readout for T cell activation. FIG. 15E- FIG. 151 show the results of the flow cytometry analysis illustrated in FIG. 15A-FIG. 15D on nanovial cavity surface with different conjugations: NYES01 / MHCI (FIG. 15E), aCD45 antibodies (FIG. 15F), aCD45 antibodies and MART1 / MHCI (FIG. 15G), NYES01 pMHC- eVLPs conjugated to nanovial cavity through a NYES01 / MHCI antibodies (FIG. 15H), and NYES01 and CD80 pMHC-eVLPs conjugated to nanovial cavity through a NYES01 / MHCI antibodies (FIG. 151). First panels from top of FIG. 15E-FIG. 151 show comparison of interaction between T cells and nanovial cavity surface with different conjugations. Second panels from top of FIG. 15E-FIG. 151 show relative cell loading rates into nanovials using different binding moi eties. Third panels from top of FIG. 15E-FIG. 151 show IFN-y secretion levels from single T cells on nanovials. Matched pMHCs (protein monomer and eVLP format) triggered T cell activation.

[0065] FIG. 16 displays a western blot showing presence of pMHC-EABR particles in exosomal fraction after centrifugation using an anti-HLA-A antibody.

[0066] FIG. 17 shows a diagram explaining a proposed mechanism of action for how the SCT pMHC mRNA LNP vaccine would work to down-regulate immune cells against a specific target.

[0067] FIG. 18 shows a diagram explaining a proposed mechanism of action for how a SCT pMHC and CD86 mRNA LNP vaccine would work to activate immune cells against a specific target.

[0068] FIG. 19 shows a flowchart explaining how the vesicles disclosed herein can be generated and purified.DETAILED DESCRIPTION

[0069] In the following detailed description, reference is made to the accompanying drawings, which form a part hereof. In the drawings, similar symbols typically identify similar components, unless context dictates otherwise. The illustrative embodiments described in the detailed description, drawings, and claims are not meant to be limiting. Other embodiments may be utilized, and other changes may be made, without departing from the spirit or scope of the subject matter presented herein. It will be readily understood that the aspects of the presentdisclosure, as generally described herein, and illustrated in the Figures, can be arranged, substituted, combined, separated, and designed in a wide variety of different configurations, all of which are explicitly contemplated herein and made part of the disclosure herein.

[0070] All patents, published patent applications, other publications, and sequences from GenBank, and other databases referred to herein are incorporated by reference in their entirety with respect to the related technology.

[0071] Disclosed herein include compositions. In some embodiments, the composition comprises: a nucleic acid composition comprising one or more polynucleotides encoding components of an antigen presentation complex (APC). In some embodiments, the components of the APC are capable of assembling into an antigen-presenting vesicle (APV) budded from a cell in which the APC components are expressed. In some embodiments, the APV comprises a plurality of APCs. In some embodiments, the APC comprises an APC- assembly domain, one or more antigen presentation polypeptide(s) and a presenting peptide. Disclosed herein include compositions. In some embodiments, the composition comprises: a population of an antigen-presenting vesicles (APVs). In some embodiments, each of the APVs comprises a plurality of antigen presentation complexes (APCs). In some embodiments, the APC comprises an APC-assembly domain, one or more antigen presentation polypeptide(s) and a presenting peptide. The composition can further comprises instructions for use of the composition for: stimulating an immune response in a subject in need thereof; treating or preventing a disease or disorder in a subject in need thereof; and / or treating or preventing a cancer or an autoimmune disorder in a subject in need thereof.

[0072] Disclosed herein include kits. In some embodiments, the kit comprises the composition disclosed herein. Disclosed herein include cells. In some embodiments, the cell comprises the nucleic acid composition disclosed herein.

[0073] Disclosed herein include methods of stimulating an immune response in a subject in need thereof. In some embodiments, the method comprises: administering to the subject a therapeutically effective amount of the composition or the cell disclosed herein, thereby stimulating an immune response in the subject. Disclosed herein include methods of treating or preventing a disease or disorder in a subject in need thereof. In some embodiments, the method comprises: administering to the subject a therapeutically effective amount of the composition or the cell disclosed herein, thereby treating or preventing the disease or disorder in the subject. In some embodiments, the disease or disorder is a cancer or an autoimmune disorder. Disclosed herein include methods for treating or preventing a cancer or an autoimmune disorder in a subject in need thereof. In some embodiments, the method comprises: administering to the subject a therapeutically effective amount of the composition or the cell disclosed herein,thereby treating or preventing a cancer or the autoimmune disorder in the subject.

[0074] Disclosed herein include methods of modulating an immune cell. In some embodiments, the method comprises: contacting the immune cell with the composition disclosed herein. In some embodiments, modulating comprising activating, regulating, stimulating, and / or suppressing. Disclosed herein include method of isolating an immune cell of interest. In some embodiments, the method comprises: contacting a population of cells suspected of comprising of an immune cell of interest with the composition disclosed herein.Definitions

[0075] Unless defined otherwise, technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which the present disclosure belongs. See, e.g. Singleton et al., Dictionary of Microbiology and Molecular Biology 2nd ed., J. Wiley & Sons (New York, NY 1994); Sambrook et al., Molecular Cloning, A Laboratory Manual, Cold Spring Harbor Press (Cold Spring Harbor, NY 1989). For purposes of the present disclosure, the following terms are defined below.

[0076] As used herein, the terms “antigen” or “immunogen” are used interchangeably to refer to a substance, typically a protein, which is capable of inducing an immune response in a subject (e.g. a mammal, such as a human). The term also refers to proteins that are immunologically active in the sense that once administered to a subject, either directly or in the form of a nucleotide sequence or vector that encodes the protein, is able to evoke an immune response of the humoral and / or cellular type directed against that protein or a variant thereof.

[0077] As used herein, “sequence identity” or “identity” in the context of two nucleic acid or polypeptide sequences makes reference to the nucleotide bases or residues in the two sequences that are the same when aligned for maximum correspondence over a specified comparison window. Methods of alignment of sequences for comparison are well known in the art. Various programs and alignment algorithms are described in: Smith & Waterman, Adv. Appl. Math. 2:482, 1981; Needleman & Wunsch, J. Mol. Biol. 48:443, 1970; Pearson & Lipman, Proc. Natl. Acad. Sci. USA 85:2444, 1988; Higgins & Sharp, Gene, 73:237-44, 1988; Higgins & Sharp, CABIOS 5: 151-3, 1989; Corpet et al., Nuc. Acids Res. 16: 10881-90, 1988; Huang et al. Computer Appls. in the Biosciences 8, 155-65, 1992; Pearson et al., Meth. Mol. Bio. 24:307-31, 1994; and Altschul et al., J. Mol. Biol. 215:403-10, 1990 (the content of each of these references is incorporated herein in its entirety).

[0078] When percentage of sequence identity or similarity is used in reference to proteins, it is recognized that residue positions which are not identical often differ by conservative amino acid substitutions, where amino acid residues are substituted with afunctionally equivalent residue of the amino acid residues with similar physiochemical properties and therefore do not change the functional properties of the molecule. A functionally equivalent residue of an amino acid used herein typically can refer to other amino acid residues having physiochemical and stereochemical characteristics substantially similar to the original amino acid. The physiochemical properties include water solubility (hydrophobicity or hydrophilicity), dielectric and electrochemical properties, physiological pH, partial charge of side chains (positive, negative or neutral) and other properties identifiable to one of skill in the art. The stereochemical characteristics include spatial and conformational arrangement of the amino acids and their chirality. For example, glutamic acid is considered to be a functionally equivalent residue to aspartic acid in the sense of the current disclosure. Tyrosine and tryptophan are considered as functionally equivalent residues to phenylalanine. Arginine and lysine are considered as functionally equivalent residues to histidine.

[0079] The term “substantially identical” as used herein in the context of two or more sequences refers to a specified percentage of amino acid residues or nucleotides that are identical or functionally equivalent, such as about, at least or at least about 65% identity, optionally, about, at least or at least about 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity over a specified region or over the entire sequence.

[0080] As used herein, the term “variant” refers to a polynucleotide or polypeptide having a sequence substantially similar or identical to a reference (e.g., the parent) polynucleotide or polypeptide. In the case of a polynucleotide, a variant can have deletions, substitutions, additions of one or more nucleotides at the 5' end, 3' end, and / or one or more internal sites in comparison to the reference polynucleotide. Similarities and / or differences in sequences between a variant and the reference polynucleotide can be detected using conventional techniques known in the art, for example polymerase chain reaction (PCR) and hybridization techniques. Variant polynucleotides also include synthetically derived polynucleotides, such as those generated, for example, by using site-directed mutagenesis. Generally, a variant of a polynucleotide, including, but not limited to, a DNA, can have at least, or at least about, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or more sequence identity to the reference polynucleotide as determined by sequence alignment programs known in the art. In the case of a polypeptide, a variant can have deletions, substitutions, additions of one or more amino acids in comparison to the reference polypeptide. Similarities and / or differences in sequences between a variant and the reference polypeptide can be detected using conventional techniques known in the art, for example Western blot. A variant of a polypeptide can have, for example, at least, or at least about, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,99%, or more sequence identity to the reference polypeptide as determined by sequence alignment programs known in the art.

[0081] Standard techniques can be used for recombinant DNA, oligonucleotide synthesis, and tissue culture and transformation (e.g., electroporation, lipofection). Enzymatic reactions and purification techniques can be performed according to manufacturer's specifications or as commonly accomplished in the art or as described herein. The foregoing techniques and procedures can be generally performed according to conventional methods well known in the art and as described in various general and more specific references that are cited and discussed throughout the present specification. See, e.g., Sambrook et al., Molecular Cloning: A Laboratory Manual (2d ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. (1989)), which is incorporated herein by reference for any purpose. Unless specific definitions are provided, the nomenclatures utilized in connection with, and the laboratory procedures and techniques of, analytical chemistry, synthetic organic chemistry, and medicinal and pharmaceutical chemistry described herein are those commonly known and used in the art. Standard techniques can be used for chemical syntheses, chemical analyses, pharmaceutical preparation, formulation, and delivery, and treatment of patients.

[0082] The term “construct,” as used herein, refers to a recombinant nucleic acid that has been generated for the purpose of the expression of a specific nucleotide sequence(s), or that is to be used in the construction of other recombinant nucleotide sequences.

[0083] As used herein, the terms “nucleic acid” and “polynucleotide” are interchangeable and refer to any nucleic acid, whether composed of phosphodiester linkages or modified linkages such as phosphotriester, phosphoramidate, siloxane, carbonate, carboxymethylester, acetamidate, carbamate, thioether, bridged phosphoramidate, bridged methylene phosphonate, bridged phosphoramidate, bridged phosphoramidate, bridged methylene phosphonate, phosphorothioate, methylphosphonate, phosphorodithioate, bridged phosphorothioate or sultone linkages, and combinations of such linkages. The terms “nucleic acid” and “polynucleotide” also specifically include nucleic acids composed of bases other than the five biologically occurring bases (adenine, guanine, thymine, cytosine and uracil). Assembly of Antigen Presentation Vesicles

[0084] All nucleated cells of the human body present intracellular proteins on their surface as digested peptides bound to class I major histocompatibility complexes (MHCI). When a peptide is bound to MHCI, the complex is referred to as peptide:MHCI (pMHCI). The T cell receptors (TCRs) of CD8+ T cells can recognize the presence of infection or cancer by binding pMHCI strongly and specifically, when the peptide presented by MHCI is of pathologic origin. Class II major histocompatibility complex, MHCII, is present on the membrane surface ofprofessional antigen presenting cells, such as macrophages and dendritic cells, which are specialized cells of the immune system that are efficient at presenting pMHCII. In this case, the peptide on MHCII originates from extracellular origins such as a foreign pathogen or virus. When pMHCII binds to its cognate TCR on CD4+ T cells, a focused, adaptive immune response is initiated to eliminate targets presenting the antigenic peptide. In cases of both classes of MHC, the activation of T cells and the initiation of an immune response requires additional co- stimulatory / molecules, such as CD80 / CD86 and CD28, to bind along with the pMHC-TCR interaction. Without these co-stimulatory signals, pMHC complexes binding to TCRs can do the opposite: they can cause T cell anergy, apoptosis, or differentiation into a regulatory phenotype that turns down immune responses specifically for that peptide.

[0085] In 1996, the release of B cell-derived extracellular vesicles (EVs) with functional pMHC complexes on their surface was reported. Over the next two decades, EVs that were previously labeled as simple cellular “debris” were increasingly recognized for their immunoregulatory potential. Naturally occurring antigen-presenting vesicles (APVs), in particular, have been demonstrated to orchestrate immune responses either directly or with the aid of antigen-presenting cells.

[0086] The significance of antigen presenting cells and APVs in regulating immune responses has inspired researchers to try recreating the functionality of the antigen presenting cells synthetically. In 1978, pMHCI was incorporated into phospholipid vesicles to induce cytotoxic T lymphocytes. Research teams have since ventured to engineer more complex versions of these APVs that can direct the immune system to attack a target of interest, deeming them “artificial antigen-presenting cells.” Initial rudimentary artificial antigen-presenting cells were designed by conjugating MHC together as tetramers using biotin and streptavidin, which is still used today to capture and identify T cells with high affinity for a specific pMHC. Later designs for artificial antigen-presenting cells included whole mammalian cells conjugated with immunostimulatory molecules, iron-oxide or polymer nanoparticles conjugated with effector proteins from antigen presenting cells, nanoparticles coated with membranes of antigen presenting cell via extrusion or sonication, or engineered extracellular blebs from dendritic cells. These existing approaches often involve non-specific activation of the adaptive immune system to demonstrate a proof-of-concept, or they require the patient’s own cells (i.e. autologous cells) to be harvested and processed before treatment can be administered. Furthermore, while the direct manipulation of dendritic cells through gene therapy or targeted antigen delivery has shown promising results, there are also some limitations of this route. For example, copy numbers of dendritic cell in blood are relatively low. Thus, the generation of sufficient autologous antigen presenting cells to prepare exosomes or artificial antigen presenting cellsfrom dendritic cell lysates remains a barrier to the broad utility of antigen-presenting cells - based therapies. Moreover, better T cell activation from the nanoparticle artificial antigen- presenting cells than from actual dendritic cells can be due in part to the low copy number and activation potential of the autologous dendritic cells and the added benefit afforded by “crossdressing” nearby cells with the nano-sized artificial antigen-presenting cells.

[0087] Significant attention has been given to producing antigen-presenting cells via microfluidics, but existing microfluidic vesicles suffer from short half-lives and are very susceptible to rupture due to osmotic changes and the turbulent flow of the lymphatic and cardiovascular systems. It was demonstrated that iron-oxide nanoparticles coated in pMHCI complexes could restore normoglycemia in non-obese diabetic mice. Since then, the efficacy of his pMHCI and pMHCII nanoparticles was demonstrated for restoring motor function in a murine model of experimental autoimmune encephalitis (a corollary to multiple sclerosis) and collagen-induced arthritis (a corollary to rheumatoid arthritis), in addition to increasing the efficacy of the normoglycemia-restoring nanoparticles in diabetic mice. There are some critical limitations of these iron-oxide nanoparticles. For example, rigid adherence of the pMHC complex to the nanoparticle surface reduces pMHC movement, which has been considered important for allowing signal protein and receptor reorganization in response to T cell contact, i.e. forming an immunological synapse between a T cell TCR cluster and a pMHC bouquet. Rigid spherical structure of the nanoparticle scaffold reduces the potential surface area for ideal pMHC-TCR interactions, as oblong artificial antigen-presenting cells have been demonstrated to more effectively activate T cells than spherical artificial antigen-presenting cells. The biodistribution of pMHC iron-oxide nanoparticles was largely sequestered to the liver and spleen. Particles that more closely resemble endogenous extracellular vesicles may have better biodistribution. Exogenously generated iron-oxide nanoparticles require each patient’s HLA type to be sequenced before administration of the therapy. In comparison, an endogenously generated APV could potentially use the patient’s own MHC molecules without requiring any patient HLA-typing.

[0088] An ideal antigen-presenting vesicle therapeutic, such as the antigen- presenting vesicle (APV) disclosed herein, would avoid the aforementioned limitations. The APV can also have advantages that has not been fully accomplished by existing therapeutic. Targeted immunoregulation of a single immune pathology can be achieved without suppressing any desirable immune responses to viral, bacterial, or parasitic pathogens, the APV can recapitulate existing, physiologically natural pathways for immunoregulation. The APVs can be made / produced in sufficient quantities without difficulty (e.g. therapies relying on the use of antigen-presenting cells may be difficult to manufacture or collect from the patient). To achievegood biodistribution, the APV can be >30 nm in size to avoid excretion in the kidneys and <100 nm in size to avoid the reticuloendothelial system, which sequesters larger particles in the liver and spleen. The APV can allow for additional “tissue targeting” moieties to be added if desirable. Moreover, the APV can also be easily administered for both the patient and healthcare team, well-tolerated by patients and of low-cost.

[0089] By leveraging recent advances in the creation of enveloped virus like particles (eVLPs) generated in vivo from mRNA vaccination, APVs that can either stimulate an immune response against targets of interest (e.g., cancer and viral targets) or down-regulate an undesirable autoimmune response (e.g. type I diabetes, rheumatoid arthritis, multiple sclerosis) are disclosed herein (FIG. 17 and FIG. 18).

[0090] These APVs supported pMHC complexes in lipid membranes that were sturdy and survived paraformaldehyde fixation, disruption by repeated aspiration and centrifugation, and changes in temperature. The pMHC complexes were distributed throughout the enveloped lipid membrane of exosome-like vesicles when observed by negative stain immuno-electron microscopy, and the vesicles were produced in high-copy number as evident by both western blotting and enzyme-linked immunosorbent assay (ELISA) (FIG. 16). Both pMHCI and pMHCII vesicles were made using this technology.

[0091] Additional immunoregulatory proteins (e.g., costimulatory molecules CD80 / CD86, immunosuppressive proteins such as CD73, cellular adhesion proteins such as LFA-1, anti -phagocytic proteins such as CD47, or tissue-homing proteins such as CCR7) can be added to the membranes of the vesicles in a similar fashion as disclosed herein.

[0092] In one embodiment, the APVs disclosed herein can be manufactured using large-scale biomanufacturing, processed externally, optionally stored for an extended period of time, and later injected into patients as therapeutic immunoregulatory vesicles.

[0093] In another embodiment, the APVs disclosed herein can be delivered therapeutically in the form of a lipid nanoparticle mRNA vaccine, and the APVs are translated / generated in the patient by the patient’s own cells. These APVs can recruit / use the patient’s own cellular proteins in addition to new proteins that were generated by an RNA transcript delivered as part of the nanoparticle mRNA vaccine.

[0094] In another embodiment, the APVs can be used as a way to activate / regulate / stimulate and / or isolate PBMCs or T cells in an in vitro context - these pMHC vesicles can be generated to search for unconventional major histocompatibility complex (MHC) molecules or rare TCRs in a large cell-based screen, e.g. Dino Di Carlo’s nanovial system.

[0095] In some embodiments, the APC comprises an amino acid sequence having at least 65%, 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% sequence identity to an amino acidsequence selected from SEQ ID NOs: 37-52, 55-56, 59-60, 63-80, 114-119, 122-143, 146-151, and 154-159. Exemplary APCs and / or portions thereof provided herein are listed in Table 1 below.Table 1 : Exemplary APCs and portions thereofThe APC-Assembly Domain

[0096] In some embodiments, the APC-assembly domain recruits one or more ESCRT proteins to the cytoplasmic tail of the APC. In some embodiments, the recruitment of ESCRT proteins via the APC-assembly domain induces the self-assembly and budding of APVs. The cytoplasmic portion of the APC can comprise the APC-assembly domain. The cytoplasmic tail of the APC can comprise the APC-assembly domain. In some embodiments, the APC- assembly domain interacts with the ESCRT proteins TSG101, NEDD4, and / or ALIX. The systems, methods, compositions, and kits provided herein can, in some embodiments, be employed in concert with the systems, methods, compositions, and kits described in PCT Application Publication No. WO2022261230A1, the content of which is incorporated herein by reference in its entirety.

[0097] The APC-assembly domain can comprise or can be derived from a nonhuman protein, optionally a nonmammalian protein, further optionally a chicken protein, a mouse protein, a lizard protein, a reptile protein, a hamster protein, or a goldfish protein. The APC- assembly domain can comprise or can be derived from the ESCRT and ALIX binding region (EABR) of the human CEP55 protein, optionally residues 170-213. The APC-assembly domain can comprise or can be derived from Syntenin-1, rat Galectin-3 (rGalectin-3), Hrs, and / or CD2AP. The APC-assembly domain can comprise or can be derived from a viral protein, optionally a fragment of a viral protein, further optionally a retroviral protein, herpes simplex viral protein, vaccinia viral protein, hepadnaviral protein, togaviral protein, flaviviral protein, arenaviral protein, coronaviral protein, orthomyxoviral protein, paramyxoviral protein, bunyaviral protein, bornaviral protein, rhabdoviral protein or filoviral protein, optionally a Gag protein, further optionally derived from EIAV, HTLV-1, MLV, or MPMV, optionally EIAV p9 and / or HIV-1 p6. The APC-assembly domain can comprise or can be derived from: an Ebola protein, optionally EBOV VP40. The APC-assembly domain can comprise an amino acid sequence at least about 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%,62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%,78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%,94%, 95%, 96%, 97%, 98%, 99%, 100%, or a number or a range between any two of these values, identical toFNSSINNIHEMEIQLKDALEKNQQWLVYDQQREVYVKGLLAKIFELEKKTETAAHSLPH SLP (SEQ ID NO: 33).

[0098] In some embodiments, the nucleic acid composition does not comprise a polynucleotide encoding SpyTag or lentiviral Gag. In some embodiments, the APC-assembly domain do not comprise SpyTag or lentiviral Gag.

[0099] The APC can comprise an endocytosis-preventing motif (EPM) capable ofpreventing endocytosis of the APC. In some embodiments, the EPM tethers the APC to the cytoskeleton, thereby preventing localization to coated pits and endocytosis; enhances APV assembly, APV production, and / or APV secretion; and / or prevents endocytosis of the APC, thereby extending the time an APV remains at the plasma membrane to interact with ESCRT proteins. In some embodiments, an EPM disclosed herein is employed to generate fusion protein complex with APC, which can, in some embodiments, enhance the activity and / or potency of the APC (e.g., activating T cells), optionally at least about 1.1-fold. There are provided, in some embodiments, an EPM-APC fusion protein complex wherein an EPM is fused with an APC. There are provided, in some embodiments, nucleic acid compositions encoding one or more EPM-APC fusion protein complex. There are provided, in some embodiments, methods of treating a disease or disorder (e.g., a cancer, an autoimmune disease, or an infectious disease) comprising administering an effective amount of said nucleic acid compositions and / or population of APVs to a subject.

[0100] The EPM can be capable of: increasing the abundance and / or density of APCs on and / or in the APV by at least about 2-fold (e.g., 2-fold, 3-fold, 4-fold, 5-fold, 6-fold, 7- fold, 8-fold, 9-fold, 10-fold, 20-fold, 30-fold, 40-fold, 50-fold, 60-fold, 70-fold, 80-fold, 90-fold, 100-fold, or a number or a range between any of these values) as compared to an APV comprising an APC that does not comprise the EPM; and / or increasing the number of APVs secreted by a cell by at least about 2-fold (e.g., 2-fold, 3-fold, 4-fold, 5-fold, 6-fold, 7-fold, 8- fold, 9-fold, 10-fold, 20-fold, 30-fold, 40-fold, 50-fold, 60-fold, 70-fold, 80-fold, 90-fold, 100- fold, or a number or a range between any of these values) as compared to a cell expressing an APC that does not comprise the EPM.

[0101] The EPM can comprise or can be derived from a portion of murine low- affinity gamma Fc region receptor II isoform FcRII-Bl. The EPM can comprise all or a portion of the cytoplasmic tail of FcRII-Bl.The Antisen Presentation Polypeptide

[0102] Antigen presentation comprises the cellular and biochemical events necessary for the recognition and stimulation of CD4 and CD8 T lymphocytes. Antigen presentation requires the T cell receptor to engage the major histocompatibility complex (MHC) molecules together with the presenting peptide (e.g., a segment of the protein antigen). Naturally, the MHCs with a presenting peptide are displayed on the membrane of antigen-presenting cells. The receptor does not engage the antigen unless the antigen forms part of a biomolecular complex with the MHCs. In some embodiments, the antigen presentation polypeptide(s) is capable of forming a binding site that binds the presenting peptide.

[0103] There are two sets of MHC molecules, class I and class II, are required for therecognition of protein antigens. Antigens presented in association with class I MHC molecules are recognized by CD8 T cells, while the antigens in association with class II MHC molecules are recognized by CD4 T cells.

[0104] In some embodiments, the MHC can be derived from a mammal. Mammals includes, but not limited to, humans, domestic and farm animals, zoo animals, sports and pet animals. Non-limiting examples of mammals include mice; rats; rabbits; guinea pigs; dogs; cats; sheep; goats; cows; horses; primates, such as monkeys, chimpanzees and apes, and, in particular, humans. In some embodiments, the MHC is derived from a human. Human MHC is also known as Human Leukocyte Antigen (HLA). In some embodiments, the MHC comprises human leukocyte antigen (HLA) and / or mouse MHC. However, in some embodiments, the MHC is not derived from a human. In some embodiments, the MHC is derived from mouse. Mouse MHC is also called H-2.

[0105] The MHC Class I proteins (“MHCI” or “MHC-I”) are complex transmembrane glycoproteins composed of two main components: a heavy chain, also known as the a chain, and a smaller non-covalently associated protein called p2-microglobulin. The a chain is highly polymorphic. It can exist in various allelic forms leading to a diverse array of MHC-I molecules. The a chain consists of three domains: al, a2, and a3. The al and a2 domains form a peptide-binding cleft, while the a3 domain anchors the complex to the cell membrane. The p2-microglobulin, which is non-polymorphic, is essential for the proper folding and stability of the MHC-I. In some embodiments, the MHC-I is mouse MHC-I or human MHC- I.

[0106] MHC Class II proteins (“MHCII” or “MHC-II”) are primarily expressed on antigen-presenting cells, including dendritic cells, macrophages, and B cells. The MHC-II consists of two transmembrane chains: an a chain and a P chain. Both chains are synthesized in the endoplasmic reticulum and form a heterodimeric complex. The a and P chains each have two domains: al, a2, pi, and P2. In some embodiments, the MHC-II is mouse MHC-II.

[0107] The subclasses of the human HLA-I can be classified into HLA-A, HLA-B, HLA-C, HLA-E, HLA-F, and HLA-G. The sub-classes of human HLA-II can be classified into HLA-DMA, HLA-DMB, HLA-DOA, HLADOB, HLA-DPA1, HLA-DPB1, HLA-DQA1, HLADQB1, HLA-DRA, and HLA-DRB. In some embodiments, the antigen presentation polypeptide(s) are selected from MHC-I a chain, beta-2 microglobulin (P2M), MHC-II a chain, MHC-II P chain, a classical HLA Class I molecule, a non-classical HLA Class I molecule, a classical HLA Class II molecule, a non-classical HLA Class II molecule, HLA-A, HLA-B, HLA-C, HLA-E, HLA-F, HLA-G, HLA-DRA, HLA-DRB 1, HLA-DRB3, HLA-DRB4, HLA- DRB5, HLA-DQA1, HLA-DQB1, HLA-DPA1, HLA-DPB1, HLA-DMA, HLA-DMB, HLA-DOA, HLA-DOB, derivatives thereof, homologs thereof, or any combination thereof.

[0108] HLA can be further classified based on serological typing and / or allele variations. In some embodiments, the HLA comprises serological typing A*02, A*03, A* 11, A*23, A*24, A*26, A*31, A*33, A*34, A*43, A*66, and / or A*74. In some embodiments, the HLA comprises HLA A* 11:01, HLA-A*03:01, and / or HLA-A*02:01. In some embodiments, the HLA is HLA-A*02:01. In some embodiments, the HLA class I is selected from an HLA allele selected from HLA-A*01:01, HLA-A*02:01, HLA-A*02:03, HLA-A*02:06, HLA- A*03:01, HLA-A* 11:01, HLA-A*23:01, HLA-A*24:02, HLA-A*26:01, HLA-A*30:01, HLA- A*30:02, HLA-A*31:01, HLA-A*32:01, HLA-A*33:01, HLA-A*68:01, HLA-A*68:02, HLA- B*07:02, HLA-B*08:01, HLA-B*15:01, HLA-B*35:01, HLA-B*40:01, HLA-B*44:02, HLA- B*44:03, HLA-B*51:01, HLA-B*53:01, HLA-B*57:01, and HLA-B*58:01. In some embodiments, the HLA class II is selected from an HLA allele selected from HLA- DRBl*01:01, HLA-DRBl*15:01, HLA-DRB 1*03:01, HLA-DRB 1*04:01, HLA-DRBl*ll:01, HLA-DRBl*13:01, HLA-DRB 1*07:01, HLA-DRB 1*01:01, HLA-DRB 1*01:02, HLA- DRBl*04:02, HLA-DRB 1*04: 05, HLA-DRB 1*04: 07, HLA-DRB 1*04:08, HLA-DRBl*08:04, HLA-DRB 1*09:01, HLA-DRBl*10:01, HLA-DRB1*11:O2, HLA-DRBl*l l:03, HLA- DRB1*11:O4, HLA-DRB1* 15:02, HLA-DRB1* 15:03, HLA-DRB 1*16:01, HLA-DRB 1*16:02, HLA-DRB3 *02:02, HL A-DRB3 *03:01, HLA-DRB5*01:01, HLA-DQAl*01:01 / DQBl*05:01,HLA-DQAl*05:01 / DQBl*02:01, HLA-DQAl*01:02 / DQBl*05:02, HLA-DQA1 *01 :02 / DQB 1*06:02, HLA-DQAl*03:01 / DQBl*03:02, HLA-DQA1 *01 :02 / DQB 1*06:04, HLA-DQAl*05:01 / DQBl*03:01, HLA-DQAl*02:01 / DQB 1*02:02, HLA-DQA1 *03 :01 / DQB 1*03:01, HLA-DQAl*02:01 / DQB 1*03:03, HLA-DQA1 *03 :03 / DQB 1*03:03, HLA-DPAl*01:03 / DPBl*01:01, HLA-DPAl*01:03 / DPBl*02:01, HLA-DPAl*01:03 / DPBl*03:01, HLA-DPAl*01:03 / DPBl*04:01, HLA-DPA1 *01 :03 / DPB 1*04:02, HLA-DPAl*01:03 / DPBl*05:01, HLA-DPAl*02:01 / DPBl*01:01, HLA-DPAl*02:01 / DPBl*02:01, HLA-DPAl*02:01 / DPBl*03:01, HLA-DPAl*02:01 / DPB 1*04:01, HLA-DPAl*02:01 / DPBl*04:02, HLA-DPAl*02:01 / DPBl*05:01, HLA-DPAl*02:01 / DPBl*06:01, HLA-DPAl*02:01 / DPBl*09:01, HLA-DPAl*02:01 / DPBl*l l:01, HLA-DPAl*02:01 / DPBl*13:01, HLA-DPAl*02:01 / DPBl*14:01, HLA-DPAl*02:01 / DPBl*15:01, and HLA-DPA1*O2:O1 / DPB1*17:OL

[0109] Mouse MHC-I includes the "classical MHC class I" (also called MHC-Ia) that comprises H-2D, H-2K and H-2L subclasses, and the "non-classical MHC class I" (MHC-Ib) that comprises H-2Q, H-2M and H-2T subclasses. Mouse MHC -II includes the "classical MHC class II" (MHC-IIa) that includes H-2A (LA), H-2E (I-E) and H-2P subclasses, and the "non-classical MHC class II" (MHC-IIb) comprises H-2M and H-2O. The mouse MHC can be further classified into haplotypes that designated by a small letter (e.g., a, b, d, k, q, s, etc.). In some embodiments, the mouse MHC comprises H-2Dd, H-2Kd, H-2Ld, H-2Qa, H-2Qb, H-2Ad (I- Ad), H-2Ed (I-Ed), H-2Db, H-2Kb, H-2Ab (I-Ab), H-2Dk, H-2Kk, H-2Ak (I-Ak), H-2Ek (I-Ek), H-2Dp, H-2Kp, H-2Lp, H-2Ap (I-Ap), H-2Ep (I-Ep), H-2Dq, H-2Kq, H-2Lq, H-2Aq (I-Aq), H- 2Eq (I-Eq), H-2Db, H-2Kb, H-2Ab (I-Ab), H-2Ds, H-2Dw3, H-2Kj, H-2jA (I-Aj), H-2Ej (I-Ej), H-2Af (I-Af), H-2Ag7 (I-Ag7), H-2Dz, H-2Ku, H-2Lz, H-2Au (I- Au), H-2Eu (I-Eu), H-2Dr, H- 2Kr, H-2Lr, H-2Ar (I-Ar), H-2Er (I-Er), H-2Ds, H-2Ks, H-2Ls, H-2As (I-As), H-2Dv, H-2Kv, H-2Lv, H-2Av (I-Av), or H-2Ev (I-Ev). In some embodiments, the mouse MHC is H-2Kd, H- 2Db, or I-Ab.

[0110] In some embodiments, the antigen presentation polypeptide(s) comprises an amino acid sequence having at least 65%, 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% sequence identity to an amino acid sequence selected from SEQ ID NOs: 53-54, 57-58, 61-62, 81-86, 112-113, 120-121, 144-145, and 152-153, as listed in Table 2 below.Table 2: Exemplary antigen presentation polypeptides[OHl] In some embodiments, the antigen presentation polypeptide comprises at least one mutation. In some embodiment, the mutation is an addition, a deletion, or a substitution. In some embodiments, the mutation is a point mutation. In some embodiments, the mutation is at positions equivalent to Y84 and / or A139 of HLA-A. In some embodiments, the mutation is Y84A, Y84C, and / or A139C.The Linker

[0112] The APC can comprise one or more linkers. The one or more linkers can comprise one or more flexible amino acid residues, optionally about 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 30, 35, 40, 50, or a number or a range between any twoof these values, flexible amino acid residues, further optionally the flexible amino acid residues comprise glycine, serine, or a combination thereof. The one or more linkers can be a glycineserine (GS) linker, optionally 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 30, 35, 40, 50, or a number or a range between any two of these values, amino acids in length. In some embodiments, the linker comprises no more than 25 amino acids. In some embodiments, the linkers is about 1, 2, 3, 4, 5, 6, 7, 8, 9, 11, 12, 15, 20, 25, amino acids in length.

[0113] The one or more linkers can be situated between the APC-assembly domain and the presenting peptide, between the APC-assembly domain and the EPM, between the APC- assembly domain and the antigen presentation polypeptide, between the EPM and the antigen presentation polypeptide, between the presenting peptide and the EPM, and / or between the presenting peptide and the antigen presentation polypeptide.

[0114] In some embodiments, the linker is a flexible linker. In some embodiments, the flexible linker is a G / S-rich linker. In some embodiments, the flexible linker is a peptide (G / S)n. In some embodiments, n is a position integer that is smaller than 21. In some embodiments, the linker is, or comprises, one or more of GSGSGSG (SEQ ID NO: 1), GGGGS (SEQ ID NO: 2), GSGSG (SEQ ID NO: 3), GGGG (SEQ ID NO: 4), GGG, GG, GS, GSGS (SEQ ID NO: 8), GGGS (SEQ ID NO: 9), GGS, GTS, GGSGGS (SEQ ID NO: 12), GGG, GGGGGG (SEQ ID NO: 14), GGGGGGGGG (SEQ ID NO: 15), GGGGGGGGGGGG (SEQ ID NO: 16), GGGGGGGGGGGGGGG (SEQ ID NO: 17), GGS, GGSGGS (SEQ ID NO: 19), GGSGGSGGS (SEQ ID NO: 20), GGSGGSGGSGGS (SEQ ID NO: 21), GGSGGSGGSGGSGGS (SEQ ID NO: 22), GSG, GSGGSG (SEQ ID NO: 24), GSGGSGGSG (SEQ ID NO: 25), GSGGSGGSGGSG (SEQ ID NO: 26), GS GGS GGS GGS GGS G (SEQ ID NO: 27), (GGGGS)n (SEQ ID NO: 28), GGGGSGGGGS (SEQ ID NO: 29), GGGGSGGGGSGGGGS (SEQ ID NO: 30), GGGGSGGGGSGGGGSGGGGS (SEQ ID NO: 31), and GGGGS GGGGS GGGGS GGGGS GGGGS (SEQ ID NO: 32). In some embodiments, the linker is, or comprises, GGGGS (SEQ ID NO: 2), and / or GGGS (SEQ ID NO: 9). In some embodiments, the linker is, or comprises, n GGGGS (SEQ ID NO: 2) or GGGS (SEQ ID NO: 9). In some embodiments, n is an integer from 1 to 10, optionally n is 3 or 4. In some embodiments, the linker is, or comprises GGGGSGGGGSGGGGS (SEQ ID NO: 30), and / or GGGGSGGGGSGGGGSGGGGS (SEQ ID NO: 31).The Presentins Peptide

[0115] The presenting peptides, or a portion thereof, presented on the APVs herein described can be displayed on its surface. Alternatively, the presenting peptide presented on the APVs herein described can be partially encapsulated or embedded such that at least an immunogenic portion of the presenting peptide is exposed and accessible by an immune cellreceptor so as to induce an immune response. The presenting peptide, or a portion thereof, can be displayed in and / or on the surface of the APV. The presenting peptide can be about 1 to about 10000 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25,26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51,52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77,78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 200, 300,400, 500, 600, 700, 800, 900, 1000, 2000, 3000, 4000, 5000, 6000, 7000, 8000, 9000, 10000, or a number or a range between any of these values) amino acids in length. In some embodiments, the presenting peptide is 5-20 amino acids in length.

[0116] The presenting peptide can comprise or can be derived from an antigenic protein associated with a disease or disorder, optionally an immunogenic variant and / or an immunogenic fragment of said antigenic protein. The presenting peptide can comprise or be derived from at least a portion of an antigenic protein. The presenting peptide can comprise or can be derived from a conserved portion of said antigenic protein. The presenting peptide can be present on and / or in the APV in its natural membrane-associated conformation. The presenting peptide can comprise or can be derived from at least about 5 percent (e.g., 5%, 6%, 7%, 8%, 9%, 10%, 11%, 12%, 13%, 14%, 15%, 16%, 17%, 18%, 19%, 20%, 21%, 22%, 23%, 24%, 25%,26%, 27%, 28%, 29%, 30%, 31%, 32%, 33%, 34%, 35%, 36%, 37%, 38%, 39%, 40%, 41%,42%, 43%, 44%, 45%, 46%, 47%, 48%, 49%, 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%,58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%,74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%,90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 100%, or a number or a range between any two of these values) of the full length of said antigenic protein. The presenting peptide can comprise a membrane protein. In some embodiments, the presenting peptide is not configured to be a soluble protein. In some embodiments, the presenting peptide does not comprise one or more mutations configured to enhance its solubility and / or stability. In some embodiments, the presenting peptide is present on and / or in the APV in its natural membrane- associated conformation. In some embodiments, antigenic proteins / peptides provided herein can be intra-cellular, membrane bound or extra-cellular.

[0117] Accordingly, the presenting peptides can contain amino acid substitutions relative to the antigenic proteins disclosed herein. Any amino acid substitution is permissible so long as the immunogenic activity of the protein is not significantly altered (e.g., at most 10%, 20%, 30%, 40% or 50% decrease relative to the coronavirus protein antigens disclosed herein) and the variants retain the desired activity. Preferred variants typically contains substitutions with one or more amino acids substituted with their functional equivalents. In someembodiments, the presenting peptide does not comprise a transmembrane domain and / or is a soluble protein, and the APC comprises a transmembrane domain.

[0118] In some embodiments, the presenting peptide is derived from one or more of MART-1; NYESO1; neuropilin (NRP); IGRP; CD19; CD123; CD22; CD30; CD171; CS-1 (also referred to as CD2 subset 1, CRACC, SLAMF7, CD319, and 19A24); C-type lectin-like molecule- 1 (CLL-1 or CLECL1); CD33; epidermal growth factor receptor variant III (EGFRvIII); ganglioside G2 (GD2); ganglioside GD3 (aNeu5Ac(2-8)aNeu5Ac(2-3)bDGalp(l- 4)bDGlcp(l-l)Cer); TNF receptor family member B cell maturation (BCMA); Tn antigen ((Tn Ag) or (GalNAca-Ser / Thr)); prostate-specific membrane antigen (PSMA); Receptor tyrosine kinase-like orphan receptor 1 (ROR1); Fms-Like Tyrosine Kinase 3 (FLT3); Tumor-associated glycoprotein 72 (TAG72); CD38; CD44v6; Carcinoembryonic antigen (CEA); Epithelial cell adhesion molecule (EPCAM); B7H3 (CD276); KIT (CD117); Interleukin- 13 receptor subunit alpha-2 (IL-13Ra2 or CD213A2); Mesothelin; Interleukin 11 receptor alpha (IL-l lRa); prostate stem cell antigen (PSCA); Protease Serine 21 (Testisin or PRSS21); vascular endothelial growth factor receptor 2 (VEGFR2); Lewis(Y) antigen; CD24; Platelet-derived growth factor receptor beta (PDGFR-beta); Stage-specific embryonic antigen-4 (S SEA-4); CD20; Folate receptor alpha; Receptor tyrosine-protein kinase ERBB2 (Her2 / neu); Mucin 1, cell surface associated (MUC1); epidermal growth factor receptor (EGFR); neural cell adhesion molecule (NCAM); Prostase; prostatic acid phosphatase (PAP); elongation factor 2 mutated (ELF2M); Ephrin B2; fibroblast activation protein alpha (FAP); insulin-like growth factor 1 receptor (IGF -I receptor), carbonic anhydrase IX (CAIX); Proteasome (Prosome, Macropain) Subunit, Beta Type, 9 (LMP2); glycoprotein 100 (gplOO); oncogene fusion protein consisting of breakpoint cluster region (BCR) and Abelson murine leukemia viral oncogene homolog 1 (Abl) (bcr-abl); tyrosinase; ephrin type-A receptor 2 (EphA2); Fucosyl GM1; sialyl Lewis adhesion molecule (sLe); ganglioside GM3 (aNeu5Ac(2-3)bDGalp(l-4)bDGlcp(l-l)Cer); transglutaminase 5 (TGS5); high molecular weight-melanoma-associated antigen (HMWMAA); o-acetyl-GD2 ganglioside (OAcGD2); Folate receptor beta; tumor endothelial marker 1 (TEM1 / CD248); tumor endothelial marker 7-related (TEM7R); claudin 6 (CLDN6); thyroid stimulating hormone receptor (TSHR); G protein-coupled receptor class C group 5, member D (GPRC5D); chromosome X open reading frame 61 (CXORF61); CD97; CD179a; anaplastic lymphoma kinase (ALK); Poly sialic acid; placenta-specific 1 (PLAC1); hexasaccharide portion of globoH glycoceramide (GloboH); mammary gland differentiation antigen (NY-BR-1); uroplakin 2 (UPK2); Hepatitis A virus cellular receptor 1 (HAVCR1); adrenoceptor beta 3 (ADRB3); pannexin 3 (PANX3); G protein-coupled receptor 20 (GPR20); lymphocyte antigen 6 complex, locus K 9 (LY6K); Olfactory receptor 51E2 (OR51E2); TCR Gamma Alternate Reading FrameProtein (TARP); Wilms tumor protein (WT1); Cancer / testis antigen 1 (NY-ESO-1); Cancer / testis antigen 2 (LAGE-la); Melanoma-associated antigen 1 (MAGE-A1); ETS translocation-variant gene 6, located on chromosome 12p (ETV6-AML); sperm protein 17 (SPA17); X Antigen Family, Member 1A (XAGE1); angiopoietin-binding cell surface receptor 2 (Tie 2); melanoma cancer testis antigen-1 (MAD-CT-1); melanoma cancer testis antigen-2 (MAD-CT-2); Fos-related antigen 1; tumor protein p53 (p53); p53 mutant; prostein; survivin; telomerase; prostate carcinoma tumor antigen- 1 (PCTA-1 or Galectin 8), melanoma antigen recognized by T cells 1 (MelanA or MARTI); Rat sarcoma (Ras) mutant; human Telomerase reverse transcriptase (hTERT); sarcoma translocation breakpoints; melanoma inhibitor of apoptosis (ML-IAP); ERG (transmembrane protease, serine 2 (TMPRSS2) ETS fusion gene); N- Acetyl glucosaminyl-transferase V (NA17); paired box protein Pax-3 (PAX3); Androgen receptor; Cyclin Bl; v-myc avian myelocytomatosis viral oncogene neuroblastoma derived homolog (MYCN); Ras Homolog Family Member C (RhoC); Tyrosinase-related protein 2 (TRP-2); Cytochrome P450 1B1 (CYP1B1); CCCTC-Binding Factor (Zinc Finger Protein)-Like (BORIS or Brother of the Regulator of Imprinted Sites), Squamous Cell Carcinoma Antigen Recognized By T Cells 3 (SART3); Paired box protein Pax-5 (PAX5); proacrosin binding protein sp32 (OY-TES1); lymphocyte-specific protein tyrosine kinase (LCK); A kinase anchor protein 4 (AKAP-4); synovial sarcoma, X breakpoint 2 (SSX2); Receptor for Advanced Glycation Endproducts (RAGE-1); renal ubiquitous 1 (RU1); renal ubiquitous 2 (RU2); legumain; human papilloma virus E6 (HPV E6); human papilloma virus E7 (HPV E7); intestinal carboxyl esterase; heat shock protein 70-2 mutated (mut hsp70-2); CD79a; CD79b; CD72; Leukocyte-associated immunoglobulin-like receptor 1 (LAIR1); Fc fragment of IgA receptor (FCAR or CD89); Leukocyte immunoglobulin-like receptor subfamily A member 2 (LILRA2); CD300 molecule-like family member f (CD300LF); C-type lectin domain family 12 member A (CLEC12A); bone marrow stromal cell antigen 2 (BST2); EGF-like module-containing mucinlike hormone receptor-like 2 (EMR2); lymphocyte antigen 75 (LY75); Glypican-3 (GPC3); Fc receptor-like 5 (FCRL5); and immunoglobulin lambda-like polypeptide 1 (IGLL1).

[0119] In some embodiments, the presenting peptide comprise the nucleotide sequence of any one of SEQ ID NOs: 184-266 or a sequence that is at least 80%, 85%, 90%, 95%, 98%, 99%, or 100% identical to any one of SEQ ID NOs: 184-266. The sequences of exemplary presenting peptides are in Table 3 below.Table 3: Exemplary presenting peptidesPathogenic Antisens

[0120] The presenting peptide can comprise or can be derived from the full-length surface protein of an infectious agent. The disease or disorder can be an infectious disease or disorder caused by an infectious agent, the presenting peptide can comprise or can be derived from an antigenic protein of said infectious agent, and the antigenic protein of said infectious agent can be a pathogenic antigen. In some embodiments, the pathogenic antigen is selected from: Outer membrane protein A OmpA, biofilm associated protein Bap, transport protein MucK (Acinetobacter baumannii, Acinetobacter infections)); variable surface glycoprotein VSG, microtubule-associated protein MAPP15, trans-sialidase TSA (Trypanosoma briicen African sleeping sickness (African trypanosomiasis)); HIV p24 antigen, HIV envelope proteins (Gpl20, Gp41, Gpl60), polyprotein GAG, negative factor protein Nef, trans-activator oftranscription Tat (HIV (Human immunodeficiency virus), AIDS (Acquired immunodeficiency syndrome)); galactose-inhibitable adherence protein GIAP, 29 kDa antigen Eh29, Gal / GalNAc lectin, protein CRT, 125 kDa immunodominant antigen, protein M17, adhesin ADH112, protein STIRP (Entamoeba histolytica, Amoebiasis); Major surface proteins 1-5 (MSP la, MSP lb, MSP2, MSP3, MSP4, MSP5), type IV secreotion system proteins (VirB2, VirB7, VirBl l, VirD4) (Anaplasma genus, Anaplasmosis); protective Antigen PA, edema factor EF, lethal facotor LF, the S-layer homology proteins SLH (Bacillus anlhracis. Anthrax); acranolysin, phospholipase D, collagen-binding protein CbpA (Arcanobacterium haemolyticum, Arcanobacterium haemolyticum infection); nucleocapsid protein NP, glycoprotein precursor GPC, glycoprotein GP1, glycoprotein GP2 (Junin virus, Argentine hemorrhagic fever); chitinprotein layer proteins, 14 kDa suarface antigen A14, major sperm protein MSP, MSP polymerization-organizing protein MPOP, MSP fiber protein 2 MFP2, MSP polymerizationactivating kinase MPAK, ABA-l-like protein ALB, protein ABA-1, cuticulin CUT-1 (Ascaris lumbricoides, Ascariasis); 41 kDa allergen Asp vl3, allergen Asp f3, major coni dial surface protein rodlet A, protease Pep Ip, GPI-anchored protein Gel Ip, GPI-anchored protein Crap (Aspergillus genus, Aspergillosis); family VP26 protein, VP29 protein (Astroviridae, Astrovirus infection); Rhoptry-associated protein 1 RAP-1, merozoite surface antigens MSA-1, MSA-2 (al, a2, c), 12D3, 1105, 21134, P29, variant erythrocyte surface antigen VESA1, Apical Membrane Antigen 1 AMA-1 (Babesia genus, Babesiosis); hemolysin, enterotoxin C, PX01-51, glycolate oxidase, ABC-transporter, penicillin-bingdn protein, zinc transporter family protein, pseudouridine synthase Rsu, plasmid replication protein RepX, oligoendopeptidase F, prophage membrane protein, protein HemK, flagellar antigen H, 28.5-kDa cell surface antigen (Bacillus cereus, Bacillus cereus infection); large T antigen LT, small T antigen, capsid protein VP1, capsid protein VP2 (BK virus, BK virus infection); 29 kDa-protein, caspase-3 -like antigens, glycoproteins (Blastocystis hominis, Blastocystis hominis infection); yeast surface adhesin WI-1 (Blastomyces dermatitidis, Blastomycosis); nucleoprotein N, polymerase L, matrix protein Z, glycoprotein GP (Machupo virus, Bolivian hemorrhagic fever); outer surface protein A OspA, outer surface protein OspB, outer surface protein OspC, decorin binding protein A DbpA, decorin binding protein B DbpB, flagellar filament 41 kDa core protein Fla, basic membrane protein A precursor Bmp A (Immunodominant antigen P39), outer surface 22 kDa lipoprotein precursor (antigen IPLA7), variable surface lipoprotein vlsE (Borrelia genus, Borrelia infection); Botulinum neurotoxins BoNT / Al, BoNT / A2, BoNT / A3, BoNT / B, BoNT / C, BoNT / D, BoNTZE, BoNT / F, BoNT / G, recombinant botulinum toxin F He domain FHc (Clostridium botulinum, Botulism (and Infant botulism)); nucleocapsid, glycoprotein precursor (Sabia virus, Brazilian hemorrhagic fever); copper / Zinc superoxide dismutase SodC,bacterioferritin Bfr, 50S ribosomal protein RplL, OmpA-like transmembrane domain-containing protein 0mp31, immunogenic 39-kDa protein M5 P39, zinc ABC transporter periplasmic zinc- bnding protein znuA, periplasmic immunogenic protein Bp26, 30S ribosomal protein S12 RpsL, glyceraldehyde-3 -phosphate dehydrogenase Gap, 25 kDa outer-membrane immunogenic protein precursor Omp25, invasion protein B lalB, trigger factor Tig, molecular chaperone DnaK, putative peptidyl-prolyl cis-trans isomerase SurA, lipoprotein 0mpl9, outer membrane protein MotY 0mpl6, conserved outer membrane protein DI 5, malate dehydrogenase Mdh, component of the Type-IV secretion system (TOSS) VirJ, lipoprotein of unknown function BAB1 0187 (Brucella genus, Brucellosis); members of the ABC transporter family (LoIC, OppA, and PotF), putative lipoprotein releasing system transmembrane protein LoICZE, flagellin FliC, Burkholderia intracellular motility A BimA, bacterial Elongation factor-Tu EF-Tu, 17 kDa OmpA-like protein, boaA coding protein, boaB coding protein (Burkholderia cepacia and other Burkholderia species, Burkholderia infection); mycolyl-transferase Ag85A, heat-shock protein Hsp65, protein TB10.4, 19 kDa antigen, protein PstS3, heat-shock protein Hsp70 (Mycobacterium ulcerous. Buruli ulcer); norovirus major and minor viral capsid proteins VP1 and VP2, genome polyprotein, Sapoviurus capsid protein VP1, protein Vp3, geome polyprotein (Caliciviridae family, Calicivirus infection (Norovirus and Sapovirus)); major outer membrane protein PorA, flagellin FlaA, surface antigen CjaA, fibronectin binding protein CadF, aspartate / glutamate-binding ABC transporter protein PeblA, protein FspAl, protein FspA2 (Campylobacter genus, Campylobacteriosis); glycolytic enzyme enolase, secreted aspartyl proteinases SAP1-10, glycophosphatidylinositol (GPI)-linked cell wall protein, protein Hyrl, complement receptor 3-related protein CR3-RP, adhesin Als3p, heat shock protein 90 kDa hsp90, cell surface hydrophobicity protein CSH (usually Candida albicans and other Candida species, Candidiasis); 17-kDa antigen, protein P26, trimeric autotransporter adhesins TAAs, Bartonella adhesin A BadA, variably expressed outer-membrane proteins Vomps, protein Pap3, protein HbpA, envelope-associated protease HtrA, protein OMP89, protein GroEL, protein LalB, protein OMP43, dihydrolipoamide succinyltransferase SucB (Bartonella henselae, Catscratch disease); amastigote surface protein-2, amastigote-specific surface protein SSP4, cruzipain, trans-sialidase TS, trypomastigote surface glycoprotein TSA-1, complement regulatory protein CRP-10, protein G4, protein G2, paraxonemal rod protein PAR2, paraflagellar rod component Part, mucin-Associated Surface Proteins MPSP (Trypanosoma cruzi, Chagas Disease (American trypanosomiasis)); envelope glycoproteins (gB, gC, gE, gH, gl, gK, gL) (Varicella zoster virus (VZV), Chickenpox); major outer membrane protein MOMP, probable outer membrane protein PMPC, outer membrane complex protein B OmcB, heat shock proteins Hsp60 HSP10, protein IncA, proteins from the type III secretion system, ribonucleotidereductase small chain protein NrdB, plasmid protein Pgp3, chlamydial outer protein N CopN, antigen CT521, antigen CT425, antigen CT043, antigen TC0052, antigen TC0189, antigen TC0582, antigen TC0660, antigen TC0726, antigen TC0816, antigen TC0828 (Chlamydia trachomatis, Chlamydia),' low calcium response protein E LCrE, chlamydial outer protein N CopN, serine / threonine-protein kinase PknD, acyl-carrier-protein S-malonyltransferase FabD, single-stranded DNA-binding protein Ssb, major outer membrane protein MOMP, outer membrane protein 2 0mp2, polymorphic membrane protein family (Pmpl, Pmp2, Pmp3, Pmp4, Pmp5, Pmp6, Pmp7, Pmp8, Pmp9, PmplO, Pmpl l, Pmpl2, Pmpl3, Pmpl4, Pmpl5, Pmpl6, Pmpl 7, Pmpl 8, Pmpl 9, Pmp20, Pmp21) (Chlamydophila pneumoniae, Chlamydophila pneumoniae infection); cholera toxin B CTB, toxin coregulated pilin A TcpA, toxin coregulated pilin TcpF, toxin co-regulated pilus biosynthesis ptrotein F TcpF, cholera enterotoxin subunit A, cholera enterotoxin subunit B, Heat-stable enterotoxin ST, mannose-sensitive hemagglutinin MSHA, outer membrane protein U Porin ompU, Poring B protein, polymorphic membrane protein-D (Vibrio cholerae, Cholera); propionyl-CoA carboxylase PCC, 14-3-3 protein, prohibitin, cysteine proteases, glutathione transferases, gelsolin, cathepsin L proteinase CatL, Tegumental Protein 20.8 kDa TP20.8, tegumental protein 31.8 kDa TP31.8, lysophosphatidic acid phosphatase LPAP, (Clonorchis sinensis, Cl onor chiasis); surface layer proteins SLPs, glutamate dehydrogenase antigen GDH, toxin A, toxin B, cysteine protease Cwp84, cysteine protease Cwpl3, cysteine protease Cwpl9, Cell Wall Protein CwpV, flagellar protein FliC, flagellar protein FliD (Clostridium difficile, Clostridium difficile infection); rhinoviruses: capsid proteins VP1, VP2, VP3, VP4; coronaviruses: sprike proteins S, envelope proteins E, membrane proteins M, nucleocapsid proteins N (usually rhinoviruses and coronaviruses, Common cold (Acute viral rhinopharyngitis; Acute coryza)); prion protein Prp (CJD prion, Creutzfeldt-Jakob disease (CJD)); envelope protein Gc, envelope protein Gn, nucleocapsid proteins (Crimean- Congo hemorrhagic fever virus, Crimean-Congo hemorrhagic fever (CCHF)); virulence- associated DEAD-box RNA helicase VAD1, galactoxylomannan-protein GalXM, glucuronoxylomannan GXM, mannoprotein MP (Cryptococcus neoformans, Cryptococcosis); acidic ribosomal protein P2 CpP2, mucin antigens Mucl, Muc2, Muc3 Muc4, Muc5, Muc6, Muc7, surface adherence protein CP20, surface adherence protein CP23, surface protein CP 12, surface protein CP21, surface protein CP40, surface protein CP60, surface protein CP 15, surface-associated glycopeptides gp40, surface-associated glycopeptides gpl5, oocyst wall protein AB, profilin PRF, apyrase (Cryptosporidium genus, Cryptosporidiosis); fatty acid and retinol binding protein-1 FAR-1, tissue inhibitor of metalloproteinase TIMP (TMP), cysteine proteinase ACEY-1, cysteine proteinase ACCP-1, surface antigen Ac- 16, secreted protein 2 ASP-2, metalloprotease 1 MTP-1, aspartyl protease inhibitor API-1, surface-associated antigenSAA-1, adult-specific secreted factor Xa serine protease inhibitor anticoagulant AP, cathepsin D-like aspartic protease ARR-1 (usually Ancylostoma braziliense: multiple other parasites, Cutaneous larva migrans (CLM)); cathepsin L-like proteases, 53 / 25-kDa antigen, 8 kDa family members, cysticercus protein with a marginal trypsin-like activity TsAg5, oncosphere protein TSOL18, oncosphere protein TSOL45-1A, lactate dehydrogenase A LDHA, lactate dehydrogenase B LDHB (Taenia solium, Cysticercosis); pp65 antigen, membrane protein ppi 5, capsid-proximal tegument protein ppi 50, protein M45, DNA polymerase UL54, helicase UL105, glycoprotein gM, glycoprotein gN, glcoprotein H, glycoprotein B gB, protein UL83, protein UL94, protein UL99 (Cytomegalovirus (CMV), Cytomegalovirus infection); capsid protein C, premembrane protein prM, membrane protein M, envelope protein E (domain I, domain II, domain II), protein NS1, protein NS2A, protein NS2B, protein NS3, protein NS4A, protein 2K, protein NS4B, protein NS5 (Dengue viruses (DEN-1, DEN-2, DEN-3 and DEN-4)- Flaviviruses, Dengue fever); 39 kDa protein (Dientamoeba fragilis, Dientamoebiasis); diphtheria toxin precursor Tox, diphteria toxin DT, pilin-specific sortase SrtA, shaft pilin protein SpaA, tip pilin protein SpaC, minor pilin protein SpaB, surface-associated protein DIP1281 (Corynebacterium diphlheriae. Diphtheria); glycoprotein GP, nucleoprotein NP, minor matrix protein VP24, major matrix protein VP40, transcription activator VP30, polymerase cofactor VP35, RNA polymerase L (Ebolavirus (EBOV), Ebola hemorrhagic fever); prion protein (vCJD prion, Variant Creutzfeldt-Jakob disease (vCJD, nvCJD)); UvrABC system protein B, protein Flpl, protein Flp2, protein Flp3, protein TadA, hemoglobin receptor HgbA, outer membrane protein TdhA, protein CpsRA, regulator CpxR, protein Sap A, 18 kDa antigen, outer membrane protein NcaA, protein LspA, protein LspAl, protein LspA2, protein LspB, outer membrane component DsrA, lectin DItA, lipoprotein Hip, major outer membrane protein OMP, outer membrane protein 0mpA2 Haemophilus ducreyi, Chancroid); aspartyl protease 1 Pepl, phospholipase B PLB, alpha-mannosidase 1 AMN1, glucanosyltransferase GEL1, urease URE, peroxisomal matrix protein Pmpl, proline-rich antigen Pra, humal T-cell reative protein TcrP (Coccidioides immitis and Coccidioides posadasii, Coccidioidomycosis); allergen Tri r 2, heat shock protein 60 Hsp60, fungal actin Act, antigen Tri r2, antigen Tri r4, antigen Tri tl, protein IV, glycerol-3 -phosphate dehydrogenase Gpdl, osmosensor HwShol A, osmosensor HwSholB, histidine kinase HwHhk7B, allergen Mala s 1, allergen Mala s 11, thioredoxin Trx Mala s 13, allergen Mala f, allergen Mala s (usually Trichophyton spp, Epidermophyton spp., Malassezia spp., Hortaea werneckii, Dermatophytosis); protein EG95, protein EG10, protein EG18, protein EgA31, protein EM18, antigen EPCI, antigen B, antigen 5, protein P29, protein 14-3-3, 8-kDa protein, myophilin, heat shock protein 20 HSP20, glycoprotein GP-89, fatty acid binding protein FAPB (Echinococcus genus, Echinococcosis); major surface protein 2 MSP2, major surfaceprotein 4 MSP4, MSP variant SGV1, MSP variant SGV2, outer membrane protein OMP, outer membrande protein 19 OMP- 19, major antigenic protein MAPI, major antigenic protein MAP1- 2, major antigenic protein MAP1B, major antigenic protein MAPI-3, Erum2510 coding protein, protein GroEL, protein GroES, 30-kDA major outer membrane proteins, GE 100-kDa protein, GE 130-kDa protein, GE 160-kDa protein (Ehrlichia genus, Ehrlichiosis); secreted antigen SagA, sagA-like proteins Sal A and SalB, collagen adhesin Scm, surface proteins Fmsl (EbpA(fm), Fms5 (EbpB(fm), Fms9 (EpbC(fm) and FmslO, protein EbpC(fm), 96 kDa immunoprotective glycoprotein G1 (Enterococcus genus, Enterococcus infection); genome polyprotein, polymerase 3D, viral capsid protein VP1, viral capsid protein VP2, viral capsid protein VP3, viral capsid protein VP4, protease 2 A, protease 3C (Enterovirus genus, Enterovirus infection); outer membrane proteins OM, 60 kDa outer membrane protein, cell surface antigen OmpA, cell surface antigen OmpB (sca5), 134 kDa outer membrane protein, 31 kDa outer membrane protein, 29.5 kDa outer membrane protein, cell surface protein SCA4, cell surface protein Adri (RP827), cell surface protein Adr2 (RP828), cell surface protein SCA1, Invasion protein invA, cell division protein fts, secretion proteins sec Ofamily, virulence proteins virB, tlyA, tlyC, parvulin-like protein Pip, preprotein translocase SecA, 120-kDa surface protein antigen SPA, 138 kD complex antigen, major 100-kD protein (protein I), intracytoplasmic protein D, protective surface protein antigen SPA (Rickettsia prowazekii, Epidemic typhus); Epstein-Barr nuclear antigens (EBNA-1, EBNA-2, EBNA-3A, EBNA-3B, EBNA-3C, EBNA- leader protein (EBNA-LP)), latent membrane proteins (LMP-1, LMP-2A, LMP-2B), early antigen EBV-EA, membrane antigen EBV-MA, viral capsid antigen EBV-VCA, alkaline nuclease EBV-AN, glycoprotein glycoprotein gp350, glycoprotein gpl lO, glycoprotein gp42, glycoprotein gHgL, glycoprotein gB (Epstein-Barr Virus (EBV), Epstein-Barr Virus Infectious Mononucleosis); cpasid protein VP2, capsid protein VP1, major protein NS1 (Parvovirus B19, Erythema infectiosum (Fifth disease)); pp65 antigen, glycoprotein 105, major capsid protein, envelope glycoprotein H, protein U51 (Human herpesvirus 6 (HHV-6) and Human herpesvirus 7 (HHV-7), Exanthem subitum); thioredoxin-glutathione reductase TGR, cathepsins LI and L2, Kunitz-type protein KTM, leucine aminopeptidase LAP, cysteine proteinase Fast, saposin-like protein-2 SAP-2, thioredoxin peroxidases TPx, Prx-1, Prx-2, cathepsin I cysteine proteinase CL3, protease cathepsin L CL1, phosphoglycerate kinase PGK, 27-kDa secretory protein, 60 kDa protein HSP35alpha, glutathione transferase GST, 28.5 kDa tegumental antigen 28.5 kDa TA, cathepsin B3 protease CatB3, Type I cystatin stefin-1, cathepsin L5, cathepsin Llg and cathepsin B, fatty acid binding protein FABP, leucine aminopeptidases LAP (Fasciola hepatica and Fasciola giganlica. Fasciolosis); prion protein (FFI prion, Fatal familial insomnia (FFI)); venom allergen homolog-like protein VAL-1, abundant larval transcript ALT-1, abundant larvaltranscript ALT-2, thioredoxin peroxidase TPX, vespid allergen homologue VAH, thiordoxin peroxidase 2 TPX-2, antigenic protein SXP (peptides N, Nl, N2, and N3), activation associated protein-1 ASP-1, Thioredoxin TRX, transglutaminase BmTGA, glutathione-S-transferases GST, myosin, vespid allergen homologue VAH, 175 kDa collagenase, glyceraldehyde-3 -phosphate dehydrogenase GAPDH, cuticular collagen Col-4, secreted larval acidic proteins SLAPs, chitinase CHI-1, maltose binding protein MBP, glycolytic enzyme fructose- 1,6-bisphosphate aldolase Fba, tropomyosin TMY-1, nematode specific gene product OvB20, onchocy statin CPI- 2, Cox-2 (Filarioidea superfamily, Filariasis); phospholipase C PLC, heat-labile enterotoxin B, Iota toxin component lb, protein CPE1281 pyruvate ferredoxin oxidoreductase, elongation factor G EF-G, perfringolysin O Pfo, glyceraldehyde-3 -phosphate dehydrogenase GapC, Fructose-bisphosphate aldolase Alf2, Clostridium perfringens enterotoxin CPE, alpha toxin AT, alpha toxoid ATd, epsilon-toxoid ETd, protein HP, large cytotoxin TpeL, endo-beta-N- acetylglucosaminidase Naglu, phosphoglyceromutase Pgm (Clostridium perfringens, Food poisoning by Clostridium perfringens),' leukotoxin IktA, adhesion FadA, outer membrane protein RadD, high-molecular weight arginine-binding protein (Fusobacterium genus, Fusobacterium infection); phospholipase C PLC, heat-labile enterotoxin B, Iota toxin component lb, protein CPE1281, pyruvate ferredoxin oxidoreductase, elongation factor G EF-G, perfringolysin 0 Pfo, glyceraldehyde-3 -phosphate dehydrogenase GapC, fructose-bisphosphate aldolase Alf2, Clostridium perfringens enterotoxin CPE, alpha toxin AT, alpha toxoid ATd, epsilon-toxoid ETd, protein HP, large cytotoxin TpeL, endo-beta-N-acetylglucosaminidase Naglu, phosphoglyceromutase Pgm (usually Clostridium perfringens,' other Clostridium species, Gas gangrene (Clostridial myonecrosis)); lipase A, lipase B, peroxidase Decl (Geotrichum candidum, Geotrichosis); prion protein (GSS prion, Gerstmann-Straussler-Scheinker syndrome (GSS)); cyst wall proteins CWP1, CWP2, CWP3, variant surface protein VSP, VSP1, VSP2, VSP3, VSP4, VSP5, VSP6, 56 kDa antigen, pyruvate ferredoxin oxidoreductase PFOR, alcohol dehydrogenase E ADHE, alpha-giardin, alpha8-giardin, alphal-guiardin, beta-giardin, cystein proteases, glutathione-S-transferase GST, arginine deiminase ADI, fructose- 1,6-bisphosphat aldolase FBA, Giardia trophozoite antigens GTA (GTA1, GTA2), ornithine carboxyl transferase OCT, striated fiber-asseblin-like protein SALP, uridine phosphoryl-like protein UPL, alphatubulin, beta-tubulin (Giardia intestinalis, Giardiasis); members of the ABC transporter family (LoIC, OppA, and PotF), putative lipoprotein releasing system transmembrane protein LoICZE, flagellin FliC, Burkholderia intracellular motility A BimA, bacterial Elongation factor-Tu EF- Tu, 17 kDa OmpA-like protein, boaA coding protein (Burkholderia mallei, Glanders); cyclophilin CyP, 24 kDa third-stage larvae protien GS24, excretion-secretion products ESPs (40, 80, 120 and 208 kDa) (Gnathostoma spinigerum and Gnathostoma hispidum, Gnathostomiasis);pilin proteins, minor pilin-associated subunit pilC, major pilin subunit and variants pilE, pilS, phase variation protein porA, Porin B PorB, protein TraD, Neisserial outer membrane antigen H.8, 70 kDa antigen, major outer membrane protein PI, outer membrane proteins PIA and PIB, W antigen, surface protein A NspA, transferrin binding protein TbpA, transferrin binding protein TbpB PBP2, mtrR coding protein, ponA coding protein, membrane permease FbpBC, FbpABC protein system, LbpAB proteins, outer membrane protein Opa, outer membrane transporter FetA, iron-repressed regulator MpeR (Neisseria gonorrhoeae, Gonorrhea); outer membrane protein A OmpA, outer membrane protein C OmpC, outer membrane protein KI 7 0mpK17 (Klebsiella gramilomalis. Granuloma inguinale (Donovanosis)); fibronectin-binding protein Sfb, fibronectin / fibrinogen-binding protein FBP54, fibronectin-binding protein FbaA, M protein type 1 Emml, M protein type 6 Emm6, immunoglobulin-binding protein 35 Sib35, Surface protein R28 Spr28, superoxide dismutase SOD, C5a peptidase ScpA, antigen I / II Agl / II, adhesin AspA, G-related alpha2-macroglobulin-binding protein GRAB, surface fibrillar protein M5 (Streptococcus pyogenes, Group A streptococcal infection); C protein P antigen, arginine deiminase proteins, adhesin Bib A, 105 kDA protein BPS, surface antigens c, surface antigens R, surface antigens X, trypsin-resistant protein Rl, trypsin-resistant protein R3, trypsin-resistant protein R4, surface immunogenic protein Sip, surface protein Rib, Leucine-rich repeats protein LrrG, serine-rich repeat protein Srr-2, C protein alpha-antigen Bea, Beta antigen Bag, surface antigen Epsilon, alpha-like protein ALP1, alpha-like protein ALP5 surface antigen delta, alphalike protein ALP2, alpha-like protein ALP3, alpha-like protein ALP4, Cbeta protein Bac (Streptococcus agalacliae. Group B streptococcal infection); transferrin-binding protein 2 Tbp2, phosphatase P4, outer membrane protein P6, peptidoglycan-associated lipoprotein Pal, protein D, protein E, adherence and penetration protein Hap, outer membrane protein 26 Omp26, outer membrane protein P5 (Fimbrin), outer membrane protein DI 5, outer membrane protein OmpP2, 5 '-nucleotidase NucA, outer membrane protein Pl, outer membrane protein P2, outer membrane lipoprotein Pep, Lipoprotein E, outer membrane protein P4, fuculokinase FucK, [Cu,Zn]- superoxide dismutase SodC, protease HtrA, protein 0145, alpha-galactosylceramide Haemophilus influenzae, Haemophilus influenzae infection); polymerase 3D, viral capsid protein VP1, viral capsid protein VP2, viral capsid protein VP3, viral capsid protein VP4, protease 2 A, protease 3C (Enteroviruses, mainly Coxsackie A virus and Enterovirus 71 (EV71), Hand, foot and mouth disease (HFMD)); RNA polymerase L, protein L, glycoprotein Gn, glycoprotein Gc, nucleocapsid protein 5, envelope glycoprotein Gl, nucleoprotein NP, protein N, polyprotein M (Sin Nombre virus, Hantavirus, Hantavirus Pulmonary Syndrome (HPS)); heat shock protein HspA, heat shock protein HspB, citrate synthase GItA, protein UreB, heat shock protein Hsp60, neutrophil-activating protein NAP, catalase KatA, vacuolating cytotoxin VacA,urease alpha UreA, urease beta Ureb, protein CpnlO, protein groES, heat shock protein HsplO, protein MopB, cytotoxicity-associated 10 kDa protein CAG, 36 kDa antigen, beta-lactamase HcpA, Beta-lactamase HcpB (Helicobacter pylori, Helicobacter pylori infection); integral membrane proteins, aggregation-prone proteins, 0-antigen, toxin-antigens Stx2B, toxin-antigen StxlB, adhesion-antigen fragment Int28, protein EspA, protein EspB, Intimin, protein Tir, protein IntC300, protein Eae (Escherichia coli O157:H7, 0111 and 0104:H4, Hemolytic-uremic syndrome (HUS)); RNA polymerase L, protein L, glycoprotein Gn, glycoprotein Gc, nucleocapsid protein 5, envelope glycoprotein Gl, nucleoprotein NP, protein N, polyprotein M (Bunyaviridae family, Hemorrhagic fever with renal syndrome (HFRS)); glycoprotein G, matrix protein M, nucleoprotein N, fusion protein F, polymerase L, protein W, proteinC, phosphoprotein p, non- structural protein V (Henipavirus (Hendra virus Nipah virus), Henipavirus infections); polyprotein, glycoproten Gp2, hepatitis A surface antigen HBAg, protein 2 A, virus protein VP1, virus protein VP2, virus protein VP3, virus protein VP4, protein P1B, protein P2A, protein P3AB, protein P3D (Hepatitis A Virus, Hepatitis A); hepatitis B surface antigen HBsAg, Hepatitis B core antigen HbcAg, polymerase, protein Hbx, preS2 middle surface protein, surface protein L, large S protein, virus protein VP1, virus protein VP2, virus protein VP3, virus protein VP4 (Hepatitis B Virus (HBV), Hepatitis B); envelope glycoprotein El gp32 gp35 envelope glycoprotein E2 NS1 gp68 gp70, capsid protein C core protein Core, polyprotein, virus protein VP1, virus protein VP2, virus protein VP3, virus protein VP4, antigen G, protein NS3, protein NSSA, (Hepatitis C Virus, Hepatitis C); virus protein VP1, virus protein VP2, virus protein VP3, virus protein VP4, large hepaptitis delta antigen, small hepaptitis delta antigen (Hepatitis D Virus, Hepatitis D); virus protein VP1, virus protein VP2, virus protein VP3, virus protein VP4, capsid protein E2 (Hepatitis E Virus, Hepatitis E); glycoprotein L ULI, uracil-DNA glycosylase UL2, protein UL3, protein UL4, DNA replication protein UL5, portal protein UL6, virion maturation protein UL7, DNA helicase UL8, replication origin-binding protein UL9, glycoprotein M UL10, protein UL11, alkaline exonuclease ULI 2, serine-threonine protein kinase ULI 3, tegument protein ULI 4, terminase ULI 5, tegument protein ULI 6, protein ULI 7, capsid protein VP23 ULI 8, major capsid protein VP5 ULI 9, membrane protein UL20, tegument protein UL21, Glycoprotein H (UL22), Thymidine Kinase UL23, protein UL24, protein UL25, capsid protein P40 (UL26, VP24, VP22A), glycoprotein B (UL27), ICP18.5 protein (UL28), major DNA-binding protein ICP8 (UL29), DNA polymerase UL30, nuclear matrix protein UL31, envelope glycoprotein UL32, protein UL33, inner nuclear membrane protein UL34, capsid protein VP26 (UL35), large tegument protein UL36, capsid assembly protein UL37, VP19C protein (UL38), ribonucleotide reductase (Large subunit) UL39, ribonucleotide reductase (Small subunit) UL40, tegument protein / virion host shutoff VHSprotein (UL41), DNA polymerase processivity factor UL42, membrane protein UL43, glycoprotein C (UL44), membrane protein UL45, tegument proteins VP11 / 12 (UL46), tegument protein VP 13 / 14 (UL47), virion maturation protein VP 16 (UL48, Alpha- TIF), envelope protein UL49, dUTP diphosphatase UL50, tegument protein UL51, DNA helicase / primase complex protein UL52, glycoprotein K (UL53), transcriptional regulation protein 1E63 (ICP27, UL54), protein UL55, protein UL56, viral replication protein ICP22 (1E68, US1), protein U52, serine / threonine-protein kinase U53, glycoprotein G (U54), glycoprotein J (U55), glycoprotein D (U56), glycoprotein I (U57), glycoprotein E (U58), tegument protein U59, capsid / tegument protein US10, Vmw21 protein (US11), ICP47 protein (IE12, US12), major transcriptional activator ICP4 (1E175, RSI), E3 ubiquitin ligase ICPO (IE110), latency-related protein 1 LRP1, latency-related protein 2 LRP2, neurovirulence factor RL1 (ICP34.5), latency-associated transcript LAT (Herpes simplex virus 1 and 2 (HSV-1 and HSV-2), Herpes simplex); heat shock protein Hsp60, cell surface protein H1C, dipeptidyl peptidase type IV DppIV, M antigen, 70 kDa protein, 17 kDa histone-like protein (Histoplasma capsulatum, Histoplasmosis); fatty acid and retinol binding protein-1 FAR-1, tissue inhibitor of metalloproteinase TIMP (TMP), cysteine proteinase ACEY-1, cysteine proteinase ACCP-1, surface antigen Ac- 16, secreted protein 2 ASP-2, metalloprotease 1 MTP-1, aspartyl protease inhibitor API-1, surface-associated antigen SAA-1, surface-associated antigen SAA-2, adult-specific secreted factor Xa, serine protease inhibitor anticoagulant AP, cathepsin D-like aspartic protease ARR-1, 5-transferase GST, aspartic protease APR-1, acetylcholinesterase AChE (Ancylostoma duodena le and Necator americanus. Hookworm infection); protein NS1, protein NP1, protein VP1, protein VP2, protein VP3 (Human bocavirus (HBoV), Human bocavirus infection); major surface protein 2 MSP2, major surface protein 4 MSP4, MSP variant SGV1, MSP variant SGV2, outer membrane protein OMP, outer membrande protein 19 OMP-19, major antigenic protein MAPI, major antigenic protein MAP 1-2, major antigenic protein MAP IB, major antigenic protein MAP 1-3, Erum2510 coding protein, protein GroEL, protein GroES, 30-kDA major outer membrane proteins, GE 100-kDa protein, GE 130-kDa protein, GE 160-kDa protein (Ehrlichia ewingii, Human ewingii ehrlichiosis); major surface proteins 1-5 (MSPla, MSPlb, MSP2, MSP3, MSP4, MSP5), type IV secreotion system proteins VirB2, VirB7, VirBl l, VirD4 (Anaplasma phagocy tophilum, Human granulocytic anaplasmosis (HGA)); protein NS1, small hydrophobic protein N52, SH protein, fusion protein F, glycoprotein G, matrix protein M, matrix protein M2-1, matrix protein M2 -2, phosphoprotein P, nucleoprotein N, polymerase L (Human metapneumovirus (hMPV), Human metapneumovirus infection); major surface protein 2 MSP2, major surface protein 4 MSP4, MSP variant SGV1, MSP variant SGV2, outer membrane protein OMP, outer membrande protein 19 OMP-19, major antigenic protein MAPI,major antigenic protein MAP 1-2, major antigenic protein MAP IB, major antigenic protein MAP 1-3, Erum2510 coding protein, protein GroEL, protein GroES, 30-kDA major outer membrane proteins, GE 100-kDa protein, GE 130-kDa protein, GE 160-kDa protein (Ehrlichia chaffeensis, Human monocytic ehrlichiosis); replication protein El., regulatory protein E2, protein E3, protein E4, protein ES, protein E6, protein E7, protein E8, major capsid protein LI, minor capsid protein L2 (Human papillomavirus (HPV), Human papillomavirus (HPV) infection); fusion protein F, hemagglutinin-neuramidase HN, glycoprotein G, matrix protein M, phosphoprotein P, nucleoprotein N, polymerase L (Human parainfluenza viruses (HPIV), Human parainfluenza virus infection); Hemagglutinin (HA), Neuraminidase (NA), Nucleoprotein (NP), Ml protein, M2 protein, NS1 protein, NS2 protein (NEP protein: nuclear export protein), PA protein, PB1 protein (polymerase basic 1 protein), PB1-F2 protein and PB2 protein (Orthomyxoviridae family, Influenza virus (flu)); genome polyprotein, protein E, protein M, capsid protein C (Japanese encephalitis virus, Japanese encephalitis); RTX toxin, type IV pili, major pilus subunit PilA, regulatory transcription factors PilS and PilR, protein sigma54, outer membrane proteins (Kingella kingae, Kingella kingae infection); prion protein (Kuru prion, Kuru); nucleoprotein N, polymerase L, matrix protein Z, glycoprotein GP (Lassa virus, Lassa fever); peptidoglycan-associated lipoprotein PAL, 60 kDa chaperonin Cpn60 (groEL, HspB), type IV pilin PilE, outer membrane protein MIP, major outer membrane protein MompS, zinc metalloproteinase MSP (Legionella pneumophila, Legionellosis (Legionnaires' disease, Pontiac fever)); P4 nuclease, protein WD, ribonucleotide reductase M2, surface membrane glycoprotein Pg46, cysteine proteinase CP, glucose-regulated protein 78 GRP-78, stage-specific S antigen-like protein A2, ATPase Fl, beta-tubulin, heat shock protein 70 Hsp70, KMP-11, glycoprotein GP63, protein BT1, nucleoside hydrolase NH, cell surface protein Bl, ribosomal protein Pl -like protein Pl, sterol 24-c-methyltransf erase SMT, LACK protein, histone Hl, SPB1 protein, thiol specific antioxidant TSA, protein antigen STI1, signal peptidase SP, histone H2B, suface antigen PSA-2, cystein proteinase b Cpb (Leishmania genus, Leishmaniasis); major membrane protein I, serine-rich antigen-45 kDa, 10 kDa caperonin GroES, HSP kDa antigen, amino-oxononanoate synthase AONS, protein recombinase A RecA, AcetyL / propionyl- coenzyme A carboxylase alpha, alanine racemase, 60 kDa chaperonin 2, ESAT-6-like protein EcxB (L-ESAT-6), protein Lsr2, protein ML0276, Heparin-binding hemagglutinin HBHA, heatshock protein 65 Hsp65, mycPl or ML0041 coding protein htrA2 or ML0176 coding protein htrA4 or ML2659 coding protein, gcp or ML0379 coding protein, clpC or ML0235 coding protein (Mycobacterium leprae and Mycobacterium lepromatosis, Leprosy); outer membrane protein LipL32, membrane protein LIC10258, membrane protein LP30, membrane protein LIC 12238, Ompa-like protein Lsa66, surface protein LigA, surface protein LigB, major outermembrane protein OmpLl, outer membrane protein LipL41, protein LigAni, surface protein LcpA, adhesion protein LipL53, outer membrane protein UpL32, surface protein Lsa63, flagellin FlaBl, membran lipoprotein LipL21, membrane protein pL40, leptospiral surface adhesin Lsa27, outer membrane protein OmpL36, outer membrane protein OmpL37, outer membrane protein OmpL47, outer membrane protein OmpL54, acyltransferase LpxA (Leptospira genus, Leptospirosis); listeriolysin 0 precursor Hly (LLO), invasion-associated protein lap (P60), Listeriolysin regulatory protein PrfA, Zinc metalloproteinase Mpl, Phosphatidylinositol-specific phospholipase C PLC (PIcA, PlcB), O-acetyltransferase Oat, ABC- transporter permease Im.G_1771, adhesion protein LAP, LAP receptor Hsp60, adhesin LapB, haemolysin listeriolysin 0 LLO, protein ActA, Intemalin A InIA, protein InIB (Listeria monocytogenes, Listeriosis); outer surface protein A OspA, outer surface protein OspB, outer surface protein OspC, decorin binding protein A DbpA, decorin binding protein B DbpB, flagellar filament 41 kDa core protein Fla, basic membrane protein A Bmp A (Immunodominant antigen P39), outer surface 22 kDa lipoprotein precursor (antigen IPLA7), variable surface lipoprotein vlsE (usually Borrelia burgdorferi and other Borrelia species, Lyme disease (Lyme borreliosis)); venom allergen homolog-like protein VAL-1, abundant larval transcript ALT-1, abundant larval transcript ALT-2, thioredoxin peroxidase TPX, vespid allergen homologue VAH, thi ordoxin peroxidase 2 TPX-2, antigenic protein SXP (peptides N, Nl, N2, and N3), activation associated protein- 1 ASP-1, thioredoxin TRX, transglutaminase BmTGA, glutathione-S-transferases GST, myosin, vespid allergen homologue VAH, 175 kDa collagenase, glyceraldehyde-3 -phosphate dehydrogenase GAPDH, cuticular collagen Col-4, Secreted Larval Acidic Proteins SLAPs, chitinase CHI-1, maltose binding protein MBP, glycolytic enzyme fructose- 1,6-bisphosphate aldolase Fba, tropomyosin TMY-1, nematode specific gene product OvB20, onchocystatin CPL2, protein Cox-2 (Wuchereria bancrofti and Brugia malayi. Lymphatic filariasis (Elephantiasis)); glycoprotein GP, matrix protein polymerase L, nucleoprotein N (Lymphocytic choriomeningitis virus (LCMV), Lymphocytic choriomeningitis); thrombospondin-related anonymous protein TRAP, SSP2 Sporozoite surface protein 2, apical membrane antigen 1 AMA1, rhoptry membrane antigen RMA1, acidic basic repeat antigen ABRA, cell-traversal protein PF, protein Pvs25, merozoite surface protein 1 MSP-1, merozoite surface protein 2 MSP-2, ring-infected erythrocyte surface antigen RESALiver stage antigen 3 LSA-3, protein Eba-175, serine repeat antigen 5 SERA-5, circumsporozoite protein CS, merozoite surface protein 3 MSP3, merozoite surface protein 8 MSP5, enolase PF10, hepatocyte erythrocyte protein 17 kDa HEP17, erythrocyte membrane protein 1 EMP1, protein Kbetamerozoite surface protein 4 / 5 MSP 4 / 5, heat shock protein Hsp90, glutamate-rich protein GLURP, merozoite surface protein 4 MSP-4, protein STARP,circumsporozoite protein-related antigen precursor CRA (Plasmodium genus, Malaria); nucleoprotein N, membrane-associated protein VP24, minor nucleoprotein VP30, polymerase cofactor VP35, polymerase L, matrix protein VP40, envelope glycoprotein GP (Marburg virus, Marburg hemorrhagic fever (MHF)); protein C, matrix protein M, phosphoprotein P, non- structural protein V, hemagglutinin glycoprotein H, polymerase L, nucleoprotein N, fusion protein F (Measles virus, Measles); members of the ABC transporter family (LoIC, OppA, and PotF), putative lipoprotein releasing system transmembrane protein LoIC / E, flagellin FliC, Burkholderia intracellular motility A BimA, bacterial Elongation factor-Tu EF-Tu, 17 kDa OmpA-like protein, boaA coding protein, boaB coding protein (Burkholderia pseudomallei, Melioidosis (Whitmore's disease)); pilin proteins, minor pilin-associated subunit pilC, major pilin subunit and variants pilE, pilS, phase variation protein porA, Porin B PorB, protein TraD, Neisserial outer membrane antigen H.8, 70 kDa antigen, major outer membrane protein PI, outer membrane proteins PIA and PIB, W antigen, surface protein A NspA, transferrin binding protein TbpA, transferrin binding protein TbpB PBP2, mtrR coding protein, ponA coding protein, membrane permease FbpBC, FbpABC protein system, LbpAB proteins, outer membrane protein Opa, outer membrane transporter FetA, iron-repressed regulator MpeR, factor H-binding protein fHbp, adhesin NadA, protein NhbA, repressor FarR (Neisseria meningitidis, Meningococcal disease); 66 kDa protein, 22 kDa protein (usually Metagonimus yokagawai, Metagonimiasis); polar tube proteins (34, 75, and 170 kDa in Glugea, 35, 55 and 150 kDa in Encephalitozoon), kinesin-related protein, RNA polymerase II largest subunit, similar of integral membrane protein YIP A, anti-silencing protein 1, heat shock transcription factor HSF, protein kinase, thymidine kinase, NOP-2 like nucleolar protein (Microsporidia phylum, Microsporidiosis); CASP8 and FADD-like apoptosis regulator, Glutathione peroxidase GPX1, RNA helicase NPH-II NPH2, Poly(A) polymerase catalytic subunit PAPL, Major envelope protein P43K, early transcription factor 70 kDa subunit VETFS, early transcription factor 82 kDa subunit VETFL, metalloendopeptidase Gl-type, nucleoside triphosphatase I NPH1, replication protein A28-like MC134L, RNA polymease 7 kDa subunit RPO7 (Molluscum contagiosum virus (MCV), Molluscum contagiosum (MC)); matrix protein M, phosphoprotein P / V, small hydrophobic protein SH, nucleoprotein N, protein V, fusion glycoprotein hemagglutinin-neuraminidase HN, RNA polymerase L (Mumps virus, Mumps); Outer membrane proteins OM, cell surface antigen OmpA, cell surface antigen OmpB (sca5), cell surface protein SCA4, cell surface protein SCA1, intracytoplasmic protein D, crystalline surface layer protein SLP, protective surface protein antigen SPA (Rickettsia typhi, Murine typhus (Endemic typhus)); adhesin Pl, adhesion P30, protein pl 16, protein P40, cytoskeletal protein HMW1, cytoskeletal protein HMW2, cytoskeletal protein HMW3, MPN152 coding protein, MPN426 coding protein, MPN456 codingprotein, MPN-500coding protein (Mycoplasma pneumoniae, Mycoplasma pneumonia); NocA, Iron dependent regulatory protein, VapA, VapD, VapF, VapG, caseinolytic protease, filament tip-associated 43-kDa protein, protein P24, protein P61, 15-kDa protein, 56-kDa protein (usually Nocardia asteroides and other Nocardia species, Nocardiosis); venom allergen homolog-like protein VAL-1, abundant larval transcript ALT-1, abundant larval transcript ALT-2, thioredoxin peroxidase TPX, vespid allergen homologue VAH, thiordoxin peroxidase 2 TPX-2, antigenic protein SXP (peptides N, Nl, N2, and N3), activation associated protein-1 ASP-1, Thioredoxin TRX, transglutaminase BmTGA, glutathione-S-transferases GST, myosin, vespid allergen homologue VAH, 175 kDa collagenase, glyceraldehyde-3 -phosphate dehydrogenase GAPDH, cuticular collagen Col -4, Secreted Larval Acidic Proteins SLAPs, chitinase CHI-1, maltose binding protein MBP, glycolytic enzyme fructose- 1,6-bisphosphate aldolase Fba, tropomyosin TMY-1, nematode specific gene product OvB20, onchocy statin CPI-2, Cox-2 (Onchocerca volvulus, Onchocerciasis (River blindness)); 43 kDa secreted glycoprotein, glycoprotein gpO, glycoprotein gp75, antigen Pb27, antigen Pb40, heat shock protein Hsp65, heat shock protein Hsp70, heat shock protein Hsp90, protein PIO, triosephosphate isomerase TPI, N-acetyl- glucosamine-binding lectin Paracoccin, 28 kDa protein Pb28 (Paracoccidioides brasiliensis, Paracoccidioidomycosis (South American blastomycosis)); 28-kDa cruzipain-like cystein protease Pw28CCP (usually Paragonimus westermani and other Paragonimus species, Paragonimiasis); outer membrane protein OmpH, outer membrane protein Omp28, protein PM1539, protein PM0355, protein PM1417, repair protein MutL, protein BcbC, prtein PM0305, formate dehydrogenase-N, protein PM0698, protein PM1422, DNA gyrase, lipoprotein PIpE, adhesive protein Cp39, heme aquisition system receptor HasR, 39 kDa capsular protein, iron- regulated OMP IROMP, outer membrane protein OmpA87, fimbrial protein Ptf, fimbrial subunit protein PtfA, transferrin binding protein Tbpl, esterase enzyme MesA, Pasteurella multocida toxin PMT, adhesive protein Cp39 (Pasteurella genus, Pasteurellosis); “filamentous hemagglutinin FhaB, adenylate cyclase CyaA, pertussis toxin subunit 4 precursor PtxD, pertactin precursor Prn, toxin subunit 1 PtxA, protein Cpn60, protein brkA, pertussis toxin subunit 2 precursor PtxB, pertussis toxin subunit 3 precursor PtxC, pertussis toxin subunit 5 precursor PtxE, pertactin Pm, protein Fim2, protein Fim3;” (Bordetella pertussis, Pertussis (Whooping cough)); “Fl capsule antigen, virulence-associated V antigen, secreted effector protein LcrV, V antigen, outer membrane protease Pla, secreted effector protein YopD, putative secreted protein-tyrosine phosphatase YopH, needle complex major subunit YscF, protein kinase YopO, putative autotransporter protein YapF, inner membrane ABC-transporter YbtQ (Irp7), putative sugar binding protein YP00612, heat shock protein 90 HtpG, putative sulfatase protein YdeN, outer-membrane lipoprotein carrier protein LoIA, secretion chaperone YerA,putative lipoprotein YP00420, hemolysin activator protein HpmB, pesticin / yersiniabactin outer membrane receptor Psn, secreted effector protein YopE, secreted effector protein YopF, secreted effector protein YopK, outer membrane protein YopN outer membrane protein YopM, Coagulase / fibrinolysin precursor Pla;” (Yersinia pestis, Plague); protein PhpA, surface adhesin PsaA, pneumolysin Ply, ATP-dependent protease CIp, lipoate-protein ligase LpIA, cell wall surface anchored protein psrP, sortase SrtA, glutamyl-tRNA synthetase GItX, choline binding protein A CbpA, pneumococcal surface protein A PspA, pneumococcal surface protein C PspC, 6-phosphogluconate dehydrogenase Gnd, iron-binding protein PiaA, Murein hydrolase LytB, proteon LytC, protease Al (Streptococcus pneumoniae, Pneumococcal infection); major surface protein B, kexin-like protease KEX1, protein A12, 55 kDa antigen P55, major surface glycoprotein Msg (Pneumocystis jirovecii, Pneumocystis pneumonia (PCP)); genome polyprotein, polymerase 3D, viral capsid protein VP1, viral capsid protein VP2, viral capsid protein VP3, viral capsid protein VP4, protease 2 A, protease 3C (Poliovirus, Poliomyelitis); protein Nfal, exendin-3, secretory lipase, cathepsin B-like protease, cysteine protease, cathepsin, peroxiredoxin, protein CrylAc (usually Naegleria fow leri. Primary amoebic meningoencephalitis (PAM)); agnoprotein, large T antigen, small T antigen, major capsid protein VP1, minor capsid protein Vp2 (JC virus, Progressive multifocal leukoencephalopathy); low calcium response protein E LCrE, chlamydial outer protein N CopN, serine / threonine- protein kinase PknD, acyl-carrier-protein S-ma lonyltransferase FabD, single-stranded DNA- binding protein Ssb, major outer membrane protein MOMP, outer membrane protein 2 0mp2, polymorphic membrane protein family (Pmpl, Pmp2, Pmp3, Pmp4, Pmp5, Pmp6, Pmp7, Pmp8, Pmp9, PmplO, Pmpl l, Pmpl2, Pmpl3, Pmpl4, Pmpl5, Pmpl6, Pmpl7, Pmpl8, Pmpl9, Pmp20, Pmp21) (Chlamydophila psillaci. Psittacosis); outer membrane protein Pl, heat shock protein B HspB, peptide ABC transporter, GTP-binding protein, protein IcmB, ribonuclease R, phosphatas SixA, protein DsbD, outer membrane protein ToIC, DNA-binding protein PhoB, ATPase DotB, heat shock protein B HspB, membrane protein Coml, 28 kDa protein, DNA-3- methyladenine glycosidase I, pouter membrane protein OmpH, outer membrane protein AdaA, glycine cleavage system T-protein (Coxiella burnetii, Q fever); nucleoprotein N, large structural protein L, phophoprotein P, matrix protein M, glycoprotein G (Rabies virus, Rabies); fusionprotein F, nucleoprotein N, matrix protein M, matrix protein M2-1, matrix protein M2-2, phophoprotein P, small hydrophobic protein SH, major surface glycoprotein G, polymerase L, non- structural protein 1 NS1, non-structural protein 2 NS2 (Respiratory syncytial virus (RSV), Respiratory syncytial virus infection); genome polyprotein, polymerase 3D, viral capsid protein VP1, viral capsid protein VP2, viral capsid protein VP3, viral capsid protein VP4, protease 2 A, protease 3C (Rhinovirus, Rhinovirus infection); outer membrane proteins OM, cell surfaceantigen OmpA, cell surface antigen OmpB (sca5), cell surface protein SCA4, cell surface protein SCA1, protein PS120, intracytoplasmic protein D, protective surface protein antigen SPA (Rickettsia genus, Rickettsial infection); outer membrane proteins OM, cell surface antigen OmpA, cell surface antigen OmpB (sca5), cell surface protein SCA4, cell surface protein SCA1, intracytoplasmic protein D (Rickettsia akari. Rickettsialpox); envelope glycoprotein GP, polymerase L, nucleoprotein N, non- structural protein NSS (Rift Valley fever virus, Rift Valley fever (RVF)); outer membrane proteins OM, cell surface antigen OmpA, cell surface antigen OmpB (sca5), cell surface protein SCA4, cell surface protein SC Al, intracytoplasmic protein D (Rickettsia rickeUsii. Rocky mountain spotted fever (RMSF)); non-structural protein 6 N56, non- structural protein 2 N52, intermediate capsid protein VP6, inner capsid protein VP2, non- structural protein 3 NS3, RNA-directed RNA polymerase L, protein VP3, non-structural protein 1 NS1, non-structural protein 5 N55, outer capsid glycoprotein VP7, non-structural glycoprotein 4 N54, outer capsid protein VP4; (Rotavirus, Rotavirus infection); polyprotein P200, glycoprotein El, glycoprotein E2, protein N52, capsid protein C (Rubella virus, Rubella); chaperonin GroEL (MopA), inositol phosphate phosphatase SopB, heat shock protein HslU, chaperone protein DnaJ, protein TviB, protein IroN, flagellin FliC, invasion protein SipC, glycoprotein gp43, outer membrane protein LamB, outer membrane protein PagC, outer membrane protein ToIC, outer membrane protein NmpC, outer membrane protein FadL, transport protein SadA, transferase WgaP, effector proteins SifA, SteC, SseL, SseJ and SseF (Salmonella genus, Salmonellosis),' “protein 14, non-structural protein NS7b, non-structural protein NS8a, protein 9b, protein 3a, nucleoprotein N, non-structural protein NS3b, non- structural protein N56, protein 7a, non-structural protein NS8b, membrane protein M, envelope small membrane protein EsM, replicase polyprotein la, spike glycoprotein S, replicase polyprotein lab; SARS coronavirus, SARS (Severe Acute Respiratory Syndrome)); serin protease, Atypical Sarcoptes Antigen 1 ASAI, glutathione 5 -transferases GST, cystein protease, serine protease, apolipoprotein (Sarcoptes scabiei, Scabies); glutathione 5 -transferases GST, paramyosin, hemoglbinase SM32, major egg antigen, 14 kDa fatty acid-binding protein Sml4, major larval surface antigen P37, 22.6 kDa tegumental antigen, calpain CANP, triphospate isomerase Tim, surface protein 9B, outer capsid protein VP2, 23 kDa integral membrane protein Sm23, Cu / Zn-superoxide dismutase, glycoprotein Gp, myosin (Schistosoma genus, Schistosomiasis (Bilharziosis)); 60 kDa chaperonin, 56 kDa type-specific antigen, pyruvate phosphate dikinase, 4-hydroxybenzoate octaprenyltransferase (Orientia tsutsugamushi, Scrub typhus); dehydrogenase GuaB, invasion protein Spa32, invasin IpaA, invasin IpaB, invasin IpaC, invasin IpaD, invasin IpaH, invasin IpaJ (Shigella genus, Shigellosis (Bacillary dysentery)); protein P53, virion protein US10 homolog, transcriptional regulator 1E63,transcriptional transactivator 1E62, protease P33, alpha trans-inducing factor 74 kDa protein, deoxyuridine 5 '-triphosphate nucleotidohydrolase, transcriptional transactivator 1E4, membrane protein UL43 homolog, nuclear phosphoprotein UL3 homolog, nuclear protein UL4 homolog, replication origin-binding protein, membrane protein 2, phosphoprotein 32, protein 57, DNA polymerase processivity factor, portal protein 54, DNA primase, tegument protein ULI 4 homolog, tegument protein UL21 homolog, tegument protein UL55 homolog, tripartite terminase subunit UL33 homolog, tripartite terminase subunit ULI 5 homolog, capsid-binding protein 44, virion-packaging protein 43 (Varicella zoster virus (VZV), Shingles (Herpes zoster)); truncated 3-beta hydroxy-5-ene steroid dehydrogenase homolog, virion membrane protein A13, protein A19, protein A31, truncated protein A35 homolog, protein A37.5 homolog, protein A47, protein A49, protein A51, semaphorin-like protein A43, serine proteinase inhibitor 1, serine proteinase inhibitor 2, serine proteinase inhibitor 3, protein A6, protein Bl 5, protein Cl, protein C5, protein C6, protein F7, protein F8, protein F9, protein Fl 1, protein F14, protein Fl 5, protein F16 (Variola major or Variola minor, Smallpox (Variola)); adhesin / gly coprotein gp70, proteases (Sporothrix schenckii, Sporotrichosis); heme-iron binding protein IsdB, collagen adhesin Cna, clumping factor A ClfA, protein MecA, fibronectin-binding protein A FnbA, enterotoxin type A EntA, enterotoxin type B EntB, enterotoxin type C EntCl, enterotoxin type C EntC2, enterotoxin type D EntD, enterotoxin type E EntE, Toxic shock syndrome toxin-1 TSST- 1, Staphylokinase, Penicillin binding protein 2a PBP2a (MecA), secretory antigen SssA Staphylococcus genus, Staphylococcal food poisoning); heme-iron binding protein IsdB, collagen adhesin Cna, clumping factor A ClfA, protein MecA, fibronectin-binding protein A FnbA, enterotoxin type A EntA, enterotoxin type B EntB, enterotoxin type C EntCl, enterotoxin type C EntC2, enterotoxin type D EntD, enterotoxin type E EntE, Toxic shock syndrome toxin- 1 TSST-1, Staphylokinase, Penicillin binding protein 2a PBP2a (MecA), secretory antigen SssA (Staphylococcus Qmxs e.g. aureus, Staphylococcal infection); antigen Ss-IR, antigen NIE, strongylastacin, Na+-K+ ATPase Sseat-6, tropomysin SsTmy-1, protein LEC-5, 41 kDa aantigen P5, 41 -kDa larval protein, 31 -kDa larval protein, 28-kDa larval protein (Strongyloides stercoralis, Strongyloidiasis); glycerophosphodiester phosphodiesterase GlpQ (Gpd), outer membrane protein TmpB, protein Tp92, antigen TpFl, repeat protein Tpr, repeat protein F TprF, repeat protein G TprG, repeat protein I Tprl, repeat protein J TprJ, repeat protein KTprK, treponemal membrane protein A TmpA, lipoprotein, 15 kDa Tppl5, 47 kDa membrane antigen, miniferritin TpFl, adhesin Tp0751, lipoprotein TP0136, protein TpN17, protein TpN47, outer membrane protein TP0136, outer membrane protein TP0155, outer membrane protein TP0326, outer membrane protein TP0483, outer membrane protein TP0956 (Treponema pallidum, Syphilis); Cathepsin L-like proteases, 53 / 25-kDa antigen, 8 kDa family members, cysticercusprotein with a marginal trypsin-like activity TsAg5, oncosphere protein TSOL18, oncosphere protein TSOL45-1A, lactate dehydrogenase A LDHA, lactate dehydrogenase B LDHB (Taenia genus, Taeniasis); tetanus toxin TetX, tetanus toxin C TTC, 140 kDa S layer protein, flavoprotein beta-subunit CT3, phospholipase (lecithinase), phosphocarrier protein HPr (Clostridium lelani. Tetanus (Lockjaw)); genome polyprotein, protein E, protein M, capsid protein C (Tick-borne encephalitis virus (TBEV), Tick-borne encephalitis); 58-kDa antigen, 68- kDa antigens, Toxocara larvae excretory-secretory antigen TES, 32-kDa glycoprotein, glycoprotein TES-70, glycoprotein GP31, excretory-secretory antigen TcES-57, perienteric fluid antigen Pe, soluble extract antigens Ex, excretory / secretory larval antigens ES, antigen TES- 120, polyprotein allergen TBA-1, cathepsin L-like cysteine protease c-cpl-1, 26-kDa protein (Toxocara canis or Toxocara call. Toxocariasis (Ocular Larva Migrans (OLM) and Visceral Larva Migrans (VLM))); microneme proteins (MIC1, MIC2, MIC3, MIC4, MIC5, MICE, MIC7, MICE), rhoptry protein Rop2, rhoptry proteins (Ropl, Rop2, Rop3, Rop4, Rop5, Rop6, Rop7, Ropl 6, Rjopl7), protein SRI, surface antigen P22, major antigen p24, major surface antigen p30, dense granule proteins (GRA1, GRA2, GRA3, GRA4, GRA5, GRA6, GRA7, GRAB, GRA9, GRA10), 28 kDa antigen, surface antigen SAG1, SAG2 related antigen, nucleoside-triphosphatase 1, nucleoside-triphosphatase 2, protein Stt3, HesB-like domaincontaining protein, rhomboid-like protease 5, toxomepsin 1 (Toxoplasma gondii, Toxoplasmosis); 43 kDa secreted glycoprotein, 53 kDa secreted glycoprotein, paramyosin, antigen Ts21, antigen Ts87, antigen p46000, TSL-1 antigens, caveolin-1 CAV-1, 49 kDa newborn larva antigen, prosaposin homologue, serine protease, serine proteinase inhibitor, 45- kDa glycoprotein Gp45 (Trichinella spiralis, Trichinellosis); Myb-like transcriptional factors (Mybl, Myb2, Myb3), adhesion protein AP23, adhesion protein AP33, adhesin protein AP33-3, adhesins AP51, adhesin AP65, adhesion protein AP65-1, alpha-actinin, kinesin-associated protein, teneurin, 62 kDa proteinase, subtili sin-like serine protease SUB1, cysteine proteinase gene 3 CP3, alpha-enolase Enol, cysteine proteinase CP30, heat shock proteins (Hsp70, Hsp60) immunogenic protein P270, (Trichomonas vaginalis, Trichomoniasis); beta-tubulin, 47-kDa protein, secretory leucocyte-like proteinase- 1 SLP-1, 50-kDa protein TT50, 17 kDa antigen, 43 / 47 kDa protein (Trichuris trichiura, Trichuriasis (Whipworm infection)); protein ESAT-6 (EsxA), 10 kDa filtrate antigen EsxB, secreted antigen 85-B FBPB, fibronectin-binding protein A FbpA (Ag85A), serine protease PepA, PPE family protein PPE18, fibronectin-binding protein D FbpD, immunogenic protein MPT64, secreted protein MPT51, catalase-peroxidase- peroxynitritase T KATG, periplasmic phosphate-binding lipoprotein PSTS3 (PBP-3, Phos-1), iron-regulated heparin binding hemagglutinin Hbha, PPE family protein PPE 14, PPE family protein PPE68, protein Mtb72F, protein Apa, immunogenic protein MPT63, periplasmicphosphate-binding lipoprotein PSTS1 (PBP-1), molecular chaperone DnaK, cell surface lipoprotein Mpt83, lipoprotein P23, phosphate transport system permease protein pstA, 14 kDa antigen, fibronectin-binding protein C FbpCl, Alanine dehydrogenase TB43, Glutamine synthetase 1, ESX-1 protein, protein CFP10, TB10.4 protein, protein MPT83, protein MTB12, protein MTBE, Rpf-like proteins, protein MTB32, protein MTB39, crystallin, heat-shock protein HSP65, protein PST-S(usually Mycobacterium tuberculosis, Tuberculosis); outer membrane protein Fob A, outer membrane protein FobB, intracellular growth locus IgICl, intracellular growth locus IgIC2, aminotransferase Wbtl, chaperonin GroEL, 17 kDa major membrane protein TUL4, lipoprotein LpnA, chitinase family 18 protein, isocitrate dehydrogenase, Nif3 family protein, type IV pili glycosylation protein, outer membrane protein toIC, FAD binding family protein, type IV pilin multimeric outer membrane protein, two component sensor protein KdpD, chaperone protein DnaK, protein TolQ (Francisella lularensis. Tularemia); “MB antigen, urease, protein GyrA, protein GyrB, protein ParC, protein ParE, lipid associated membrane proteins LAMP, thymidine kinase TK, phospholipase PL-A1, phospholipase PL-A2, phospholipase PL-C, surface-expressed 96-kDa antigen;” Ureaplasma urealyticum, Ureaplasma urealyticum infection); non- structural polyprotein, structural polyprotein, capsid protein CP, protein El, protein E2, protein E3, protease Pb, protease P2, protease P3 (Venezuelan equine encephalitis virus, Venezuelan equine encephalitis); glycoprotein GP, matrix protein Z, polymerase L, nucleoprotein N (Guanarito virus, Venezuelan hemorrhagic fever); polyprotein, protein E, protein M, capsid protein C, protease NS3, protein NS1, protein NS2A, protein AS2B, brotein NS4A, protein NS4B, protein NS5 (West Nile virus, West Nile Fever); cpasid protein CP, protein El, protein E2, protein E3, protease P2 (Western equine encephalitis virus, Western equine encephalitis); genome polyprotein, protein E, protein M, capsid protein C, protease NS3, protein NS1, protein NS2A, protein AS2B, protein NS4A, protein NS4B, protein NS5 (Yellow fever virus, Yellow fever); putative Yop targeting protein YobB, effector protein YopD, effector protein YopE, protein YopH, effector protein Yop J, protein translocation protein YopK, effector protein YopT, protein YpkA, flagellar biosyntheses protein FlhA, peptidase M48, potassium efflux system KefA, transcriptional regulatoer RovA, adhesin Ifp, translocator portein LcrV, protein PcrV, invasin Inv, outer membrane protein OmpF-like porin, adhesin YadA, protein kinase C, phospholipase Cl, protein PsaA, mannosyltransf erase-like protein WbyK, protein YscU, antigen YPMa (Yersinia pseudotuberculosis, Yersinia pseudotuberculosis infection); and effector protein YopB, 60 kDa chaperonin, protein WbcP, tyrosin-protein phosphatase YopH, protein YopQ, enterotoxin, Galactoside permease, reductaase NrdE, protein YasN, Invasin Inv, adhesin YadA, outer membrane porin F OmpF, protein UspAl, protein EibA, protein Hia, cell surface protein Ail,chaperone SycD, protein LcrD, protein LcrG, protein LcrV, protein SycE, protein YopE, regulator protein TyeA, protein YopM, protein YopN, protein YopO, protein YopT, protein YopD, protease CIpP, protein MyfA, protein FilA, and protein PsaA (Yersinia enterocolitica, Yersiniosis).

[0121] The infectious agent can be a bacterium, a fungus, a virus, or a protist. The infectious agent can be a coronavirus (CoV) (e.g., an alphacoronavirus, a betacoronavirus, a gammacoronavirus, or a deltacoronavirus). The infectious agent can be selected from Acinetobacter baumannii, Anaplasma genus, Anaplasma phagocytophilum, Ancylostoma braziliense, Ancylostoma duodenale, Arcanobacterium haemolyticum, Ascaris lumbricoides, Aspergillus genus, Astroviridae, Babesia genus, Bacillus anthracis, Bacillus cereus, Bartonella henselae, BK virus, Blastocystis hominis, Blastomyces dermatitidis, Bordetella pertussis, Borrelia burgdorferi, Borrelia genus, Borrelia spp, Brucella genus, Brugia malayi, Bunyaviridae family, Burkholderia cepacia and other Burkholderia species, Burkholderia mallei, Burkholderia pseudomallei, Caliciviridae family, Campylobacter genus, Candida albicans, Candida spp, Chlamydia trachomatis, Chlamydophila pneumoniae, Chlamydophila psittaci, CJD prion, Clonorchis sinensis, Clostridium botulinum, Clostridium difficile, Clostridium perfringens, Clostridium perfringens, Clostridium spp, Clostridium tetani, Coccidioides spp, coronaviruses, Corynebacterium diphtheriae, Coxiella burnetii, Crimean- Congo hemorrhagic fever virus, Cryptococcus neoformans, Cryptosporidium genus, Cytomegalovirus (CMV), Dengue viruses (DEN-1, DEN-2, DEN-3 and DEN-4), Dientamoeba fragilis, Ebolavirus (EBOV), Echinococcus genus, Ehrlichia chaffeensis, Ehrlichia ewingii, Ehrlichia genus, Entamoeba histolytica, Enterococcus genus, Enterovirus genus, Enteroviruses, mainly Coxsackie A virus and Enterovirus 71 (EV71), Epidermophyton spp, Epstein-Barr Virus (EBV), Escherichia coli 0157:147, 0111 and 0104:144, Fasciola hepatica and Fasciola gigantica, FFI prion, Filarioidea superfamily, Filoviruses, Flaviviruses, Francisella tularensis, Fusobacterium genus, Geotrichum candidum, Giardia intestinalis, Gnathostoma spp, GSS prion, Guanarito virus, Haemophilus ducreyi, Haemophilus influenzae, Helicobacter pylori, Henipavirus (Hendra virus Nipah virus), Hepatitis A Virus, Hepatitis B Virus (HBV), Hepatitis C Virus (HCV), Hepatitis D Virus, Hepatitis E Virus, Herpes simplex virus 1 and 2 (HSV-1 and HSV-2), Histoplasma capsulatum, HIV (Human immunodeficiency virus), Hortaea werneckii, Human bocavirus (HBoV), Human herpesvirus 6 (HHV-6) and Human herpesvirus 7 (HHV-7), Human metapneumovirus (hMPV), Human papillomavirus (HPV), Human parainfluenza viruses (HPIV), Japanese encephalitis virus, JC virus, Junin virus, Kingella kingae, Klebsiella granulomatis, Kuru prion, Lassa virus, Legionella pneumophila, Leishmania genus, Leptospira genus, Listeria monocytogenes, Lymphocytic choriomeningitis virus (LCMV), Machupo virus,Malassezia spp, Marburg virus, Measles virus, Metagonimus yokagawai, Microsporidia phylum, Molluscum contagiosum virus (MCV), Mumps virus, Mycobacterium leprae and Mycobacterium lepromatosis, Mycobacterium tuberculosis, Mycobacterium ulcerans, Mycoplasma pneumoniae, Naegleria fowleri, Necator americanus, Neisseria gonorrhoeae, Neisseria meningitidis, Nocardia asteroides, Nocardia spp, Onchocerca volvulus, Orientia tsutsugamushi, Orthomyxoviridae family (Influenza), Paracoccidioides brasiliensis, Paragonimus spp, Paragonimus westermani, Parvovirus Bl 9, Pasteur ella genus, Plasmodium genus, Pneumocystis jirovecii, Poliovirus, Rabies virus, Respiratory syncytial virus (RSV), Rhinovirus, rhinoviruses, Rickettsia akari, Rickettsia genus, Rickettsia prowazekii, Rickettsia rickettsii, Rickettsia typhi, Rift Valley fever virus, Rotavirus, Rubella virus, Sabia virus, Salmonella genus, Sarcoptes scabiei, SARS coronavirus, Schistosoma genus, Shigella genus, Sin Nombre virus, Hantavirus, Sporothrix schenckii, Staphylococcus genus, Staphylococcus genus, Streptococcus agalactiae, Streptococcus pneumoniae, Streptococcus pyogenes, Strongyloides stercoralis, Taenia genus, Taenia solium, Tick-borne encephalitis virus (TBEV), Toxocara canis or Toxocara cati, Toxoplasma gondii, Treponema pallidum, Trichinella spiralis, Trichomonas vaginalis, Trichophyton spp, Trichuris trichiura, Trypanosoma brucei, Trypanosoma cruzi, Ureaplasma urealyticum, Varicella zoster virus N7N Variola major or Variola minor, vCJD prion, Venezuelan equine encephalitis virus, Vibrio cholerae, West Nile virus, Western equine encephalitis virus, Wuchereria bancrofti, Yellow fever virus, Yersinia enter ocolitica, Yersinia pestis, and Yersinia pseudotuberculosis.

[0122] The presenting peptide can comprise or can be derived from the full-length surface protein of a coronavirus. The disease or disorder can be an infectious disease or disorder caused by a coronavirus, and the presenting peptide can comprise or can be derived from an antigenic protein of a coronavirus. The term “coronavirus” as used herein refers to a virus in the family Coronaviridae, which is in turn classified within the order Nidovirales. The coronaviruses are large, enveloped, positive-stranded RNA viruses. The coronaviruses have the largest genomes of the RNA viruses known in the art and replicate by a unique mechanism that results in a high frequency of recombination. The coronaviruses include antigenic groups I, II, and III. Nonlimiting examples of coronaviruses include SARS coronavirus (e.g., SARS-CoV and SARS-CoV-2), MERS coronavirus, transmissible gastroenteritis virus (TGEV), human respiratory coronavirus, porcine respiratory coronavirus, canine coronavirus, feline enteric coronavirus, feline infectious peritonitis virus, rabbit coronavirus, murine hepatitis virus, sialodacryoadenitis virus, porcine hemagglutinating encephalomyelitis virus, bovine coronavirus, avian infectious bronchitis virus, and turkey coronavirus, as well as chimeras thereof. Additional information related to coronavirus including classification, virion structure,genome structure, genetics and pathology is described, for example, in KV Holmes, Encyclopedia of Virology, 1999: 291-298, the content of which is incorporated herein by reference.

[0123] In some embodiments, a coronavirus described herein is in the genus of Alpha-coronavirus and the coronavirus antigens can be of or derived from any species or strains in the genus of Alpha-coronavirus. In some embodiments, a coronavirus described herein is in the genus of Beta-coronavirus and the coronavirus antigens can be of or derived from any species or strains in the genus of Beta-coronavirus . Member viruses in the genus of Alphacoronavirus and Beta-coronavirus are enveloped, positive-strand RNA viruses that can infect mammals.

[0124] A coronavirus described herein can be of any subgenus of Alpha-coronavirus genus, including but not limited to Colacovirus (e.g. Bat coronavirus CDPHE15), Decacovirus (e.g. Bat coronavirus HKU10 and Rhinolophus ferrumequinum alphacoronavirus HuB-2013), Duvinacovirus (Human coronavirus 229E), Luchacovirus (e.g. Lucheng Rn rat coronavirus), Minacovirus (e.g. Mink coronavirus 1), Minunacovirus (e.g. Miniopterus bat coronavirus 1 and Miniopterus bat coronavirus HKU8), Myotacovirus (e.g. Myotis ricketti alphacoronavirus Sax- 2011), Nyctacovirus (e.g. Nyctalus velutinus alphacoronavirus SC-2013 and Pipistrellus kuhlii coronavirus 3398), Pedacovirus (e.g. Porcine epidemic diarrhea virus and Scotophilus bat coronavirus 512), Rhinacovirus (e.g. Rhinolophus bat coronavirus HKU2), Setracovirus (e.g. Human coronavirus NL63 and NL63-related bat coronavirus strain BtKYNL63-9b), Soracovirus (e.g. Sorex araneus coronavirus T14), Sunacovirus (e.g. Suncus murinus coronavirus X74), and Tegacovirus (e.g. Alphacoronavirus 1).

[0125] Within the genus Beta-coronavirus, five subgenera or lineages have been recognized, including Embecovirus (lineage A), Sarbecovirus (lineage B), Merbecovirus (lineage C), Nobecovirus (lineage D), and Hibecovirus. Accordingly, in some embodiments, a coronavirus described herein can be any strain or species in any of the subgenera or lineages of Beta-coronavirus.

[0126] For example, a coronavirus antigen can be of or derived from any species or strains in the subgenus of Embecovirus, including but not limited to Beta-coronavirus 1 (e.g. Bow'we coronavirus and human coronavirus OC43), China Rattus coronavirus HKU24, Human coronavirus HKU1, Murine coronavirus (e.g. mouse heptatitis virus), and Myodes coronavirus 2JL14. The coronavirus antigen can be of or derived from any species or strains in the subgenus of Sarbecovirus, including but not limited to SARS-CoV, SARS-CoV2, 16BO133, Bat SARS CoV Rfl, Bat coronavirus HKU3 (BtCoV HKU3), LYRal 1, Bat SARS-CoV / Rp3, Bat SL-CoV YNLF 31C, Bat SL-CoV YNLF 34C, SHC014-CoV, WIV1, WIV16, Civet SARS-CoV, Rc-o319, SL-ZXC21, SL-ZC45, Pangolin SARSr-COV-GX, Pangolin SARSr-COV-GD, RshSTT182, RshSTT200, RacCS203, RmYN02, RpYN06, RaTG13, Bat CoV BtKY72, and Bat CoV BM48-31. The coronavirus antigen can be of any species or strains in the subgenus of Merbecovirus, including but not limited to Hedgehog coronavirus 7, MERS-CoV, Pipistrellus bat coronavirus HKU5, and Tylonycteris bat coronavirus HKU4. The coronavirus antigen can be of any species or strains in the subgenus of Nobecovirus, including but not limited to Eidolon bat coronavirus C704, Rousettus bat coronavirus GCCDC1, and Rousettus bat coronavirus HKU9. The coronavirus antigen can be of any species or strains in the subgenus of Hibecovirus, including but not limited to Bat Hp-betacoronavirus Zhejiang 2013.

[0127] The coronaviruses described herein can be, for example, phylogenetically clustered in functionally distinct clades. For example, the coronaviruses of lineage B Betacoronavirus (Sarbecovirus) can be clustered into clade 1, clade 2, clade 1 / 2, or clade 3 using the nucleotide sequences of nonstructural protein gene ORF la and ORF lb (see, for example, Hu et al., PLoS Pathog 13(11): el006698). Accordingly, the coronavirus antigens can be of or derived from any species or strain in any one of these clades. For example, the coronavirus antigens can be of any species or strain in clade 1, including but not limited to SARS-CoV, WIV1, LYRal l, Rs7327, Rs4231, Rs4084, and SHC014. The coronavirus antigens can be of any species or strain in clade 2, including but not limited to As6526, Yunnan 2011, Shaanxi 2011, 279-2005, Rs4237, Rs4081, Rp3, Rs4247, HKU3-8, HKU3-13, GX2013, Longquan-140,YN2013, Rf4092, ZXC21, ZC45, JL2012, HuB2013, Rfl, HeB2013, and 273-2005. The coronavirus antigens can be of any species or strain in clade 1 / 2, including but not limited to SARS-CoV2. The coronavirus antigens can be of any species or strain in clade 3, including but not limited to BM48-31. The coronavirus antigen described herein can be of a coronavirus, for example, SARS, SARS-2, WIV1, SHC014, Rfl, RmYN02, pangl7, RaTG13, and Rs4081.

[0128] As exemplified herein, SARS virus (e.g., SARS-CoV and SARS-CoV-2) is an enveloped coronavirus carrying a single-stranded positive-sense RNA genome (~30 kb), belonging to the genus Betacoronavirus from the Coronaviridae family. The virus RNA encodes four structural proteins including spike (S), envelope (E), membrane (M), and nucleocapsid (N) proteins, 16 non- structural proteins, and nine accessory proteins. The S glycoprotein contains an ectodomain that can be processed into SI and S2 subunits, a transmembrane domain, and an intracellular domain. Both SARS-CoV and SARS-CoV-2 bind the human ACE2 via the receptor binding domain within the SI subunit to facilitate entry into host cells, followed by membrane fusion mediated by the S2 subunit.

[0129] A coronavirus antigen of a coronavirus herein described can be any of a variety of coronavirus proteins capable of inducing an immune response against a coronavirus.Suitable coronavirus antigens are those that can elicit a protective immune response, such as producing broadly neutralizing antibodies. For example, the coronavirus antigen can comprise a coronavirus spike (S) protein, spike receptor binding domain (RBD), SI subunit, S2 subunit, spike full ectodomain proteins, papain-like proteases, 3 CL proteases, nucleocapsid proteins, envelope proteins, membrane proteins, or any of the structural, non- structural or accessory proteins that form a coronavirus.

[0130] In some embodiments, a coronavirus antigen used herein comprises a spike (S) protein or a portion thereof. A S protein is one of four major structural proteins covering the surface of each virion. The S protein, comprising a SI subunit and a S2 subunit, is a highly glycosylated, type I transmembrane protein capable of binding to a host-cell receptor and mediates viral entry. The S protein comprises a domain referred to as the RBD that mediates the interaction with the host-cell receptor to enter the host cell after one or more RBDs adopts an “up” position to bind the host receptor. It is believed that after binding the receptor, a nearby host protease cleaves the spike, which releases the spike fusion peptide, facilitating virus entry. Known host receptors for coronaviruses (e.g., Beta-coronaviruses) include antiotensin- converting enzyme 2 (ACE2), dipeptidyl peptidase-4 (DPP4) or sialic acids. For example, the RBDs of human coronaviruses SARS-CoV-2, SARS-CoV, HCoV-NL63, and related animal coronaviruses (WIV1 and SCH014) use ACE2 as their host receptor, while MERS-CoV uses DPP4 as its host receptor.

[0131] The coronavirus antigen used herein can, for example, comprise a coronavirus nucleocapsid protein (N protein) or a portion thereof. The N protein is a multifunctional RNA-binding protein required for viral RNA transcription, replication, and packaging. The N protein consists of three domains, an N-terminal RNA-binding domain, a central intrinsically disordered region, followed by a C-terminal dimerization domain. The RNA-binding domain contains multiple positively charged binding surfaces that form charged interactions with RNA promoting its helical arrangement. The coronavirus antigen used herein can comprise any of these N protein domains or a portion thereof.

[0132] In some embodiments, the coronavirus antigen used herein comprises a coronavirus membrane protein (M protein) or a portion thereof. The M protein is the most abundant structural protein and defines the shape of the viral envelope. The M protein is regarded as the central organizer of the viral assembly, interacting with other major coronaviral structural proteins.

[0133] In some embodiments, the coronavirus antigen used herein comprises a coronavirus envelope protein (E protein) or a portion thereof. The E protein is a small membrane protein and minor component of the virus particles. Without being bound to any theory, it isbelieved that the E protein plays roles in virion assembly and morphogenesis, alteration of the membrane of host cells and virus-host cell interaction.

[0134] In some embodiments, the coronavirus antigen used herein comprises a coronavirus hemagglutinin-esterase protein (HE protein) or a portion thereof. The HE protein, which is another envelope protein, mediates reversible attachment to O-acetylated sialic acids by acting both as lectins and receptor-destroying enzymes.

[0135] In some embodiments, the coronavirus antigen used herein comprises a coronavirus papain-like protease or a portion thereof. The coronavirus papain-like protease is one of several nonstructural proteins, and is responsible for processing of viral proteins into functional, mature subunits during maturation. For example, the coronavirus papain-like protease can cleave a site at the amino-terminal end of the viral replicase region. In addition to its role in viral protein maturation, papain-like protease exhibits both a deubiquitinating and deISG15ylating activity. In vivo, this protease antagonizes innate immunity by acting on IFN beta and NF- kappa B signaling pathways.

[0136] In some embodiments, the coronavirus antigen used herein comprises a coronavirus 3CL protease or a portion thereof. The 3CL protease is another main protease in addition to the papain-like protease and is required for processing of viral polypeptides into distinct, functional proteins. In some embodiments, the 3CL protease is a SARS-CoV-2 3CL Protease, which is a C30-type cysteine protease located within the non-structural proteins 3 (NS3) region of the viral polypeptide. Analysis of the Coronavirus genome reveals at least 11 sites of cleavage for the 3CL protease, many containing the amino acid sequence LQ[S / A / G],

[0137] The coronavirus antigen disclosed herein can, in some embodiments, comprise a S protein or a portion thereof, a N protein or a portion thereof, a HE protein or a portion thereof, a papain-like protease or a portion thereof, a coronavirus 3 CL protease or a portion thereof, a M protein or a portion thereof, or a combination thereof.

[0138] In some embodiments, the coronavirus antigen can be an immunogenic portion of a coronavirus protein herein described. It will be appreciated by those skilled in the art that an immunogenic portion of a coronavirus antigen can be fragments of the S protein (e.g., spike protein RBD), N protein, HE protein, papain-like protease, 3 CL protease, or M protein capable of eliciting an immune response against one or more coronaviruses. The immunogenic portion can comprise about, at least or at least about, at most or at most about, 50, 60, 70, 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, or a number or a range between any two of these values, contiguous amino acid residues from the coronavirus proteins. In some embodiments, the immunogenic portion comprises a S protein RBD or a portion thereof. The portion of the S protein RBD can comprise the receptor binding motif of theS protein RBD.

[0139] One or more of the plurality of CoV antigens can be of Co Vs in the genus of Alpha-CoV and / or Beta-CoV, and optionally each of the plurality of CoV antigens are of CoVs in the genus of Beta-CoV. The plurality of CoV antigens can be of CoVs in the subgenus of Sarbecovirus. The first CoV and the second CoV can be in the genus of Beta-CoV, optionally in the subgenus of Sarbecovirus. The plurality of CoV antigens can be of CoVs selected from: SARS-CoV, SARS-CoV-2, WIV1, SHC014, Rfl, RmYN02, pangl7, RaTG13, Rs4081, LYRal l, HKU3, Yunnan2011, BtKY72, BM48-31, WIV16, Khosta-1, and Khosta-2. The first CoV, the second CoV, or both can be selected from: SARS-CoV, SARS-CoV-2, WIV1, SHC014, Rfl, RmYN02, pangl7, RaTG13, Rs4081, LYRal l, HKU3, Yunnan2011, BtKY72, BM48-31, WIV16, Khosta-1, and Khosta-2. The CoV can be selected from a species or subspecies of SARS-CoV, SARS-CoV- 1, SARS-CoV-2, MERS-CoV, SL-CoV-WIVl, HKU4, HKU5, HCoV-OC43, HCoV-HKUl, HKU9, HKU3, HKU8, HKU24, NL63, SHC014, 229E and / or SARS-CoV-2 variants B.1.351, B.l.1.7, P. l, B.1.617.2, B.1.1.529, BA.l, BA.1.1, BA.2, BA.3, BA.4, BA.5 and other descendent lineages.

[0140] The CoV can be a species or subspecies of Embecovirus, Sarbecovirus, Merbecovirus, Nobevovirus, Hibecovirus, SARSr-CoV, MERS-CoV, or any combination thereof. The CoV can be selected from a beta-CoV from the sarbe-, embeco-, merbeco-, and / or nobecovirus lineages. The CoV can be selected from a sarbecovirus strain, optionally, SARS, LYRal l, Rfl, Rs4081, BtKY72, and / or BM48-31. The CoV can be selected from a merbecovirus strain, optionally HKU4, HKU5, HKU25, BtCoV-Vs-CoVl, MERS-related NL13845, MERS-related NL140422. The CoV can be selected from an embecovirus strain, optionally HKU1, Rat CoV Parker, PHEV, Equine CoV, Rodent CoV, Longquan Rat CoV.

[0141] The plurality of presenting peptide can be of a same protein type or corresponding proteins. Presenting peptide of a same protein type may or may not have identical amino acid sequences, but generally share some sequence homology. For example, the coronavirus S proteins of different coronaviruses are of a same protein type or corresponding proteins. As another example, envelope proteins from different coronaviruses are considered the same protein type or corresponding proteins. In some embodiments, proteins of different coronavirus taxonomic groups having the same function are considered the same protein type or corresponding proteins.

[0142] Alternatively, in some embodiments the plurality of presenting peptide can derive from antigens of different protein types. Antigens of different protein types typically have different functions. For example, the plurality of presenting peptide can derive from coronavirus S proteins or portions thereof as well as other coronavirus proteins such as a coronavirus Nprotein or a portion thereof, a coronavirus HE protein or a portion thereof, a coronavirus papainlike protease or a portion thereof, a coronavirus 3CL protease or a portion thereof, and / or a coronavirus M protein or a portion thereof.

[0143] The same APV can comprise the presenting peptides derived from two or more strains of the same family, same genus, and / or same species, of infectious agent. The plurality of disparate presenting peptide can have a sequence identity of about, at least, or at least about 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%,64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%,80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%,96%, 97%, 98%, 99%, 100%, or a number or a range between any two of these values, with one another.

[0144] The plurality of disparate (e.g., heterologous) presenting peptide can comprise at least m pathogenic antigens of an mth infectious agent, wherein m is an integer greater than 2 (e.g., 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 30, 35, 40, 45, 50, 60, 70, 80, 90, 100, 110, 120, 128, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, 260, 270, 280, 290, 300, 310, 320, 330, 340, 350, 360, 370, 380, 390, 400, 410, 420, 430, 440, 450, 460, 470, 480, 490, 500, or a number or a range between any two of these values), and wherein each mth pathogenic antigen is different from one another (e.g., heterologous). In some embodiments, m is an integer greater than 50. The plurality of disparate presenting peptide can comprise two or more of a 1st pathogenic antigen (PA) of a 1st infectious agent (I A), a 2nd PA of a 2nd IA, a 3rd PA of a 3rd I A, a 4th PA of a 4th I A, a 5 th PA of a 5 th IA, a 6th PA of a 6th IA, a 7th PA of a 7th IA, a 8th PA of a 8th IA, a 9th PA of a 9th IA, a 10th PA of a 10th IA, a 11th PA of a 11th IA, a 12th PA of a 12th IA, a 13th PA of a 13th IA, a MthPA of a Mth IA, a 15th PA of a 15th IA, a 16th PA of a 16th IA, a 17th PA of a 17th IA, a 18thPA of a 18th IA, a 19th PA of a 19th IA, a 20th PA of a 20th IA, a 21st PA of a 21st IA, a 22nd PA of a 22nd IA, a 23rd PA of a 23rd IA, a 24th PA of a 24th IA, a 25th PA of a 25th IA, a 26thPA of a 26th IA, a 27th PA of a 27th IA, a 28th PA of a 28th IA, a 29th PA of a 29th IA, a 30thPA of a 30th IA, a 31st PA of a 31st IA, a 32nd PA of a 32nd IA, a 33rd PA of a 33rd IA, a 34th PA of a 34th IA, a 35th PA of a 35th IA, a 36th PA of a 36th IA, a 37th PA of a 37th IA, a 38th PA of a 38th IA, a 39th PA of a 39th IA, a 40th PA of a 40th IA, a 41st PA of a 41st IA, a 42nd PA of a 42nd IA, a 43rd PA of a 43rd IA, a 44th PA of a 44th IA, a 45th PA of a 45th IA, a 46th PA of a 46th IA, a 47th PA of a 47th IA, a 48th PA of a 48th IA, a 49th PA of a 49th IA, and a 50th PA of a 50th IA. The 1st, 2nd, 3rd, 4th, 5th, 6th, 7th, 8th, 9th, 10th, 11th, 12th, Mth, Mth, 15th, 16th, 17th, 18th, 19th, 20th, 21st, 22nd, 23rd, 24th, 25th, 26th, 27th, 28th, 29th, 30th, 31st, 32nd, 33rd, 34th, 35th, 36th, 37th, 38th, 39th, 40th, 41st, 42nd, 43rd, 44th, 45th, 46th, 47th,48th, 49th, and 50th pathogenic antigens can be the same or different from one another. The 1st, 2nd, 3rd, 4th, 5th, 6th, 7th, 8th, 9th, 10th, 11th, 12th, 13th, 14th, 15th, 16th, 17th, 18th, 19th, 20th, 21st, 22nd, 23rd, 24th, 25th, 26th, 27th, 28th, 29th, 30th, 31st, 32nd, 33rd, 34th, 35th, 36th, 37th, 38th, 39th, 40th, 41st, 42nd, 43rd, 44th, 45th, 46th, 47th, 48th, 49th, and 50th infectious agents can be the same or different from one another. The plurality of disparate (e.g., heterologous) presenting peptide can comprise a plurality of CoV antigens, a plurality of influenza antigens, and / or a plurality of HIV antigens.

[0145] The compositions provided herein can induce broadly protective immune responses by eliciting broadly neutralizing antibodies and cytokines, and activating T cells with broad specificities. As an example, the broadly neutralizing antibodies, cytokine production or T cell activation can neutralize or target coronaviruses from a taxonomic group that is not only the same as but also differs from the taxonomic groups of the coronaviruses from which the coronavirus antigens used to elicit the antibodies, the cytokine production and T cell activation are derived. Broadly neutralizing response, cytokine production or T cell activation can also be referred to as heterologous response. In some embodiments, the compositions herein described can elicit broadly neutralizing antibodies, cytokine production or T cell activation that neutralize or target one or more infectious agents from a subfamily, genus, subgenus, species, and / or strain that differ from the subfamily, genus, subgenus, species, and / or strain of the infectious agents from which presenting peptide are derived to produce the APCs provided herein.Tumor-Associated Antigens, Autoimmune Antigens, and Allergenic Antigens

[0146] The disease or disorder can be a disease associated with expression of a tumor-associated antigen, and the antigenic protein can be a tumor-associated antigen. A tumor- associated antigen can be a tumor-specific antigen. The tumor-associated antigen can be a neoantigen identified in a subject. In some embodiments, the tumor-associated antigen is selected from: lA01_HLA-A / m (UniProtKB: P30443); 1A02 (UniProtKB: P01892); 5T4 (UniProtKB: Q13641); ACRBP (UniProtKB: Q8NEB7); AFP (UniProtKB: P02771); AKAP4 (UniProtKB: Q5JQC9); alpha-actinin-_4 / m (UniProtKB: B4DSX0); alpha-actinin-_4 / m (UniProtKB: B4E337); alpha-actinin-_4 / m (UniProtKB: 043707); alpha-methylacyl- coenzyme A racemase (UniProtKB: A0A024RE16); alpha-methylacyl-coenzyme_A_racemase (UniProtKB: A8KAC3); ANDR (UniProtKB: Pl 0275); ART-4 (UniProtKB: Q9ULX3); ARTCl / m (UniProtKB: P52961); AURKB (UniProtKB: Q96GD4); B2MG (UniProtKB: P61769); B3GN5 (UniProtKB: Q9BYGO); B4GN1 (UniProtKB: Q00973); B7H4 (UniProtKB: Q7Z7D3); BAGE-1 (UniProtKB: Q13072); BASI (UniProtKB: P35613); BCL-2 (UniProtKB: A9QXG9); bcr / abl (UniProtKB: A9UEZ4); bcr / abl (UniProtKB: A9UEZ7); bcr / abl (UniProtKB: A9UEZ8); bcr / abl (UniProtKB: A9UEZ9); bcr / abl (UniProtKB: A9UF00); bcr / abl(UniProtKB: A9UF01); bcr / abl (UniProtKB: A9UF03); bcr / abl (UniProtKB: A9UF04); bcr / abl (UniProtKB: A9UF05); bcr / abl (UniProtKB: A9UF06); bcr / abl (UniProtKB: A9UF08); beta- catenin / m (UniProtKB: P35222); beta-catenin / m (UniProtKB: Q8WYA6); BING-4 (UniProtKB: 015213); BIRC7 (UniProtKB: Q96CA5); BRCAl / m (UniProtKB: A0A024R1V0); BRCAl / m (UniProtKB: A0A024R1V7); BRCAl / m (UniProtKB: A0A024R1Z8); BRCAl / m (UniProtKB: A0A068BFX7); BRCAl / m (UniProtKB: C6YB45); BRCAl / m (UniProtKB: C6YB47); BRCAl / m (UniProtKB: G3XAC3); BY55 (UniProtKB: 095971); calreticulin (UniProtKB: B4DHR1); calreticulin (UniProtKB: B4E2Y9); calreticulin (UniProtKB: P27797); calreticulin (UniProtKB: Q96L12); CAMEL (UniProtKB: 095987); CASP-8 / m (UniProtKB: Q14790); CASPA (UniProtKB: Q92851-4); cathepsin B (UniProtKB: A0A024R374); cathepsin B (UniProtKB: P07858); cathepsin L (UniProtKB: A0A024R276); cathepsin L (UniProtKB: P07711); cathepsin L (UniProtKB: Q9HBQ7); CD1A (UniProtKB: P06126); CD1B (UniProtKB: P29016); CD1C (UniProtKB: P29017); CD1D (UniProtKB: P15813); CD1E (UniProtKB: P15812); CD20 (UniProtKB: Pl 1836); CD22 (UniProtKB: 060926); CD22 (UniProtKB: P20273); CD22 (UniProtKB: QOEAF5); CD276 (UniProtKB: Q5ZPR3); CD33 (UniProtKB: B4DF51); CD33 (UniProtKB: P20138); CD33 (UniProtKB: Q546G0); CD3E (UniProtKB: P07766); CD3Z (UniProtKB: P20963); CD44_Isoform_l (UniProtKB: Pl 6070); CD44_Isoform_6 (UniProtKB: Pl 6070-6); CD4 (UniProtKB: P01730); CD52 (UniProtKB: P31358); CD52 (UniProtKB: Q6IBDO); CD52 (UniProtKB: V9HWN9); CD55 (UniProtKB: B1AP15); CD55 (UniProtKB: D3DT85); CD55 (UniProtKB: D3DT86); CD55 (UniProtKB: P08174); CD56 (UniProtKB: P13591); CD80 (UniProtKB: AONOP2); CD80 (UniProtKB: P33681); CD86 (UniProtKB: P42081); CD8A (UniProtKB: P01732); CDC127 / m (UniProtKB: G5EA36); CDC127 / m (UniProtKB: P30260); CDE30 (UniProtKB: P28908); CDK4 / m (UniProtKB: A0A024RBB6); CDK4 / m (UniProtKB: Pl 1802); CDK4 / m (UniProtKB: Q6LC83); CDK4 / m (UniProtKB: Q96BE9); CDKN2A / m (UniProtKB: D1LYX3); CDKN2A / m (UniProtKB: G3XAG3); CDKN2A / m (UniProtKB: K7PML8); CDKN2A / m (UniProtKB: L8E941); CDKN2A / m (UniProtKB: Q8N726); CEA (RefSeq: NP_004354); CEAM6 (UniProtKB: P40199); CH3L2 (UniProtKB: QI 5782); CLCA2 (UniProtKB: Q9UQC9); CML28 (UniProtKB: Q9NQT4); CML66 (UniProtKB: Q96RS6); COA-l / m (UniProtKB: Q5T124); coactosin-like_protein (UniProtKB: QI 4019); collagen XXIII (UniProtKB: L8EAS4); collagen XXIII (UniProtKB: Q86Y22); COX-2 (UniProtKB: Q6ZYK7); CP1B1 (UniProtKB: QI 6678); CSAG2 (UniProtKB: Q9Y5P2-2); CSAG2 (UniProtKB: Q9Y5P2); CT45A1 (UniProtKB: Q5HYN5); CT55 (UniProtKB: Q8WUE5); CT- 9 / BRD6 (UniProtKB: Q58F21); CTAG2_Isoform_LAGE-lA (UniProtKB: 075638-2); CTAG2_Isoform_LAGE-lB (UniProtKB: 075638); CTCFL (UniProtKB: Q8NI51); Cten (UniProtKB: Q8IZW8); cyclin Bl(UniProtKB: P14635); cyclin Dl (UniProtKB: P24385); cyp-B (UniProtKB: P23284); DAM-10 (UniProtKB: P43366); DEP1A (UniProtKB: Q5TB30); E7 (UniProtKB: P03129); E7 (UniProtKB: P06788); E7 (UniProtKB: Pl 7387); E7 (UniProtKB: P06429); E7 (UniProtKB: P27230); E7 (UniProtKB: P24837); E7 (UniProtKB: P21736); E7 (UniProtKB: P26558); E7 (UniProtKB: P36831); E7 (UniProtKB: P36833); E7 (UniProtKB: Q9QCZ1); E7 (UniProtKB: Q81965); E7 (UniProtKB: Q80956); EF1A2 (UniProtKB: Q05639); EFTUD2 / m (UniProtKB: Q15029); EGFR (UniProtKB: A0A0B4J1Y5); EGFR (UniProtKB: E7BSVO); EGFR (UniProtKB: L0R6G1); EGFR (UniProtKB: P00533-2); EGFR (UniProtKB: P00533); EGFR (UniProtKB: Q147T7); EGFR (UniProtKB: Q504U8); EGFR (UniProtKB: Q8NDU8); EGLN3 (UniProtKB: Q9H6Z9); ELF2 / m (UniProtKB: B7Z720); EMMPRIN (UniProtKB: Q54A51); EpCam (UniProtKB: Pl 6422); EphA2 (UniProtKB: P29317); EphA3 (UniProtKB: P29320); EphA3 (UniProtKB: Q6P4R6); ErbB3 (UniProtKB: B3KWG5); ErbB3 (UniProtKB: B4DGQ7); ERBB4 (UniProtKB: Q15303); ERG (UniProtKB: Pl 1308); ETV6 (UniProtKB: P41212); EWS (UniProtKB: Q01844); EZH2 (UniProtKB: F2YMM1); EZH2 (UniProtKB: G3XAL2); EZH2 (UniProtKB: LOR855); EZH2 (UniProtKB: Q15910); EZH2 (UniProtKB: S4S3R8); FABP7 (UniProtKB: 015540); FCGR3A_Version_l (UniProtKB: P08637); FCGR3A_Version_2 (CCDS: CCDS1232.1); FGFS (UniProtKB: P12034); FGFS (UniProtKB: Q60518); FGFR2 (UniProtKB: P21802); fibronectin (UniProtKB: A0A024R5I6); fibronectin (UniProtKB: A0A024RB01); fibronectin (UniProtKB: A0A024RDT9); fibronectin (UniProtKB: A0A024RDV5); fibronectin (UniProtKB: A6NH44); fibronectin (UniProtKB: A8K6A5); fibronectin (UniProtKB: B2R627); fibronectin (UniProtKB: B3KXM5); fibronectin (UniProtKB: B4DIC5); fibronectin (UniProtKB: B4DN21); fibronectin (UniProtKB: B4DS98); fibronectin (UniProtKB: B4DTH2); fibronectin (UniProtKB: B4DTK1); fibronectin (UniProtKB: B4DU16); fibronectin (UniProtKB: B7Z3W5); fibronectin (UniProtKB: B7Z939); fibronectin (UniProtKB: G5E9X3); fibronectin (UniProtKB: Q9H382); FOS (UniProtKB: P01100); FOXP3 (UniProtKB: Q9BZS1); FUT1 (UniProtKB: P19526); G250 (UniProtKB: QI 6790); GAGE-1 (Genbank: AAA82744); GAGE-2 (UniProtKB: Q6NT46); GAGE-3 (UniProtKB: QI 3067); GAGE-4 (UniProtKB: QI 3068); GAGE-5 (UniProtKB: QI 3069); GAGE-6 (UniProtKB: QI 3070); GAGE7b (UniProtKB: 076087); GAGE-8_(GAGE-2D) (UniProtKB: Q9UEU5); GASR (UniProtKB: P32239); GnT-V (UniProtKB: Q09328); GPC3 (UniProtKB: I6QTG3); GPC3 (UniProtKB: P51654); GPC3 (UniProtKB: Q8IYG2); GPNMB / m (UniProtKB: A0A024RA55); GPNMB / m (UniProtKB: Q14956); GPNMB / m (UniProtKB: Q8IXJ5); GPNMB / m (UniProtKB: Q96F58); GRM3 (UniProtKB: Q14832); HAGE (UniProtKB: Q9NXZ2); hepsin (UniProtKB: B2ZDQ2); hepsin (UniProtKB: P05981); Her2 / neu (UniProtKB: B4DTR1); Her2 / neu (UniProtKB: L8E8G2); Her2 / neu (UniProtKB:P04626); Her2 / neu (UniProtKB: Q9UK79); HLA-A2 / m (UniProtKB: Q95387); HLA-A2 / m (UniProtKB: Q9MYF8); homeobox_NKX3.1 (UniProtKB: Q99801); HOM-TES-85 (UniProtKB: B2RBQ6); HOM-TES-85 (UniProtKB: Q9P127); HPG1 (Pubmed: 12543784); HS71A (UniProtKB: P0DMV8); HS71B (UniProtKB: P0DMV9); HST-2 (UniProtKB: Pl 0767); hTERT (UniProtKB: 094807); iCE (UniProtKB: 000748); IF2B3 (UniProtKB: 000425); IL 10 (UniProtKB: P22301); IL-13Ra2 (UniProtKB: QI 4627); IL2-RA (UniProtKB: P01589); IL2-RB (UniProtKB: P14784); IL2-RG (UniProtKB: P31785); IL-5 (UniProtKB: P05113); IMP3 (UniProtKB: Q9NV31); ITA5 (UniProtKB: P08648); ITB1 (UniProtKB: P05556); ITB6 (UniProtKB: P18564); kallikrein-2 (UniProtKB: A0A024R4J4); kallikrein-2 (UniProtKB: A0A024R4N3); kallikrein-2 (UniProtKB: BOAZU9); kallikrein-2 (UniProtKB: B4DU77); kallikrein-2 (UniProtKB: P20151); kallikrein-2 (UniProtKB: Q6T774); kallikrein-2 (UniProtKB: Q6T775); kallikrein-4 (UniProtKB: A0A0C4DFQ5); kallikrein-4 (UniProtKB: Q5BQA0); kallikrein-4 (UniProtKB: Q96PTO); kallikrein-4 (UniProtKB: Q96PT1); kallikrein-4 (UniProtKB: Q9Y5K2); KI20A (UniProtKB: 095235); KIAA0205 (UniProtKB: Q92604); KIF2C (UniProtKB: Q99661); KK-LC-1 (UniProtKB: Q5H943); LDLR (UniProtKB: P01130); LGMN (UniProtKB: Q99538); LIRB2 (UniProtKB: Q8N423); LY6K (UniProtKB: Q17RY6); MAGAS (UniProtKB: P43359); MAGA8 (UniProtKB: P43361); MAGAB (UniProtKB: P43364); MAGE-A10 (UniProtKB: A0A024RC14); MAGE-A12 (UniProtKB: P43365); MAGE-A1 (UniProtKB: P43355); MAGE-A2 (UniProtKB: P43356); MAGE-A3 (UniProtKB: P43357); MAGE-A4 (UniProtKB: A0A024RC12); MAGE-A4 (UniProtKB: P43358); MAGE- A4 (UniProtKB: Q1RN33); MAGE-A6 (UniProtKB: A8K072); MAGE-A6 (UniProtKB: P43360); MAGE-A6 (UniProtKB: Q6FHI5); MAGE-A9 (UniProtKB: P43362); MAGE-B10 (UniProtKB: Q96LZ2); MAGE-B16 (UniProtKB: A2A368); MAGE-B17 (UniProtKB: A8MXT2); MAGE- Bl (UniProtKB: Q96TG1); MAGE-B2 (UniProtKB: 015479); MAGE-B3 (UniProtKB: 015480); MAGE-B4 (UniProtKB: 015481); MAGE-B5 (UniProtKB: Q9BZ81); MAGE-B6 (UniProtKB: Q8N7X4); MAGE-CI (UniProtKB: 060732); MAGE-C2 (UniProtKB: Q9UBF1); MAGE-C3 (UniProtKB: Q8TD91); MAGE-D1 (UniProtKB: Q9Y5V3); MAGE-D2 (UniProtKB: Q9UNF1); MAGE-D4 (UniProtKB: Q96JG8); MAGE- El (UniProtKB: Q6IAI7); MAGE-E1_(MAGE1) (UniProtKB: Q9HCI5); MAGE-E2 (UniProtKB: Q8TD90); MAGE-F1 (UniProtKB: Q9HAY2); MAGE-H1 (UniProtKB: Q9H213); MAGEL2 (UniProtKB: Q9U355); mammaglobin A (UniProtKB: QI 3296); mammaglobin A (UniProtKB: Q6NX70); MART- 1 / melan-A (UniProtKB: Q16655); MART-2 (UniProtKB: Q5VTY9); MC1 R (UniProtKB: Q01726); MC1 R (UniProtKB: Q1JUL4); MC1 R (UniProtKB: Q1JUL6); MC1 R (UniProtKB: Q1JUL8); MC1 R (UniProtKB: Q1JUL9); MC1 R (UniProtKB: Q1JUM0); MC1 R (UniProtKB: Q1JUM2); MC1 R (UniProtKB: Q1JUM3); MC1 R (UniProtKB:Q1JUM4); MC1 R (UniProtKB: Q1JUM5); MC1 R (UniProtKB: Q6UR92); MC1 R (UniProtKB: Q6UR94); MC1 R (UniProtKB: Q6UR95); MC1 R (UniProtKB: Q6UR96); MC1 R (UniProtKB: Q6UR97); MC1 R (UniProtKB: Q6UR98); MC1 R (UniProtKB: Q6UR99); MC1 R (UniProtKB: Q6URA0); MC1 R (UniProtKB: Q86YW1); MC1 R (UniProtKB: V9Q5S2); MC1 R (UniProtKB: V9Q671); MC1 R (UniProtKB: V9Q783); MC1 R (UniProtKB: V9Q7F1); MC1 R (UniProtKB: V9Q8N1); MC1 R (UniProtKB: V9Q977); MC1 R (UniProtKB: V9Q9P5); MC1 R (UniProtKB: V9Q9R8); MC1 R (UniProtKB: V9QAE0); MC1 R (UniProtKB: V9QAR2); MC1 R (UniProtKB: V9QAW3); MC1 R (UniProtKB: V9QB02); MC1 R (UniProtKB: V9QB58); MC1 R (UniProtKB: V9QBY6); MC1 R (UniProtKB: V9QC17); MC1 R (UniProtKB: V9QC66); MC1 R (UniProtKB: V9QCQ4); MC1 R (UniProtKB: V9QDF4); MC1 R (UniProtKB: V9QDN7); MC1 R (UniProtKB: V9QDQ6); M-CSF (UniProtKB: P09603); mesothelin (UniProtKB: Q13421); MITF (UniProtKB: 075030-8); MITF (UniProtKB: 075030-9); MITF (UniProtKB: 075030); MMPl l (UniProtKB: B3KQS8); MMP7 (UniProtKB: P09237); MUC-1 (Genbank: AAA60019); MUM-l / m (RefSeq: NP_116242); MUM-2 / m (UniProtKB: Q9Y5R8); MYCN (UniProtKB: P04198); MY01A (UniProtKB: Q9UBC5); MYO IB (UniProtKB: 043795); MY01C (UniProtKB: 000159); MYOID (UniProtKB: 094832); MY01E (UniProtKB: Q12965); MYO IF (UniProtKB: 000160); MY01G (UniProtKB: B0I1T2); MY01H (RefSeq: NP_001094891); NA I 7 (UniProtKB: Q3V5L5); NA88-A (Pubmed: 10790436); Neo-PAP (UniProtKB: Q9BWT3); NFYC / m (UniProtKB: Q13952); NGEP (UniProtKB: Q6IWH7); NPM (UniProtKB: P06748); NRCAM (UniProtKB: Q92823); NSE (UniProtKB: P09104); NUF2 (UniProtKB: Q9BZD4); NY-ESO-1 (UniProtKB: P78358); 0A1 (UniProtKB: P51810); OGT (UniProtKB: 015294); OS-9 (UniProtKB: B4DH11); OS-9 (UniProtKB: B4E321); OS-9 (UniProtKB: B7Z8E7); OS-9 (UniProtKB: QI 3438); osteocalcin (UniProtKB: P02818); osteopontin (UniProtKB: A0A024RDE2); osteopontin (UniProtKB: A0A024RDE6); osteopontin (UniProtKB: A0A024RDJ0); osteopontin (UniProtKB: B7Z351); osteopontin (UniProtKB: F2YQ21); osteopontin (UniProtKB: P10451); p53 (UniProtKB: P04637); PAGE-4 (UniProtKB: 060829); PAI-1 (UniProtKB: P05121); PAI-2 (UniProtKB: P05120); PAP (UniProtKB: Q06141); PAP (UniProtKB: Q53S56); PATE (UniProtKB: Q8WXA2); PAX3 (UniProtKB: P23760); PAXS (UniProtKB: Q02548); PD1L1 (UniProtKB: Q9NZQ7); PDCD1 (UniProtKB: QI 5116); PDEF (UniProtKB: 095238); PEC Al (UniProtKB: Pl 6284); PGCB (UniProtKB: Q96GW7); PGFRB (UniProtKB: P09619); Pim-1_-Kinase (UniProtKB: A0A024RD25); Pin-1 (UniProtKB: 015428); Pin-1 (UniProtKB: Q13526); Pin-1 (UniProtKB: Q49AR7); PLAC1 (UniProtKB: Q9HBJ0); PMEL (UniProtKB: P40967); PML (UniProtKB: P29590); POTEF (UniProtKB: A5A3E0); POTE (UniProtKB: Q86YR6); PRAME (UniProtKB:A0A024R1E6); PRAME (UniProtKB: P78395); PRDX5 / m (UniProtKB: P30044); PRM2 (UniProtKB: P04554); prostein (UniProtKB: Q96JT2); proteinase-3 (UniProtKB: D6CHE9); proteinase-3 (UniProtKB: P24158); PSA (UniProtKB: P55786); PSB9 (UniProtKB: P28065); PSCA (UniProtKB: D3DWI6); PSCA (UniProtKB: 043653); PSGR (UniProtKB: Q9H255); PSM (UniProtKB: Q04609); PTPRC (RefSeq: NP 002829); RAB8A (UniProtKB: P61006); RAGE-1 (UniProtKB: Q9UQ07); RARA (UniProtKB: Pl 0276); RASH (UniProtKB: P01112); RASK (UniProtKB: P01116); RASN (UniProtKB: P01111); RGSS (UniProtKB: 015539); RHAMM / CD168 (UniProtKB: 075330); RHOC (UniProtKB: P08134); RSSA (UniProtKB: P08865); RU1 (UniProtKB: Q9UHJ3); RU2 (UniProtKB: Q9UHG0); RUNX1 (UniProtKB: Q01196); S-100 (UniProtKB: V9HW39); SAGE (UniProtKB: Q9NXZ1); S ART- 1 (UniProtKB: 043290); SART-2 (UniProtKB: Q9UL01); SART-3 (UniProtKB: Q15020); SEPR (UniProtKB: Q12884); SERPINBS (UniProtKB: P36952); SIA7F (UniProtKB: Q969X2); SIA8A (UniProtKB: Q92185); SIAT9 (UniProtKB: Q9UNP4); SIRT2 / m (UniProtKB: A0A024ROG8); SIRT2 / m (UniProtKB: Q8IXJ6); SOX10 (UniProtKB: P56693); SP17 (UniProtKB: Q15506); SPNXA (UniProtKB : Q9NS26); SPXN3 (UniProtKB: Q5MJ09); SSX-1 (UniProtKB: Q16384); SSX-2 (UniProtKB: Q16385); SSX3 (UniProtKB: Q99909); SSX-4 (UniProtKB: 060224); ST1A1 (UniProtKB: P50225); STAG2 (UniProtKB: Q8N3U4-2); STAMP-1 (UniProtKB: Q8NFT2); STEAP-1 (UniProtKB: A0A024RA63); STEAP-1 (UniProtKB: Q9UHE8); Survivin-2B (UniProtKB: 015392-2); survivin (UniProtKB: 015392); SYCP1 (UniProtKB: A0A024R0I2); SYCP1 (UniProtKB: B7ZLS9); SYCP1 (UniProtKB: Q15431); SYCP1 (UniProtKB: Q3MHC4); SYT-SSX-1 (UniProtKB: A4PIV7); SYT-SSX-1 (UniProtKB: A4PIV8); SYT-SSX-2 (UniProtKB: A4PIV9); SYT-SSX-2 (UniProtKB: A4PIWO); TARP (UniProtKB: QOVGM3); TCRg (UniProtKB: A2JGV3); TF2AA (UniProtKB: P52655); TGFB1 (UniProtKB: P01137); TGFR2 (UniProtKB: P37173); TGM-4 (UniProtKB: B2R7D1); TIE2 (UniProtKB: Q02763); TKIL1 (UniProtKB: P51854); TPI / m (UniProtKB: P60174); TRGV11 (UniProtKB: Q99601); TRGV9 (UniProtKB: A4D1X2); TRGV9 (UniProtKB: Q99603); TRGV9 (UniProtKB: Q99604); TRPC1 (UniProtKB: P48995); TRP-p8 (UniProtKB: Q7Z2W7); TSG10 (UniProtKB: Q9BZW7); TSPY1 (UniProtKB: Q01534); TVC_(TRGV3) (Genbank: M13231.1); TX101 (UniProtKB: Q9BY14-2); tyrosinase (UniProtKB: A0A024DBG7); tyrosinase (UniProtKB: L8B082); tyrosinase (UniProtKB: L8B086); tyrosinase (UniProtKB: L8B0B9); tyrosinase (UniProtKB: 075767); tyrosinase (UniProtKB: P14679); tyrosinase (UniProtKB: U3M8N0); tyrosinase (UniProtKB: U3M9D5); tyrosinase (UniProtKB: U3M9J2); TYRP1 (UniProtKB: Pl 7643); TYRP2 (UniProtKB: P40126); UPA (UniProtKB: Q96NZ9); VEGFR1 (UniProtKB: B5A924); WT1 (UniProtKB: A0A0H5AUY0); WT1 (UniProtKB: P19544); WT1 (UniProtKB: Q06250); and XAGE1-n-(UniProtKB: Q9HD64).

[0147] The disease or disorder can be an autoimmune disease or disorder, and the antigenic protein can be an autoimmune antigen. The autoimmune antigen can be an autoimmune antigen listed in Table 3. Autoimmune antigens include, but are not limited to, one or more of myelin basic protein (MBP), proteolipid protein (PLP), and myelin oligodendrocyte glycoprotein (MOG), in each case associated with multiple sclerosis (MS); CD44, preproinsulin, proinsulin, insulin, glutamic acid decaroxylase (GAD65), tyrosine phosphatase-like insulinoma antigen 2 (IA2), zinc transporter ((ZnT8), and heat shock protein 60 (HSP60), in each case associated with diabetes Typ I; interphotoreceptor retinoid-binding protein (IRBP) associated with autoimmune uveitis; acetylcholine receptor AchR, and insulin-like growth factor- 1 receptor (IGF-1R), in each case associated with Myasthenia gravis; M-protein from beta-hemolytic streptocci (pseudo-autoantigen) associated with Rheumatic Fever, or any combination thereof. Autoimmune antigens (antigens associated with autoimmune disease or autoantigens) can be selected from autoantigens associated with autoimmune diseases selected from Addison disease (autoimmune adrenalitis, Morbus Addison), alopecia areata, Addison's anemia (Morbus Biermer), autoimmune hemolytic anemia (AIHA), autoimmune hemolytic anemia (AIHA) of the cold type (cold hemagglutinine disease, cold autoimmune hemolytic anemia (AIHA) (cold agglutinin disease), (CHAD)), autoimmune hemolytic anemia (AIHA) of the warm type (warm AIHA, warm autoimmune haemolytic anemia (AIHA)), autoimmune hemolytic Donath- Landsteiner anemia (paroxysmal cold hemoglobinuria), antiphospholipid syndrome (APS), atherosclerosis, autoimmune arthritis, arteriitis temporalis, Takayasu arteriitis (Takayasu's disease, aortic arch disease), temporal arteriitis / giant cell arteriitis, autoimmune chronic gastritis, autoimmune infertility, autoimmune inner ear disease (AIED), Basedow's disease (Morbus Basedow), Bechterew's disease (Morbus Bechterew, ankylosing spondylitis, spondylitis ankylosans), Behcet's syndrome (Morbus Behcet), bowel disease including autoimmune inflammatory bowel disease (including colitis ulcerosa (Morbus Crohn, Crohn's disease), cardiomyopathy, particularly autoimmune cardiomyopathy, idiopathic dilated cardiomyopathy (DCM), celiac sprue dermatitis (gluten mediated enteropathia), chronic fatigue immune dysfunction syndrome (CFIDS), chronic inflammatory demyelinating polyneuropathy (CIDP), chronic polyarthritis, Churg-Strauss syndrome, cicatricial pemphigoid, Cogan syndrome, CREST syndrome (syndrom with Calcinosis cutis, Raynaud phenomenon, motility disorders of the esophagus, sklerodaktylia and teleangiectasia), Crohn's disease (Morbus Crohn, colitis ulcerosa), dermatitis herpetiformis during, dermatologic autoimmune diseases, dermatomyositis, Diabetes, Diabetes mellitus Type 1 (type I diabetes, insuline dependent Diabetes mellitus), Diabetes mellitus Type 2 (type II diabetes), essential mixed cryoglobulinemia, essential mixedcryoglobulinemia, fibromyalgia, fibromyositis, Goodpasture syndrome (anti-GBM mediated glomerulonephritis), graft versus host disease, Guillain-Barre syndrome (GBM, Polyradikuloneuritis), haematologic autoimmune diseases, Hashimoto thyroiditis, hemophilia, acquired hemophilia, hepatitis, autoimmune hepatitis, particularly autoimmune forms of chronic hepatitis, idiopathic pulmonary fibrosis (IPF), idiopathic thrombocytopenic purpura, Immuno- thrombocytopenic purpura (Morbus Werlhof; ITP), IgA nephropathy, infertility, autoimmune infertility, juvenile rheumatoid arthritis (Morbus Still, Still syndrome), Lambert-Eaton syndrome, lichen planus, lichen sclerosus, lupus erythematosus, systemic lupus erythematosus (SLE), lupus erythematosus (discoid form), Lyme arthritis (Lyme disease, borrelia arthritis), Meniere's disease (Morbus Meniere); mixed connective tissue disease (MCTD) multiple sclerosis (MS, encephalomyelitis disseminate, Charcot's disease), Myasthenia gravis (myasthenia, MG), myosits, polymyositis, neural autoimmune diseases, neurodermitis, pemphigus vulgaris, bullous pemphigoid, scar forming pemphigoid; polyarteriitis nodosa (periarteiitis nodosa), polychondritis (panchondritis), polyglandular (autoimmune) syndrome (PGA syndrome, Schmidt's syndrome), Polymyalgia rheumatica, primary agammaglobulinemia, primary biliary cirrhosis PBC, primary autoimmune cholangitis), progressive systemic sclerosis (PSS), Psoriasis, Psoriasis vulgaris, Raynaud's phenomena, Reiter's syndrome (Morbus Reiter, urethral conjunctive synovial syndrome)), rheumatoid arthritis (RA, chronic polyarthritis, rheumatic disease of the joints, rheumatic fever), sarcoidosis (Morbus Boeck, Besnier-Boeck- Schaumann disease), stiff-man syndrome, Sclerodermia, Scleroderma, Sjogren's syndrome, sympathetic ophtalmia; Transient gluten intolerance, transplanted organ rejection, uveitis, autoimmune uveiitis, Vasculitis, Vitiligo, (leucoderma, piebold skin), and Wegner's disease (Morbus Wegner, Wegner's granulomatosis).

[0148] The disease or disorder can be an allergic disease or disorder, and the antigenic protein can be an allergenic antigen. In some embodiments, the allergenic antigen is selected from: Acarus spp (Aca s 1, Aca s 10, Aca s 10.0101, Aca s 13, Aca s 13.0101, Aca s 2, Aca s 3, Aca s 7, Aca s 8), Acanthocybium spp (Aca so 1), Acanthocheilonema spp (Aca v 3, Aca v 3.0101), Acetes spp (Ace ja 1), Actinidia spp (Act a 1, Act c 1, Act c 10, Act c 10.0101, Act c 2, Act c 4, Act c 5, Act c 5.0101, Act c 8, Act c 8.0101, Act c Chitinase, Act d 1, Act d 1.0101, Act d 10, Act d 10.0101, Act d 10.0201, Act d 11, Act d 11.0101, Act d 2, Act d 2.0101, Act d 3, Act d 3.0101, Act d 3.02, Act d 4, Act d 4.0101, Act d 5, Act d 5.0101, Act d 6, Act d 6.0101, Act d 7, Act d 7.0101, Act d 8, Act d 8.0101, Act d 9, Act d 9.0101, Act d Chitinase, Act e 1, Act e 5), Acyrthosiphon spp (Acy pi 7, Acy pi 7.0101, Acy pi 7.0102), Adenia spp (Ade v RIP), Aedes spp (Aed a 1, Aed a 1.0101, Aed a 2, Aed a 2.0101, Aed a 3, Aed a 3.0101, Aed a 4, Aed a 7, Aed a 7.0101, Aed a 7.0102, Aed a 7.0103, Aed a 7.0104, Aed a 7.0105, Aed a7.0106, Aed a 7.0107, Aed a 7.0108, Aed a 7.0109, Aed a 7.0110, Aed a 7.0111, Aed al 1, Aed al 3, Aed al 37 kD, Aed v 37 kD, Aed v 63 kD), Aegilops spp (Aeg ta 28, Aeg ta alpha_Gliadin, Aeg um 28, Aeg un 28), Aethaloperca spp (Aet ro 1), Agropyron spp (Agr c 7), Agrostis spp (Agr ca 1, Agr ca 5, Agr g 1, Agr g 4, Agr s 5), Agrobacterium spp (Agr sp CP4 EPSPS), Ailuropoda spp (Ail me Phosvitin, Ail me TCTP), Aix spp (Aix ga 1, Aix sp 1), Aleuroglyphus spp (Ale o 1, Ale o 10, Ale o 10.0101, Ale o 10.0102, Ale o 13, Ale o 14, Ale o 2, Ale o 20, Ale o 3, Ale o 5, Ale o 7, Ale o 8, Ale o 9), Allium spp (All a 3, All a Alliin lyase, All c 3, All c 30 kD, All c 4, All c Alliin lyase, All p Alliin lyase, All s Alliin lyase), Alnus spp (Ain g 1, Ain g 1.0101, Ain g 1 / Bet v 1 / Cor a 1 TPC7, Ain g 1 / Bet v 1 / Cor a 1 TPC9, Ain g 2, Ain g 4, Ain g 4.0101), Alopochen spp (Alo ae 1), Alopecurus spp (Alo p 1, Alo p 5), Alternaria spp (Alt a 1, Alt a 1.0101, Alt a 1.0102, Alt a 10, Alt a 10.0101, Alt a 12, Alt a 12.0101, Alt a 13, Alt a 13.0101, Alt a 2, Alt a 3, Alt a 3.0101, Alt a 4, Alt a 4.0101, Alt a 5, Alt a 5.0101, Alt a 6, Alt a 6.0101, Alt a 7, Alt a 7.0101, Alt a 70 kD, Alt a 8, Alt a 8.0101, Alt a 9, Alt a MnSOD, Alt a NTF2, Alt a TCTP, Alt ar 1, Alt arg 1, Alt b 1, Alt bl 1, Alt br 1, Alt c 1, Alt ca 1, Alt ce 1, Alt ch 1, Alt ci 1, Alt co 1, Alt cr 1, Alt ct 1, Alt cu 1, Alt cy 1, Alt d 1, Alt du 1, Alt e 1, Alt et 1, Alt eu 1, Alt ga 1, Alt gr 1, Alt j 1, Alt 1 1, Alt lo 1, Alt m 1, Alt me 1, Alt mi 1, Alt mo 1, Alto 1, Alt p 1, Alt ph 1, Alt po 1, Alt ps 1, Alt r 1, Alt s 1, Alt se 1, Alt sm 1, Alt so 1, Alt su 1, Alt t 1, Alt to 1, Alt to 1), Amaranthus spp (Ama r 2, Ama r 2.0101, Ama v 2, Ama v 2.0101, Ama v 2.0201), Ambrosia spp (Amb a 1, Amb a 1.0101, Amb a 1.0201, Amb a 1.0202, Amb a 1.0301, Amb a 1.0302, Amb a 1.0303, Amb a 1.0304, Amb a 1.0305, Amb a 1.0401, Amb a 1.0402, Amb a 1.0501, Amb a 1.0502, Amb a 10, Amb a 10.0101, Amb a 3, Amb a 3.0101, Amb a 4, Amb a 4.0101, Amb a 5, Amb a 5.0101, Amb a 6, Amb a 6.0101, Amb a 7, Amb a 7.0101, Amb a 8, Amb a 8.0101, Amb a 8.0102, Amb a 9, Amb a 9.0101, Amb a 9.0102, Amb a CPI, Amb p1, Amb p 5, Amb p 5.0101, Amb p 5.0201, Amb t 5, Amb t 5.0101, Amb t 8), Ammothea spp (Amm h 7, Amm h 7.0101), Anadara spp (Ana br 1), Ananas spp (Ana c 1, Ana c 1.0101, Ana c2, Ana c 2.0101, Ana c 2.0101 (MUXF3)), Anas spp (Ana ca 1), Anarhichas spp (Ana I I), Anacardium spp (Ana o 1, Ana o 1.0101, Ana o 1.0102, Ana o 2, Ana o 2.0101, Ana o 3, Ana o 3.0101), Anas spp (Ana p 1, Ana p 2, Ana p 3), Anguilla spp (Ang a 1, Ang j 1), Anisakis spp (Ani s 1, Ani s 1.0101, Ani s 10, Ani s 10.0101, Ani s 11, Ani s 11.0101, Ani s 12, Ani s 12.0101, Ani s 2, Ani s 2.0101, Ani s 24 kD, Ani s 3, Ani s 3.0101, Ani s 4, Ani s 4.0101, Ani s 5, Ani s 5.0101, Ani s 6, Ani s 6.0101, Ani s 7, Ani s 7.0101, Ani s 8, Ani s 8.0101, Ani s 9, Ani s 9.0101, Ani s CCOS3, Ani s Cytochrome B, Ani s FBPP, Ani s NADHDS4L, Ani s NARaS, Ani s PEPB, Ani s Troponin), Annona spp (Ann c Chitinase), Anopheles spp (Ano da 17, Ano da 17.0101, Ano da 27, Ano da 27.0101, Ano da 7, Ano da 7.0101, Ano g 7, Ano g 7.0101), Anser spp (Ans a 1, Ans a 2, Ans a 3, Ans in 1), Anthoxanthum spp (Ant o 1, Ant o 1.0101, Ant o 12,Ant o 13, Ant o 2, Ant o 4, Ant o 5, Ant o 6, Ant o 7), Apis spp (Api c 1, Api c 1.0101, Api c 10, Api c 2, Api c 4, Api d 1, Api d 1.0101, Api d 4, Api fl 4), Apium spp (Api g 1, Api g 1.0101, Api g 1.0201, Api g 2, Api g 2.0101, Api g 3, Api g 3.0101, Api g 4, Api g 4.0101, Api g 5, Api g 5.0101, Api g 6, Api g 6.0101), Apis spp (Api m 1, Api m 1.0101, Api m 10, Api m 10.0101, Api m i l, Api m 11.0101, Api m 11.0201, Api m 13 kD, Api m 2, Api m 2.0101, Api m 3, Api m 3.0101, Api m 4, Api m 4.0101, Api m 5, Api m 5.0101, Api m 6, Api m 6.0101, Api m 7, Api m 7.0101, Api m 8, Api m 8.0101, Api m 9, Api m 9.0101, Api m A1-A2, Api m A1-A2- A3, Api m Apalbumin 1, Api m Apalbumin 2, Api me 1, Api me 4), Arachis spp (Ara d 2, Ara d 6, Ara f 3, Ara f 4, Ara h 1, Ara h 1.0101, Ara h 10, Ara h 10.0101, Ara h 10.0102, Ara h 11, Ara h 11.0101, Ara h 2, Ara h 2.0101, Ara h 2.0102, Ara h 2.0201, Ara h 2.0202, Ara h 3, Ara h 3.0101, Ara h 4, Ara h 4.0101, Ara h 5, Ara h 5.0101, Ara h 6, Ara h 6.0101, Ara h 7, Ara h 7.0101, Ara h 7.0201, Ara h 7.0202, Ara h 8, Ara h 8.0101, Ara h 8.0201, Ara h 9, Ara h 9.0101, Ara h 9.0201, Ara h Agglutinin, Ara h Oleosin 18 kD, Ara i 2, Ara i 6), Arabidopsis spp (Ara t 3, Ara t 8, Ara t GLP), Archosargus spp (Arc pr 1), Archaeopotamobius spp (Arc s 8, Arc s 8.0101), Aequipecten spp (Arg i 1), Ar gas spp (Arg r 1, Arg r 1.0101), Ariopsis spp (Ari fe 1), Armoracia spp (Arm r HRP), Arrhenatherum spp (Arr e 1, Arr e 5), Artemisia spp (Art a 1, Art ap 1), Artemia spp (Art fr 1, Art fr 1.0101, Art fr 5, Art fr 5.0101), Arthrobacter spp (Art gl CO), Achorion spp (Art gy 7), Artocarpus spp (Art h 17 kD, Art h 4), Arthrospira spp (Art pl beta_Phycocyanin), Artemisia spp (Art v 1, Art v 1.0101, Art v 1.0102, Art v 1.0103, Art v 1.0104, Art v 1.0105, Art v 1.0106, Art v 1.0107, Art v 2, Art v 2.0101, Art v 3, Art v 3.0101, Art v 3.0201, Art v 3.0202, Art v 3.0301, Art v 4, Art v 4.0101, Art v 4.0201, Art v 47 kD, Art v 5, Art v 5.0101, Art v 6, Art v 6.0101, Art v 60 kD), Arthroderma spp (Art va 4), Ascaris spp (Asc 13, Asc 1 3.0101, Asc 1 3.0102, Asc 1 34 kD, Asc s 1, Asc s 1.0101, Asc s 3, Asc s 3.0101, Asc s GST), Aspergillus spp (Asp aw Glucoamylase, Asp c 22, Asp f 1, Asp f 1.0101, Asp f 10, Asp f 10.0101, Asp f 11, Asp f 11.0101, Asp f 12, Asp f 12.0101, Asp f 13, Asp f 13.0101, Asp f 15, Asp f 15.0101, Asp f 16, Asp f 16.0101, Asp f 17, Asp f 17.0101, Asp f 18, Asp f 18.0101, Asp f 2, Asp f 2.0101, Asp f 22, Asp f 22.0101, Asp f 23, Asp f 23.0101, Asp f 27, Asp f 27.0101, Asp f 28, Asp f 28.0101, Asp f 29, Asp f 29.0101, Asp f 3, Asp f 3.0101, Asp f 34, Asp f 34.0101, Asp f 4, Asp f 4.0101, Asp f 5, Asp f 5.0101, Asp f 56 kD, Asp f 6, Asp f 6.0101, Asp f 7, Asp f 7.0101, Asp f 8, Asp f 8.0101, Asp f 9, Asp f 9.0101, Asp f AfCalAp, Asp f AT_V, Asp f Catalase, Asp f Chitosanase, Asp f CP, Asp f DPPV, Asp f FDH, Asp f gamma Actin, Asp f Glucosidase, Asp f GPI, Asp f GST, Asp f GT, Asp f IAO, Asp f IPMI, Asp f LPL1, Asp f LPL3, Asp f Mannosidase, Asp f MDH, Asp f PL, Asp f PUP, Asp f RPS3, Asp f SXR, Asp fl 13, Asp fl 13.0101, Asp fl 18, Asp fl 2, Asp fl 21, Asp fl 3, Asp fl 4, Asp fl 7, Asp fl 8, Asp fl 9, Asp me Sea prose, Asp n 14, Asp n 14.0101, Asp n 18, Asp n 18.0101, Asp n 25, Asp n25.0101, Asp n 30, Asp n Glucoamylase, Asp n Hemicellulase, Asp n Pectinase, Asp o 13, Asp o 13.0101, Asp o 21, Asp o 21.0101, Asp o 3, Asp o 4, Asp o 7, Asp o 8, Asp o Lactase, Asp o Lipase, Asp oc 13, Asp r 1, Asp sa AP, Asp sp Glucoamylase, Asp sp Glucoseoxidase, Asp sp PL, Asp sp PME, Asp sy 13, Asp v 13, Asp v 13.0101, Asp v Catalase A, Asp v Enolase, Asp v GAPDH, Asp v MDH, Asp v SXR), Asparagus spp (Aspa o 1, Aspa o 1.01, Aspa o 1.02, Aspa o 17 kD, Aspa o 4), Aspergillus spp (Aspe ni 2, Aspe ni 3, Aspe ni 4, Aspe ni 7, Aspe ni 8, Aspe ni 9), Avena spp (Ave s 1, Ave s 12, Ave s 13, Ave s 2, Ave s 4, Ave s 5, Ave s 7), Babylonia spp (Bab ja 1), Bacillus spp (Bac al Subtilisin, Bac cl Subtilisin, Bac I Subtilisin, Bac li aA, Bac li Subtilisin), Bactrocera spp (Bac ol 27, Bac ol 27.0101), Bacillus spp (Bac sp aAl, Bac sp aA3, Bac sp Decarboxylase, Bac st amyM, Bac su Subtilisin, Bac t CrylAb, Bac t CrylFa, Bac t Cry3Bbl, Bac t Cry9c), Bagre spp (Bag ma 1), Batistes spp (Bal ca 1), Balanus spp (Bal r 1, Bal r 1.0101), Beauveria spp (Bea b Aid, Bea b Enol, Bea b f2, Bea b Hex), Bertholletia spp (Ber e 1, Ber e 1.0101, Ber e 2, Ber e 2.0101), Beryx spp (Ber sp 1), Betula spp (Bet ab 1, Bet al 1, Bet ch 1, Bet co 1, Bet da 1, Bet gr 1, Bet hu 1, Bet le 1, Bet me 1, Bet n 1, Bet p 1, Bet pa 1, Bet po 1, Bet pu 1, Bet pu 2, Bet pu 4, Bet pu 6, Bet pu 7, Bet sc 1, Bet ut 1, Bet v 1, Bet v 1 B 1-131- 131, Bet v 1 fv Mai 4x, Bet v 1.0101, Bet v 1.0102, Bet v 1.0103, Bet v 1.0201, Bet v 1.0301, Bet v 1.0401, Bet v 1.0402, Bet v 1.0501, Bet v 1.0601, Bet v 1.0602, Bet v 1.0701, Bet v 1.0801, Bet v 1.0901, Bet v 1.1001, Bet v 1.1101, Bet v 1.1201, Bet v 1.1301, Bet v 1.1401, Bet v 1.1402, Bet v 1.1501, Bet v 1.1502, Bet v 1.1601, Bet v 1.1701, Bet v 1.1801, Bet v 1.1901, Bet v 1.2001, Bet v 1.2101, Bet v 1.2201, Bet v 1.2301, Bet v 1.2401, Bet v 1.2501, Bet v 1.2601, Bet v 1.2701, Bet v 1.2801, Bet v 1.2901, Bet v 1.3001, Bet v 1.3101, Bet v 2, Bet v 2.0101, Bet v 3, Bet v 3.0101, Bet v 4, Bet v 4.0101, Bet v 6, Bet v 6.0101, Bet v 6.0102, Bet v 7, Bet v 7.0101, Bet v 8, Bet v Glucanase), Beta spp (Beta v 1, Beta v 1.0101, Beta v 2, Beta v 2.0101), Blattella spp (Bia g 1, Bia g 1.0101, Bia g 1.0102, Bia g 1.0103, Bia g 1.0201, Bia g 1.0202, Bia g 2, Bia g 2.0101, Bia g 2.0201, Bia g 36 kD, Bia g 4, Bia g 4.0101, Bia g 4.0201, Bia g 5, Bia g 5.0101, Bia g 5.0201, Bia g 6, Bia g 6.0101, Bia g 6.0201, Bia g 6.0301, Bia g 7, Bia g 7.0101, Bia g 8, Bia g 8.0101, Bia g 9, Bia g Enolase, Bia g GSTD1, Bia g RACK1, Bia g TPI, Bia g Trypsin, Bia g Vitellogenin), Blatta spp (Bia o 1, Bia o 7), Blomia spp (Bio t 1, Bio t 1.0101, Bio t 1.0201, Bio t 10, Bio t 10.0101, Bio t 10.0102, Bio t 11, Bio t 11.0101, Bio t 12, Bio t 12.0101, Bio t 12.0102, Bio t 13, Bio t 13.0101, Bio t 14, Bio 1 15, Bio t 18, Bio t 19, Bio t 19.0101, Bio t 2, Bio 12.0101, Bio t 2.0102, Bio t 2.0103, Bio 120, Bio t 21, Bio 121.0101, Bio t 3, Bio t 3.0101, Bio 14, Bio t 4.0101, Bio t 5, Bio t 5.0101, Bio t 6, Bio t 6.0101, Bio t 7, Bio t 8, Bio t 9, Bio t HSP70), Bombus spp (Bom ar 4, Bom by 4, Bom p 1, Bom p 1.0101, Bom p 2, Bom p 3, Bom p 4, Bom p 4.0101, Bom t 1, Bom t 1.0101, Bom t 4, Bom 14.0101), Bombyx spp (Bomb m 1, Bomb m 1.0101, Bomb m 7, Bomb m 7.0101, Bomb m 7.0102, Bomb m 7.0103,Bomb m 7.0104, Bomb m 7.0105, Bomb m 7.0106), Boophilus spp (Boo m 1, Boo m 7, Boo m 7.0101), Bos spp (Bos d 2, Bos d 2.0101, Bos d 2.0102, Bos d 2.0103, Bos d 3, Bos d 3.0101, Bos d 4, Bos d 4.0101, Bos d 5, Bos d 5.0101, Bos d 5.0102, Bos d 6, Bos d 6 (MDA), Bos d 6.0101, Bos d 7, Bos d 7.0101, Bos d 8, Bos d 8 alphaSl, Bos d 8 alphaS2, Bos d 8 beta, Bos d 8 kappa, Bos d alpha2I, Bos d alpha2I.0101, Bos d Chymosin, Bos d Fibrin, Bos d Gelatin, Bos d HG, Bos d Insulin, Bos d Lactoferrin, Bos d Lactoperoxidase, Bos d Myoglobin, Bos d OBP, Bos d OSCP, Bos d Phosvitin, Bos d PLA2, Bos d PRVB, Bos d Thrombin, Bos d TI, Bos gr ALA, Bos gr Myoglobin), Bothrops spp (Bot as 1, Bot at 1), Bouteloua spp (Bou g 1), Biting spp (Boy ov 1), Brama spp (Bra du 1), Brassica spp (Bra j 1, Bra j 1.0101, Bra n 1, Bra n 1.0101, Bra n 4, Bra n 7, Bra n 8, Bra n PG, Bra ni 8, Bra o 3, Bra o 3.0101, Bra r 1, Bra r 1.0101, Bra r 2, Bra r 2.0101, Bra r 3, Bra r 4, Bra r 7), Bromus spp (Bro a 1, Bro a 4), Brosme spp (Bro br 1), Bromus spp (Bro i 1, Bro i 5, Bro i 7), Brugia spp (Bru m 3, Bru m 3.0101, Bru m Bm33), Bubalus spp (Bub b ALA, Bub b BLG, Bub b Casein, Bub b Casein alphaSl, Bub b Casein alphaS2, Bub b Casein beta, Bub b Casein kappa), Caenorhabditis spp (Cae b 3, Cae b 3.0101, Cae br 3, Cae br 3.0101, Cae e 3, Cae e 3.0101, Cae e 3.0102, Cae re 13, Cae re 13.0101), Cajanus spp (Caj c l), Caligus spp (Cal cl 1, Cal cl 1.0101, Cal cl 1.0102), Calamus spp (Cal le 1), Callinectes spp (Cal s 2), Camelus spp (Cam d ALA, Cam d Casein, Cam d Casein alphaSl, Cam d Casein alphaS2, Cam d Casein beta, Cam d Casein kappa), Camponotus spp (Cam fl 7, Cam fl 7.0101), Canis spp (Can f 1, Can f 1.0101, Can f 2, Can f 2.0101, Can f 3, Can f 3.0101, Can f 4, Can f 4.0101, Can f 5, Can f 5.0101, Can f 6, Can f 6.0101, Can f Feldl-like, Can f Homs2-like, Can f Phosvitin, Can f TCTP), Canthidermis spp (Can ma 1), Cancer spp (Can mg 2, Can p 1), Cannabis spp (Can s 3), Candida spp (Cand a 1, Cand a 1.0101, Cand a 3, Cand a 3.0101, Cand a CAAP, Cand a CyP, Cand a Enolase, Cand a FPA, Cand a MnSOD, Cand a PGK, Cand b 2, Cand b 2.0101, Cand b FDH, Cand r Lipase), Capsicum spp (Cap a 1, Cap a 1.0101, Cap a 17 kD, Cap a 2, Cap a 2.0101, Cap a 30 kD, Cap a Glucanase, Cap ch 17 kD), Caprella spp (Cap e l), Capra spp (Cap h ALA, Cap h BLG, Cap h Casein, Cap h Casein alphaSl, Cap h Casein alphaS2, Cap h Casein beta, Cap h Casein kappa, Cap h GSA), Capitulum spp (Cap m 1), Carassius spp (Car au 1), Carpinus spp (Car b 1, Car b 1.0101, Car b 1.0102, Car b 1.0103, Car b 1.0104, Car b 1.0105, Car b 1.0106, Car b 1.0107, Car b 1.0108, Car b 1.0109, Car b 1.0110, Car b 1.0111, Car b 1.0112, Car b 1.0113, Car b 1.0201, Car b 1.0301, Car b 1.0302, Car b 2, Car b 4), Caranx spp (Car cr 1), Carya spp (Car i 1, Car i 1.0101, Car i 2, Car i 4, Car i 4.0101), Carcinus spp (Car ma 2), Caryota spp (Car mi 2), Carica spp (Car p 1, Car p Chitinase, Car p Chymopapain, Car p Endoproteinase), Castanea spp (Cas c 24 kD, Cas s 1, Cas s 1.0101, Cas s 1.0102, Cas s 1.0103, Cas s 2, Cas s 5, Cas s 5.0101, Cas s 8, Cas s 8.0101, Cas s 9, Cas s 9.0101), Catharanthus spp (Cat r 1, Cat r 1.0101, Cat r 17 kD, Cat r2), Caulolatilus spp (Cau ch 1), Cavia spp (Cav p 1, Cav p 1.0101, Cav p 2, Cav p 2.0101, Cav p 3, Cav p 3.0101, Cav p Gelatin, Cav p GSA), Centropristis spp (Cen s i), Cephalopholis spp (Cep so 1), Charybdis spp (Cha f 1, Cha f 1.0101), Chaetodipterus spp (Cha fa 1), Chamaecyparis spp (Cha o 1, Cha o 1.0101, Cha o 2, Cha o 2.0101), Chenopodium spp (Che a 1, Che a 1.0101, Che a 2, Che a 2.0101, Che a 3, Che a 3.0101), Chironomus spp (Chi k 1, Chi k 10, Chi k 10.0101), Chinchilla spp (Chi 1 21 kD_a, Chi 1 21 kD_b), Chionoecetes spp (Chi o 1, Chi o 1.0101, Chi o 2, Chi o 4, Chi o 6, Chi o alpha Actin, Chi o SERCA), Chironomus spp (Chi t 1, Chi t 1.0101, Chi t 1.0201, Chi t 2, Chi t 2.0101, Chi t 2.0102, Chi t 3, Chi t 3.0101, Chi t 4, Chi t 4.0101, Chi t 5, Chi t 5.0101, Chi t 6, Chi t 6.0101, Chi t 6.0201, Chi t 7, Chi t 7.0101, Chi t 8, Chi t 8.0101, Chi t 9, Chi t 9.0101), Chlamys spp (Chi n 1), Chloephaga spp (Chi pi 1), Chortoglyphus spp (Cho a 10), Chrysomela spp (Chr tr 7, Chr tr 7.0101), Cicer spp (Cic a 2S Albumin, Cic a Albumin), Cichorium spp (Cic i 1), Cimex spp (Cim I Nitrophorin), Citrus spp (Cit 11, Cit I 3, Cit 1 3.0101), Citrullus spp (Cit la 2, Cit la MDH, Cit la TPI), Citrus spp (Cit r 3, Cit r 3.0101, Cit s 1, Cit s 1.0101, Cit s 2, Cit s 2.0101, Cit s 3, Cit s 3.0101, Cit s 3.0102, Cit s IFR), Cladosporium spp (Cla c 14, Cla c 14.0101, Cla c 9, Cla c 9.0101, Cla h 1, Cla h 10, Cla h 10.0101, Cla h 12, Cla h 12.0101, Cla h 2, Cla h 2.0101, Cla h 42 kD, Cla h 5, Cla h 5.0101, Cla h 6, Cla h 6.0101, Cla h 7, Cla h 7.0101, Cla h 8, Cla h 8 CSP, Cla h 8.0101, Cla h 9, Cla h 9.0101, Cla h abH, Cla h GST, Cla h HChl, Cla h HSP70, Cla h NTF2, Cla h TCTP), Clostridium spp (Clo hi Collagenase, Clo t Toxoid), Clupea spp (Clu h 1, Clu h 1.0101, Clu h 1.0201, Clu h 1.0301), Cocos spp (Coc n 2, Coc n 4, Coc n 5), Coccidioides spp (Coc po 8), Coffea spp (Cof a 1, Cof a 1.0101), Columba spp (Col I PSA), Coprinus spp (Cop c 1, Cop c 1.0101, Cop c 2, Cop c 2.0101, Cop c 3, Cop c 3.0101, Cop c 4, Cop c 5, Cop c 5.0101, Cop c 6, Cop c 7, Cop c 7.0101), Corylus spp (Cor a 1, Cor a 1.0101, Cor a 1.0102, Cor a 1.0103, Cor a 1.0104, Cor a 1.0201, Cor a 1.0301, Cor a 1.0401, Cor a 1.0402, Cor a 1.0403, Cor a 1.0404, Cor a 10, Cor a 10.0101, Cor a l l, Cor a 11.0101, Cor a 12, Cor a 12.0101, Cor a 13, Cor a 13.0101, Cor a 14, Cor a 14.0101, Cor a 2, Cor a 2.0101, Cor a 2.0102, Cor a 8, Cor a 8.0101, Cor a 9, Cor a 9.0101), Corynebacterium spp (Cor d Toxoid), Corylus spp (Cor he 1), Coryphaena spp (Cor hi 1), Coriandrum spp (Cor s 1, Cor s 11 kD, Cor s 2), Cotoneaster spp (Cot I 3), Crangon spp (Cra c 1, Cra c 1.0101, Cra c 2, Cra c 2.0101, Cra c 4, Cra c 4.0101, Cra c 5, Cra c 5.0101, Cra c 6, Cra c 6.0101, Cra c 8, Cra c 8.0101), Crassostrea spp (Cra g 1), Cricetus spp (Cri c HSA), Crivellia spp (Cri pa 1), Crocus spp (Cro s 1, Cro s 1.0101, Cro s 2, Cro s 2.0101, Cro s 3, Cro s 3.01, Cro s 3.02), Cryptomeria spp (Cry j 1, Cry j 1.0101, Cry j 1.0102, Cry j 1.0103, Cry j 2, Cry j 2.0101, Cry j 2.0102, Cry j 3, Cry j 3.1, Cry j 3.2, Cry j 3.3, Cry j 3.4, Cry j 3.5, Cry j 3.6, Cry j 3.7, Cry j 3.8, Cry j 4, Cry j AP, Cry j Chitinase, Cry j CPA9, Cry j IFR, Cry j LTP, Cry j P1-P2), Cryphonectria spp (Cry p AP), Ctenocephalides spp(Cte f 1, Cte f 1.0101, Cte f 2, Cte f 2.0101, Cte f 3, Cte f 3.0101), Ctenopharyngodon spp (Cte id 1), Cucumis spp (Cue m 1, Cue m 1.0101, Cue m 2, Cue m 2.0101, Cue m 3, Cue m 3.0101, Cue m Lee 17, Cue m MDH), Cucurbita spp (Cue ma 18 kD, Cue ma 2, Cue p 2, Cue p AscO), Cucumis spp (Cue s 2), Culicoides spp (Cui n 1, Cui n 10, Cui n i l, Cui n 2, Cui n 3, Cui n 4, Cui n 5, Cui n 6, Cui n 7, Cui n 8, Cui n 9, Cui n HSP70), Culex spp (Cui q 28 kD, Cui q 35 kD, Cui q 7, Cui q 7.0101, Cui q 7.0102), Culicoides spp (Cui so 1), Cuminum spp (Cum c 1, Cum c 2), Cupressus spp (Cup a 1, Cup a 1.0101, Cup a 1.02, Cup a 2, Cup a 3, Cup a 4, Cup a 4.0101, Cups 1, Cups 1.0101, Cups 1.0102, Cup s 1.0103, Cup s 1.0104, Cup s 1.0105, Cup s 3, Cup s 3.0101, Cup s 3.0102, Cup s 3.0103, Cup s 8), Cochliobolus spp (Cur 11, Cur 11.0101, Cur I 2, Cur I 2.0101, Cur I 3, Cur I 3.0101, Cur I 4, Cur I 4.0101, Cur I ADH, Cur I GST, Cur I MnSOD, Cur I Oryzin, Cur I Trx, Cur I ZPS1), Cyanochen spp (Cya cy 1), Cynoscion spp (Cyn ar 1), Cynosurus spp (Cyn er 1, Cyn er 5), Cynodon spp (Cyn d 1, Cyn d 1.0101, Cyn d 1.0102, Cyn d 1.0103, Cyn d 1.0104, Cyn d 1.0105, Cyn d 1.0106, Cyn d 1.0107, Cyn d 1.0201, Cyn d 1.0202, Cyn d 1.0203, Cyn d 1.0204, Cyn d 10, Cyn d 11, Cyn d 12, Cyn d 12.0101, Cyn d 13, Cyn d 15, Cyn d 15.0101, Cyn d 2, Cyn d 22, Cyn d 22.0101, Cyn d 23, Cyn d 23.0101, Cyn d 24, Cyn d 24.0101, Cyn d 4, Cyn d 5, Cyn d 6, Cyn d 7, Cyn d 7.0101), Cynoscion spp (Cyn ne 1), Cynomys spp (Cyn sp Lipocalin), Cyprinus spp (Cyp c 1, Cyp c 1.01, Cyp c 1.02), Daboia spp (Dab ru 1), Dactylis spp (Dae g 1, Dae g 1.01, Dae g 1.0101, Dae g 1.02, Dae g 12, Dae g 13, Dae g 2, Dae g 2.0101, Dae g 3, Dae g 3.0101, Dae g 4, Dae g 4.0101, Dae g 5, Dae g 5.0101, Dae g 7), Dama spp (Dam d CSA), Danio spp (Dan re 1, Dan re 2, Dan re alpha21, Dan re CK), Dasyatis spp (Das ak 1, Das am 1, Das sa 1), Daucus spp (Dau c 1, Dau c 1.0101, Dau c 1.0102, Dau c 1.0103, Dau c 1.0104, Dau c 1.0105, Dau c 1.0201, Dau c 1.0301, Dau c 3, Dau c 4, Dau c 4.0101, Dau c CyP), Decapterus spp (Dec ru 1), Dendronephthya spp (Den n 1, Den n 1.0101), Dermatophagoides spp (Der f 1, Der f 1.0101, Der f 1.0102, Der f 1.0103, Der f 1.0104, Der f 1.0105, Der f 1.0106, Der f 1.0107, Der f 1.0108, Der f 1.0109, Der f 1.0110, Der f 10, Der f 10.0101, Der f 10.0102, Der f 11, Der f 11.0101, Der f 13, Der f 13.0101, Der f 14, Der f 14.0101, Der f 15, Der f 15.0101, Der f 16, Der f 16.0101, Der f 17, Der f 17.0101, Der f 18, Der f 18.0101, Der f 2, Der f 2.0101, Der f 2.0102, Der f 2.0103, Der f 2.0104, Der f 2.0105, Der f 2.0106, Der f 2.0107, Der f 2.0108, Der f 2.0109, Der f 2.0110, Der f 2.0111, Der f 2.0112, Der f 2.0113, Der f 2.0114, Der f 2.0115, Der f 2.0116, Der f 2.0117, Der f 20, Der f 21, Der f 22, Der f 22.0101, Der f 3, Der f 3.0101, Der f 4, Der f 5, Der f 6, Der f 6.0101, Der f 7, Der f 7.0101, Der f 8, Der f 9, Der f HSP70), Dermanyssus spp (Der g 10, Der g 10.0101), Dermatophagoides spp (Der m 1, Der m 1.0101, Der p 1, Der p 1.0101, Der p 1.0102, Der p 1.0103, Der p 1.0104, Der p 1.0105, Der p 1.0106, Der p 1.0107, Der p 1.0108, Der p 1.0109, Der p 1.0110, Der p 1.0111, Der p 1.0112, Der p 1.0113, Der p 1.0114, Der p 1.0115, Der p1.0116, Der p 1.0117, Der p 1.0118, Der p 1.0119, Der p 1.0120, Der p 1.0121, Der p 1.0122, Der p 1.0123, Der p 1.0124, Der p 10, Der p 10.0101, Der p 10.0102, Der p 10.0103, Der p 11, Der p 11.0101, Der p 13, Der p 14, Der p 14.0101, Der p 15, Der p 18, Der p 2, Der p 2.0101, Der p 2.0102, Der p 2.0103, Der p 2.0104, Der p 2.0105, Der p 2.0106, Der p 2.0107, Der p 2.0108, Der p 2.0109, Der p 2.0110, Der p 2.0111, Der p 2.0112, Der p 2.0113, Der p 2.0114, Der p 2.0115, Der p 20, Der p 20.0101, Der p 21, Der p 21.0101, Der p 23, Der p 23.0101, Der p 3, Der p 3.0101, Der p 4, Der p 4.0101, Der p 5, Der p 5.0101, Der p 5.0102, Der p 6, Der p 6.0101, Der p 7, Der p 7.0101, Der p 8, Der p 8.0101, Der p 9, Der p 9.0101, Der p 9.0102, Der p P1-P2, Der p P2-P1, Der s 1, Der s 2, Der s 3), Dianthus spp (Dia c RIP), Dicranopteris spp (Die I 2S Albumin), Diospyros spp (Dio k 17 kD, Dio k 4, Dio k IFR), Dioscorea spp (Dio p TSP), Diplodus spp (Dip ho 1), Distichlis spp (Dis s 1, Dis s 7), Ditrema spp (Dit to 1), Dolichovespula spp (Doi a 1, Doi a 2, Doi a 5, Doi a 5.0101), Dolichos spp (Doi b Agglutinin), Dolichovespula spp (Doi m 1, Doi m 1.0101, Doi m 1.02, Doi m 2, Doi m 2.0101, Doi m 5, Doi m 5.0101, Doi m 5.02), Drosophila spp (Dro an 7, Dro an 7.0101, Dro er 7, Dro er 7.0101, Dro er 7.0102, Dro gr 7, Dro gr 7.0101, Dro gr 7.0102, Dro m 7, Dro m 7.0101, Dro m 7.0102, Dro m 7.0103, Dro m 7.0104, Dro m 7.0105, Dro m 7.0106, Dro m 7.0107, Dro m 7.0108, Dro m 7.0109, Dro m 7.0110, Dro m 7.0111, Dro m 7.0112, Dro m 7.0113, Dro m 9, Dro m MnSOD, Dro mo 7, Dro mo 7.0101, Dro pp 7, Dro pp 7.0101, Dro se 7, Dro se 7.0101, Dro si 7, Dro si 7.0101, Dro si 7.0102, Dro vi 7, Dro vi 7.0101, Dro wi 7, Dro wi 7.0101, Dro y 7, Dro y 7.0101, Dro y 7.0102, Dro y 7.0103), Echium spp (Ech p Cytochrome C), Elaeis spp (Ela g 2, Ela g Bd31 kD), Elops spp (Elo sa 1), Embellisia spp (Emb a 1, Emb i 1, Emb nz 1, Emb t 1), Engraulis spp (Eng e l), Enteroctopus spp (Ent d 1), Epinephelus spp (Epi bl 1, Epi co 1, Epi fl 1, Epi me 1, Epi mo 1), Epicoccum spp (Epi p 1, Epi p 1.0101, Epi p 12 kD, Epi p GST), Epinephelus spp (Epi po 1, Epi un 1), Equisetum spp (Equ a 17 kD), Equus spp (Equ as 4, Equ as DSA, Equ bu 4, Equ c 1, Equ c 1.0101, Equ c 2, Equ c 2.0101, Equ c 2.0102, Equ c 3, Equ c 3.0101, Equ c 4, Equ c 4.0101, Equ c 5, Equ c 5.0101, Equ c ALA, Equ c BLG, Equ c Casein, Equ c Casein beta, Equ c Casein kappa, Equ c PRVB, Equ he 4, Equ z ZSA), Erimacrus spp (En i 1, En i 1.0101, Eri i 1.0102), Eriocheir spp (Eri s 1, Eri s 1.0101, En s 2), Erwinia spp (Erw ch Asparaginase), Escherichia spp (Esc c Asparaginase, Esc c beta GAL), Esox spp (Eso 11), Euphausia spp (Eup p 1, Eup p 1.0101), Euphasia spp (Eup s 1, Eup s 1.0101), Euroglyphus spp (Eur m 1, Eur m 1.0101, Eur m 1.0102, Eur m 1.0103, Eur m 10, Eur m 14, Eur m 14.0101, Eur m 2, Eur m 2.0101, Eur m 2.0102, Eur m 3, Eur m 3.0101, Eur m 4, Eur m 4.0101), Evynnis spp (Evy j 1), Fagopyrum spp (Fag e 1, Fag e 1.0101, Fag e 10 kD, Fag e 19 kD, Fag e 2, Fag e 2.0101, Fag e TI), Fagus spp (Fag s 1, Fag s 1.0101, Fag s 2, Fag s 4), Fagopyrum spp (Fag t 1, Fag 1 10 kD, Fag t 2, Fag 12.0101), Felis spp (Fel d 1, Fel d 1.0101, Fel d 2, Fel d 2.0101, Fel d3, Fel d 3.0101, Fel d 4, Fel d 4.0101, Fel d 5, Fel d 5.0101, Fel d 6, Fel d 6.0101, Fel d 7, Fel d 7.0101, Fel d 8, Fel d 8.0101, Fel d IgG), Fenner openaeus spp (Fen c 1, Fen c 2, Fen me 1, Fen me 1.0101), Festuca spp (Fes e 1, Fes e 13, Fes e 4, Fes e 5, Fes e 7, Fes p 1, Fes p 13, Fes p 4, Fes p 4.0101, Fes p 5, Fes r 1, Fes r 5), Ficus spp (Fic c 17 kD, Fic c 4, Fic c Ficin), Foeniculum spp (Foe v 1, Foe v 2), Forsythia spp (For s i), Forcipomyia spp (Fort 1, Fort 1.0101, Fort 2, Fort 2.0101, Fort 7, Fort FPA, Fort Myosin, Fort TPI), Fragaria spp (Fra a 1, Fra a 1.0101, Fra a 3, Fra a 3.0101, Fra a 3.0102, Fra a 3.0201, Fra a 3.0202, Fra a 3.0203, Fra a 3.0204, Fra a 3.0301, Fra a 4, Fra a 4.0101, Fra c 1), Fraxinus spp (Fra e 1, Fra e 1.0101, Fra e 1.0102, Fra e 1.0201, Fra e 12, Fra e 2, Fra e 3, Fra e 9), Fragaria spp (Fra v 1), Fusarium spp (Fus c 1, Fus c 1.0101, Fus c 2, Fus c 2.0101, Fus c 3, Fus s 1, Fus s 45 kD, Fus sp Lipase), Gadus spp (Gad c 1, Gad c 1.0101, Gad c APDH, Gad m 1, Gad m 1.0101, Gad m 1.0102, Gad m 1.0201, Gad m 1.0202, Gad m 45 kD, Gad m Gelatin, Gad ma 1), Gallus spp (Gal d 1, Gal d 1.0101, Gal d 2, Gal d 2.0101, Gal d 3, Gal d 3.0101, Gal d 4, Gal d 4.0101, Gal d 5, Gal d 5.0101, Gal d 6, Gal d 6.0101, Gal d Apo I, Gal d Apo VI, Gal d GPI, Gal d HG, Gal d IgY, Gal d L-PGDS, Gal d Ovomucin, Gal d Phosvitin, Gal d PRVB, Gal la 4), Galleria spp (Gal m 18 kD, Gal m 24 kD), Gallus spp (Gal so 4), Gammarus spp (Gam s TM), Gelonium spp (Gel m RIP), Geothelphusa spp (Geo de 1), Glossina spp (Gio m 5, Gio m 5.0101, Gio m 7, Gio m 7.0101, Gio m 7.0102, Gio m 7.0103), Glycine spp (Gly a Bd30K, Gly ar Bd30K, Gly ca Bd30K, Gly cl Bd30K, Gly cu Bd30K, Gly cy Bd30K), Glycyphagus spp (Gly d 10, Gly d 10.0101, Gly d 13, Gly d 2, Gly d 2.0101, Gly d 2.0201, Gly d 2.03, Gly d 2 / Lep d 2 LI, Gly d 2 / Lep d 2 L2, Gly d 2 / Lep d 2 L3, Gly d 2 / Lep d 2 L4, Gly d 2 / Lep d 2 Rl, Gly d 2 / Lep d 2 R2, Gly d 2 / Lep d 2 R3, Gly d 2 / Lep d 2 R4, Gly d 2 / Lep d 2 R5, Gly d 20, Gly d 3, Gly d 5, Gly d 5.01, Gly d 5.02, Gly d 7, Gly d 8), Glycine spp (Gly f Bd30K, Gly I Bd30K, Gly m 1, Gly m 1.0101, Gly m 1.0102, Gly m 2, Gly m 2.0101, Gly m 2S Albumin, Gly m 3, Gly m 3.0101, Gly m 3.0102, Gly m 39 kD, Gly m 4, Gly m 4.0101, Gly m 5, Gly m 5.0101, Gly m 5.0201, Gly m 5.0301, Gly m 5.0302, Gly m 50 kD, Gly m 6, Gly m 6.0101, Gly m 6.0201, Gly m 6.0301, Gly m 6.0401, Gly m 6.0501, Gly m 68 kD, Gly m Agglutinin, Gly m Bd28K, Gly m Bd30K, Gly m Bd60K, Gly m CPI, Gly m EAP, Gly m TI, Gly mi Bd30K, Gly s Bd30K, Gly t Bd30K, Gly to Bd30K), Gossypium spp (Gos h Vicilin), Haemophilus spp (Hae in P6), Haemaphysalis spp (Hae 17, Hae 1 7.0101, Hae q 7, Hae q 7.0101), Haliotis spp (Hal a 1, Hal d 1, Hal di 1, Hal di PM, Hal m 1, Hal m 1.0101, Hal r 1, Hal r 49 kD, Hal ru 1), Harmonia spp (Har a 1, Har a 1.0101, Har a 2, Har a 2.0101), Harpegnathos spp (Har sa 7, Har sa 7.0101, Har sa 7.0102), Helianthus spp (Hel a 1, Hel a 1.0101, Hel a 2, Hel a 2.0101, Hel a 2S Albumin, Hel a 3, Hel a 3.0101, Hel a 4), Helix spp (Hel ap 1, Hel as 1, Hel as 1.0101), Heligmosomoides spp (Hel p 3, Hel p 3.0101), Helianthus spp (Hel to 1), Hemanthias spp (Hem le 1), Hemifusus spp (Hem t 1), Heterodera spp (Het g 3, Hetg 3.0101), Hevea spp (Hey b 1, Hey b 1.0101, Hey b 10, Hey b 10.0101, Hey b 10.0102, Hey b 10.0103, Hey b 11, Hey b 11.0101, Hey b 11.0102, Hey b 12, Hey b 12.0101, Hey b 13, Hey b 13.0101, Hey b 14, Hey b 14.0101, Hey b 2, Hey b 2.0101, Hey b 3, Hey b 3.0101, Hey b 4, Hey b 4.0101, Hey b 5, Hey b 5.0101, Hey b 6, Hey b 6.01, Hey b 6.02, Hey b 6.0202, Hey b 6.03, Hey b 7, Hey b 7.01, Hey b 7.02, Hey b 7.D2, Hey b 7.S2, Hey b 8, Hey b 8.0101, Hey b 8.0102, Hey b 8.0201, Hey b 8.0202, Hey b 8.0203, Hey b 8.0204, Hey b 9, Hey b 9.0101, Hey b Citrate binding Protein, Hey b GAPDH, Hey b HSP80, Hey b IFR, Hey b Proteasome subunit, Hey b Rotamase, Hey b SPI, Hey b Trx, Hey b UDPGP), Hexagrammos spp (Hex of 1), Hippoglossus spp (Hip h l), Hippoglossoides spp (Hip pl 1), Hippoglossus spp (Hip st 1), Hirudo spp (Hir me Hirudin), Holcus spp (Hol 1 1, Hol 1 1.0101, Hol 1 1.0102, Hol 1 2, Hol 1 4, Hol 1 5, Hol 1 5.0101, Hol 1 5.0201), Holocnemus spp (Hol pl 9, Hol pl Hemocyanin), Homarus spp (Hom a 1, Hom a 1.0101, Hom a 1.0102, Hom a 1.0103, Hom a 3, Hom a 3.0101, Hom a 4, Hom a 6, Hom a 6.0101, Hom g 1, Hom g 2), Homo spp (Hom s 1, Hom s 1.0101, Hom s 2, Hom s 2.0101, Hom s 3, Hom s 3.0101, Hom s 4, Hom s 4.0101, Hom s 5, Hom s 5.0101, Hom s AAT, Hom s ACTH, Hom s Adalimumab, Hom s ALA, Hom s alpha Actin, Hom s alpha-Galactosidase, Hom s APDH, Hom s Arylsulfatase B, Hom s Casein, Hom s CyP A, Hom s CyP B, Hom s CyP C, Hom s DSF70, Hom s DSG3, Hom s eIF6, Hom s Etanercept, Hom s Factor IX, Hom s Factor VII, Hom s Factor VIII, Hom s G-CSF, Hom s Glucocerebrosidase, Hom s Glucosidase, Hom s HLA-DR-alpha, Hom s HSA, Hom s Iduronidase, Hom s Idursulfase, Hom s IgA, Hom s Insulin, Hom s Lactoferrin, Hom s Laminin gamma_2, Hom s MnSOD, Hom s Oxytocin, Hom s P2, Hom s Phosvitin, Hom s Profilin, Hom s PSA, Hom s RP1, Hom s TCTP, Hom s TL, Hom s TP A, Hom s TPO, Hom s Transaldolase, Hom s Trx, Hom s Tubulin-alpha, Hom s / Mus m Basiliximab, Hom s / Mus m Cetuximab, Hom s / Mus m Cetuximab (Gal-Gal), Hom s / Mus m Infliximab, Hom s / Mus m Natalizumab, Hom s / Mus m Omalizumab, Hom s / Mus m Palivizumab, Hom s / Mus m Rituximab, Hom s / Mus m Tocilizumab, Hom s / Mus m Trastuzumab), Hoplostethus spp (Hop a 1), Hordeum spp (Hor v 1, Hor v 12, Hor v 12.0101, Hor v 13, Hor v 14, Hor v 15, Hor v 15.0101, Hor v 16, Hor v 16.0101, Hor v 17, Hor v 17.0101, Hor v 18 kD, Hor v 2, Hor v 21, Hor v 21.0101, Hor v 28, Hor v 33, Hor v 4, Hor v 5, Hor v 5.0101, Hor v BDAI, Hor v BTI), Humicola spp (Hum in Cellulase), Humulus spp (Hum j 1, Hum j 1.0101, Hum j 10 kD, Hum j 2), Huso spp (Hus h l), Hylocereus spp (Hyl un LTP), Hymenocephalus spp (Hym st 1), Hyperoglyphe spp (Hyp by 1), Hypophthalmichthys spp (Hyp mo 1), Hypophthalmichthy spp (Hyp no 1), Ictalurus spp (let fu 1, let p 1), Imperata spp (Imp c 4, Imp c 5, Imp c Vlllel), Ixodes spp (Ixo r 2, Ixo sc 7, Ixo sc 7.0101), Jasus spp (Jas la 1, Jas la 1.0101, Jas la 1.0102), Juglans spp (Jug ca 1, Jug ca 2, Jug ci 1, Jug ci 2, Jug n 1, Jug n 1.0101, Jug n 2, Jug n 2.0101, Jug r 1, Jug r 1.0101, Jug r 2, Jug r2.0101, Jug r 3, Jug r 3.0101, Jug r 4, Jug r 4.0101, Jug r 5), Juniperus spp (Jun a 1, Jun aI.0101, Jun a 1.0102, Jun a 2, Jun a 2.0101, Jun a 3, Jun a 3.0101, Jun c 1, Jun o 1, Jun o 4, Jun o 4.0101, Jun r 3, Jun r 3.1, Jun r 3.2, Jun v 1, Jun v 1.0101, Jun v 1.0102, Jun v 3, Jun v 3.0101, Jun v 3.0102, Jun v 4), Katsuwonus spp (Kat p l), Kyphosus spp (Kyp se 1), Lachnolaimus spp (Lac ma 1), Lachesis spp (Lac mu 1), Lactuca spp (Lac s 1, Lac s 1.0101), Lagocephalus spp (Lag la 1), Larus spp (Lar a 1, Lar a 2, Lar a 3), Larimichthys spp (Lar po 1), Lates spp (Lat c 1), Lateolabrax spp (Lat ja 1), Lathyrus spp (Lat oc Agglutinin), Leiostomus spp (Lei xa 1), Lens spp (Len c 1, Len c 1.0101, Len c 1.0102, Len c 1.0103, Len c 2, Len c 2.0101, Len c 3, Len c 3.0101, Len c Agglutinin), Leopardus spp (Leo p l), Lepidoglyphus spp (Lep d 10, Lep d 10.0101, Lep d 12, Lep d 13, Lep d 13.0101, Lep d 2, Lep d 2.0101, Lep d 2.0102, Lep d 2.0201, Lep d 2.0202, Lep d 3, Lep d 39 kD, Lep d 5, Lep d 5.0101, Lep d 5.0102, Lep d 5.0103, Lep d 7, Lep d 7.0101, Lep d 8, Lep d alpha Tubulin), Lepomis spp (Lep gi 1), Leptomelanosoma spp (Lep i 1), Lepomis spp (Lep ma 1), Lepisma spp (Lep s 1, Lep s 1.0101, Lep s 1.0102), Lepeophtheirus spp (Lep sa 1, Lep sa 1.0101, Lep sa 1.0102, Lep sa 1.0103), Leptailurus spp (Lep se 1), Lepidorhombus spp (Lep w 1, Lep w 1.0101), Lethocerus spp (Let in 7, Let in 7.0101, Let in 7.0102), Leuciscus spp (Leu ce 1), Lewia spp (Lew in 1), Ligustrum spp (Lig v 1, Lig v 1.0101, Lig v 1.0102, Lig v 2), Lilium spp (Lil 12, Lil I PG), Limanda spp (Lim fe 1), Limnonectes spp (Lim m 1), Limulus spp (Lim p 1, Lim p 1.0101, Lim p 2, Lim p LPA), Liposcelis spp (Lip b 1, Lip b 1.0101), Litchi spp (Lit c 1, Lit c 1.0101, Lit c IFR, Lit c TPI), Lithobates spp (Lit ca 1), Litopenaeus spp (Lit se 1, Lit v 1, Lit v 1.0101, Lit v 2, Lit v 2.0101, Lit v 3, Lit v 3.0101, Lit v 4, Lit v 4.0101), Filiaria spp (Loa lo 3, Loa lo 3.0101), Lobotes spp (Lob su 1), Locusta spp (Loc m 7, Loc m 7.0101), Loligo spp (Lol b 1, Lol e l), Lolium spp (Lol m 2, Lol m 5, Lol p 1, Lol p 1.0101, Lol p 1.0102, Lol p 1.0103, Lol p 10, Lol p 11, Lol pI I.0101, Lol p 12, Lol p 13, Lol p 2, Lol p 2.0101, Lol p 3, Lol p 3.0101, Lol p 4, Lol p 4.0101, Lol p 5, Lol p 5.0101, Lol p 5.0102, Lol p 7, Lol p CyP, Lol p FT, Lol p Legumin), Lonomia spp (Lon o 7, Lon o 7.0101), Lophodytes spp (Lop cu 1), Lophonetta spp (Lop sp 1), Lupinus spp (Lup a 1, Lup a alpha Conglutin, Lup a delta Conglutin, Lup a gamma Conglutin, Lup an 1, Lup an 1.0101, Lup an alpha Conglutin, Lup an delta Conglutin, Lup an gamma Conglutin, Lup 117 kD), Lutjanus spp (Lut a 1, Lut c 1, Lut cy 1, Lut gr 1, Lut gu 1, Lut jo 1), Lutraria spp (Lut p l), Lutjanus spp (Lut pu 1, Lut sy 1), Lycoper sicon spp (Lyc e 1, Lyc e 1.0101, Lyc e 1 IS Globulin, Lyc e 2, Lyc e 2.0101, Lyc e 2.0102, Lyc e 3, Lyc e 3.0101, Lyc e 4, Lyc e 4.0101, Lyc e ARP60S, Lyc e Chitinase, Lyc e Glucanase, Lyc e Peroxidase, Lyc e PG, Lyc e PME, Lyc e PR23, Lyc e Vicilin), Maconellicoccus spp (Mac h 7, Mac h 7.0101), Macruronus spp (Mac ma 1, Mac n 1), Madura spp (Mac po 17 kD), Macrobrachium spp (Mac ro 1, Mac ro 1.0101, Mac ro Hemocyanin), Macropus spp (Marr s Gelatin), Malus spp (Mai d 1, Mai d 1.0101, Mai d1.0102, Mai d 1.0103, Mai d 1.0104, Mai d 1.0105, Mai d 1.0106, Mai d 1.0107, Mai d 1.0108, Mai d 1.0109, Mai d 1.0201, Mai d 1.0202, Mai d 1.0203, Mai d 1.0204, Mai d 1.0205, Mai d 1.0206, Mai d 1.0207, Mai d 1.0208, Mai d 1.0301, Mai d 1.0302, Mai d 1.0303, Mai d 1.0304, Mai d 1.0401, Mai d 1.0402, Mai d 1.0403, Mai d 2, Mai d 2.0101, Mai d 3, Mai d 3.0101, Mai d 3.0102, Mai d 3.0201, Mai d 3.0202, Mai d 3.0203, Mai d 4, Mai d 4.0101, Mai d 4.0102, Mai d 4.0201, Mai d 4.0202, Mai d 4.0301, Mai d 4.0302), Malpighia spp (Mai g 4, Mai g Hevein), Malus spp (Mai p 1), Malassezia spp (Mala f 2, Mala f 2.0101, Mala f 3, Mala f 3.0101, Mala f 4, Mala f 4.0101, Mala g 10, Mala s 1, Mala s 1.0101, Mala s 10, Mala s 10.0101, Mala s 11, Mala s 11.0101, Mala s 12, Mala s 12.0101, Mala s 13, Mala s 13.0101, Mala s 5, Mala s 5.0101, Mala s 6, Mala s 6.0101, Mala s 7, Mala s 7.0101, Mala s 8, Mala s 8.0101, Mala s 9, Mala s 9.0101), Manihot spp (Man e 5, Man e 5.0101, Man e FPA, Man e GAPDH), Mangifera spp (Man i 1, Man i 14 kD, Man i 2, Man i 3, Man i 3.01, Man i 3.02, Man i Chitinase), Marsupenaeus spp (Mar j 1, Mar j 1.0101, Mar j 2, Mar j 4), Matricaria spp (Mat c 17 kD), Mecopoda spp (Mec e 7), Megalobrama spp (Meg am 2, Meg am CK), Megathura spp (Meg c Hemocyanin), Megalops spp (Meg sp 1), Melanogrammus spp (Mel a l), Meleagris spp (Mel g 1, Mel g 2, Mel g 3, Mel g PRVB, Mel g TSA), Melicertus spp (Mel 11), Menticirrhus spp (Men am 1), Mercurialis spp (Mer a 1, Mer a 1.0101), Merluccius spp (Mer ap 1, Mer au 1, Mer bi 1, Mer ca 1, Mer ga 1, Mer hu 1), Merlangius spp (Mer me 1), Merluccius spp (Mer mr 1, Mer pa 1, Mer po 1, Mer pr 1, Mer se 1), Meriones spp (Mer un 23 kD), Metarhizium spp (Met a 30), Metapenaeopsis spp (Met ba 1), Metapenaeus spp (Mete 1, Mete 1.0101, Met e 2), Metasequoia spp (Met gl 2), Metapenaeus spp (Met j 1, Met j 2), Metanephrops spp (Met ja 1), Metapenaeopsis spp (Met la 1), Metanephrops spp (Met t 2), Micromesistius spp (Mic po 1), Micropogonias spp (Mic un 1), Mimachlamys spp (Mim n 1), Momordica spp (Mom c RIP), Morus spp (Mor a 17 kD, Mor a 4), Mor one spp (Mor am 1), Morus spp (Mor n 3, Mor n 3.0101), Mor one spp (Mor sa 1, Mor sc 1), Mugil spp (Mug c l), Muraenolepis spp (Mur mi 1), Musa spp (Mus a 1, Mus a 1.0101, Mus a 2, Mus a 2.0101, Mus a 3, Mus a 3.0101, Mus a 4, Mus a 4.0101, Mus a 5, Mus a 5.0101, Mus a 5.0102), Mus spp (Mus m 1, Mus m 1.0101, Mus m 1.0102, Mus m 2, Mus m Gelatin, Mus m IgG, Mus m MSA, Mus m Muromonab, Mus m Phosvitin), Mustela spp (Mus p 17 kD), Musa spp (Mus xp 1, Mus xp 2, Mus xp 5), Mycteroperca spp (Myc bo 1, Myc mi 1, Myc ph 1), Myceliophthora spp (Myc sp Laccase), Myrmecia spp (Myr p 1, Myr p 1.0101, Myr p 2, Myr p 2.0101, Myr p 2.0102, Myr p 3, Myr p 3.0101), Mytilus spp (Myt e 1, Myt g 1, Myt g PM), Myzus spp (Myz p 7, Myz p 7.0101), Nemorhedus spp (Nae go Hya), Necator spp (Nec a Calreticulin), Nemipterus spp (Nem vi 1), Neosartorya spp (Neo fi 1, Neo fi 22), Neochen spp (Neo ju 1), Neoscona spp (Neo n 7, Neo n 7.0101), Nephelium spp (Nep I GAPDH), Nephrops spp (Nep n 1, Nep n DF9), Neptunea spp(Nep po 1, Nep po 1.0101), Nicotiana spp (Nic t 8, Nic t Osmotin, Nic t Villin), Nimbya spp (Nim c 1, Nim s i), Nippostrongylus spp (Nip b Agl), Nycticebus spp (Nyc c l), Octopus spp (Oct f 1, Oct 11, Oct v 1, Oct v 1.0101, Oct v PM), Ocyurus spp (Ocy ch 1), Olea spp (Ole e 1, Ole e 1.0101, Ole e 1.0102, Ole e 1.0103, Ole e 1.0104, Ole e 1.0105, Ole e 1.0106, Ole e 1.0107, Ole e 10, Ole e 10.0101, Ole e 11, Ole e 11.0101, Ole e 11.0102, Ole e 12, Ole e 13, Ole e 2, Ole e 2.0101, Ole e 3, Ole e 3.0101, Ole e 36 kD, Ole e 4, Ole e 4.0101, Ole e 5, Ole e 5.0101, Ole e 6, Ole e 6.0101, Ole e 7, Ole e 7.0101, Ole e 8, Ole e 8.0101, Ole e 9, Ole e 9.0101), Ommastrephes spp (Omm b 1, Omm b 1.0101), Oncorhynchus spp (One ke 1, One ke 18 kD, One ke alpha2I, One ke Vitellogenin, One m 1, One m 1.0101, One m 1.0201, One m alpha2I, One m Protamine, One m Vitellogenin, One ma 1, One ma FPA, One ma FSA, One ma TPI, One n 1), Onchocerca spp (One o 3, One o 3.0101), Oncorhynchus spp (One is 1), Onchocerca spp (One v 3, One v 3.0101), Oratosquilla spp (Ora o 1, Ora o 1.0101), Oreochromis spp (Ore a 1, Ore mo 1, Ore mo 2, Ore mo FPA, Ore mo SCAF7145, Ore ni 1, Ore ni 18 kD, Ore ni 45 kD), Ornithonyssus spp (Om sy 10, Om sy 10.0101, Orn sy 10.0102), Oryctolagus spp (Ory c 1, Ory c 1.0101, Ory c 2, Ory c Casein, Ory c Phosvitin, Ory c RSA), Oryza spp (Ory s 1, Ory s 1.0101, Ory s 11, Ory s 12, Ory s 12.0101, Ory s 13, Ory s 14, Ory s 17 kD, Ory s 19 kD, Ory s 2, Ory s 23, Ory s 3, Ory s 7, Ory s akTI, Ory s GLP52, Ory s GLP63, Ory s Glyoxalase I, Ory s NRA), Ostrya spp (Ost c 1, Ost c 1.0101), Ovis spp (Ovi a ALA, Ovi a BLG, Ovi a Casein, Ovi a Casein alphaS 1, Ovi a Casein alphaS2, Ovi a Casein beta, Ovi a Casein kappa, Ovi a Phosvitin, Ovi a SSA), Pachycondyla spp (Pae c 3), Pagrus spp (Pag m 1, Pag pa 1), Pampus spp (Pam ar 1, Pam c l), Pandalus spp (Pan b 1, Pan b 1.0101), Pangasius spp (Pan bo 1), Pandalus spp (Pan e 1, Pan e 1.0101, Pan e 4), Panulirus spp (Pan h 1, Pan hy 1), Pangasius spp (Pan hy 18 kD, Pan hy 45 kD), Panulirus spp (Pan j 1), Panthera spp (Pan 11, Pan o 1, Pan p l), Panulirus spp (Pan s 1, Pan s 1.0101), Panthera spp (Pan t 1), Pan spp (Pan tr TCTP), Papaver spp (Pap s 17 kD, Pap s 2, Pap s 34 kD), Papilio spp (Pap xu 7, Pap xu 7.0101, Pap xu 7.0102), Paralichthys spp (Par a l), Parasilurus spp (Par as 1, Par c l), Paralithodes spp (Par c 1.0101, Par c 1.0102, Par f 1), Parthenium spp (Par h 1), Parietaria spp (Par j 1, Parj 1.0101, Par j 1.0102, Par j 1.0103, Par j 1.0201, Par j 2, Par j 2.0101, Par j 2.0102, Par j 3, Parj 3.0101, Parj 3.0102, Parj 4, Parj 4.0101, Parj J1-J2), Paralichthys spp (Par le 1), Parietaria spp (Par m 1, Par o 1, Par o 1.0101), Paralichthys spp (Par of 1, Par of alpha2I), Parahucho spp (Par pe Vitellogenin), Passiflora spp (Pas e Chitinase, Pas e Hevein), Paspalum spp (Pas n 1, Pas n 1.0101, Pas n 13), Patinopecten spp (Pat y 1), Pediculus spp (Ped h 7, Ped h 7.0101), Penaeus spp (Pen a 1, Pen a 1.0101, Pen a 1.0102, Pen a 1.0102 (103-117), Pen a 1.0102 (109-123), Pen a 1.0102 (1-15), Pen a 1.0102 (115-129), Pen a 1.0102 (121-135), Pen a 1.0102 (127-141), Pen a 1.0102 (13-27), Pen a 1.0102 (133-147), Pen a 1.0102 (139-153), Pena 1.0102 (145-159)), Farfantepenaeus spp (Pen a 1.0102 (151-165)), Penaeus spp (Pen a 1.0102 (157-171), Pen a 1.0102 (163-177), Pen a 1.0102 (169-183), Pen a 1.0102 (175-189), Pen a 1.0102 (181-195), Pen a 1.0102 (187-201), Pen a 1.0102 (193-207), Pen a 1.0102 (19-33), Pen a 1.0102 (199-213), Pen a 1.0102 (205-219), Pen a 1.0102 (211-225), Pen a 1.0102 (217-231), Pen a 1.0102 (223-237), Pen a 1.0102 (229-243)), Farfantepenaeus spp (Pen a 1.0102 (235- 249)), Penaeus spp (Pen a 1.0102 (241-255), Pen a 1.0102 (247-261), Pen a 1.0102 (253-267), Pen a 1.0102 (25-39), Pen a 1.0102 (259-273), Pen a 1.0102 (265-279), Pen a 1.0102 (270- 284), ew a 1.0102 (31-45), ew a 1.0102 (37-51), Pen a 1.0102 (43-57), Pen a 1.0102 (49-63)), Farfantepenaeus spp (Pen a 1.0102 (55-69)), Penaeus spp (Pen a 1.0102 (61-75), Pew a 1.0102 (67-81), Pew a 1.0102 (7-21), Pew a 1.0102 (73-87), Pew a 1.0102 (79-93), Pew a 1.0102 (85- 99), Pew a 1.0102 (91-105), Pew a 1.0102 (97-111), Pew a 1.0103), Penicillium spp (Pen b 13, Pen b 13.0101, Pen b 26, Pen b 26.0101, Pen c 1, Pen c 13, Pen c 13.0101, Pen c 18, Pen c 19, Pen c 19.0101, Pen c 2, Pen c 22, Pen c 22.0101, Pen c 24, Pen c 24.0101, Pen c 3, Pen c 3.0101, Pen c 30, Pen c 30.0101, Pen c 32, Pen c 32.0101, Pen c MnSOD, Pen ch 13, Pen ch 13.0101, Pen ch 18, Pen ch 18.0101, Pen ch 20, Pen ch 20.0101, Pen ch 31, Pen ch 31.0101, Pen ch 33, Pen ch 33.0101, Pen ch 35, Pen ch 35.0101, Pen ch MnSOD), Penaeus spp (Pen i 1, Pen i 1.0101, Pen m 1, Pen m 1.0101, Pen m 1.0102, Pen m 2, Pen m 2.0101, Pen m 3, Pen m 3.0101, Pen m 4, Pen m 4.0101, Pen m 6, Pen m 6.0101), Penicillium spp (Pen o 18, Pen o 18.0101), Penaeus spp (Pena o 1, Pena o 1.0101), Periplaneta spp (Per a 1, Per a 1.0101, Per a 1.0102, Per a 1.0103, Per a 1.0104, Per a 1.0105, Per a 1.0201, Per a 10, Per a 10.0101, Per a 2, Per a 3, Per a 3.0101, Per a 3.0201, Per a 3.0202, Per a 3.0203, Per a 4, Per a 5, Per a 6, Per a 6.0101, Per a 7, Per a 7.0101, Per a 7.0102, Per a 7.0103, Per a 9, Per a 9.0101, Per a Cathepsin, Per a FABP, Per a Trypsin, Per f 1, Per f 7, Per f 7.0101), Perna spp (Per v 1), Persea spp (Pers a 1, Pers a 1.0101, Pers a 4), Petroselinum spp (Pet c 1, Pet c 2, Pet c 3), Phalaris spp (Pha a 1, Pha a 1.0101, Pha a 5, Pha a 5.0101, Pha a 5.02, Pha a 5.03, Pha a 5.04), Phaseolus spp (Pha v 3, Pha v 3.0101, Pha v 3.0201, Pha v aAI, Pha v aAI.0101, Pha v Chitinase, Pha v PHA, Pha v Phaseolin), Phleum spp (Phi p 1, Phi p 1.0101, Phi p 1.0102, Phi p 11, Phi p 11.0101, Phi p 12, Phi p 12.0101, Phi p 12.0102, Phi p 12.0103, Phi p 13, Phi p 13.0101, Phi p 2, Phi p 2.0101, Phi p 3, Phi p 3.0101, Phi p 3.0102, Phi p 4, Phi p 4.0101, Phi p 4.0102, Phi p 4.0201, Phi p 4.0202, Phi p 4.0203, Phi p 4.0204, Phi p 5, Phi p 5.0101, Phi p 5.0102, Phi p 5.0103, Phi p 5.0104, Phi p 5.0105, Phi p 5.0106, Phi p 5.0107, Phi p 5.0108, Phi p 5.0109, Phi p 5.0201, Phi p 5.0202, Phi p 5.0203, Phi p 5.0204, Phi p 5.0205, Phi p 5.0206, Phi p 5.0207, Phi p 6, Phi p 6.0101, Phi p 6.0102, Phi p 7, Phi p 7.0101, Phi p P1-P2-P5-P6, Phi p P2-P6, Phi p P5-P1, Phi p P6-P2), Phoenix spp (Pho d 2, Pho d 2.0101, Pho d 40 kD, Pho d 90 kD), Phodopus spp (Pho s 21 kD), Phoma spp (Pho t 1), Phragmites spp (Phr a 1, Phr a 12, Phr a 13, Phr a 4, Phr a 5), Phytolaccaspp (Phy a RIP), Pimpinella spp (Pim a 1, Pim a 2), Pinna spp (Pin a l), Piper spp (Pip n 14 kD, Pip n 28 kD), Pisum spp (Pis s 1, Pis s 1.0101, Pis s 1.0102, Pis s 2, Pis s 2.0101, Pis s 5, Pis s Agglutinin, Pis s Albumin), Pistacia spp (Pis v 1, Pis v 1.0101, Pis v 2, Pis v 2.0101, Pis v 2.0201, Pis v 3, Pis v 3.0101, Pis v 4, Pis v 4.0101, Pis v 5, Pis v 5.0101), Platanus spp (Pla a 1, Pla a 1.0101, Pla a 2, Pla a 2.0101, Pla a 3, Pla a 3.0101, Pla a 8), Platichthys spp (Pla f 1), Plantago spp (Pla 11, Pla 11.0101, Pla I 1.0102, Pla 11.0103, Pla I Cytochrome C), Platanus spp (Pla oc 1, Pla or 1, Pla or 1.0101, Pla or 2, Pla or 2.0101, Pla or 3, Pla or 3.0101, Pla or 4, Pla or CyP, Pla r 1), Plectropomus spp (Pie ar 1), Pleospora spp (Pie h l), Plectropomus spp (Pie le 1), Plodia spp (Pio i 1, Pio i 1.0101, Pio i 2, Pio i 2.0101), Poa spp (Poa p 1, Poa p 1.0101, Poa p 10, Poa p 12, Poa p 13, Poa p 2, Poa p 4, Poa p 5, Poa p 5.0101, Poa p 6, Poa p 7), Polistes spp (Pol a 1, Pol a 1.0101, Pol a 2, Pol a 2.0101, Pol a 5, Pol a 5.0101, Pol d 1, Pol d 1.0101, Pol d 1.0102, Pol d 1.0103, Pol d 1.0104, Pol d 4, Pol d 4.0101, Pol d 5, Pol d 5.0101, Pol e 1, Pol e 1.0101, Pol e 2, Pol e 4, Pol e 4.0101, Pol e 5, Pol e 5.0101, Pol f 5, Pol f 5.0101, Pol g 1, Pol g 1.0101, Pol g 2, Pol g 4, Pol g 5, Pol g 5.0101, Pol he MLT, Pol m 5, Pol m 5.0101), Polypedilum spp (Pol n 1), Pollicipes spp (Pol po 1), Pollachius spp (Pol vi 1), Polybia spp (Poly p 1, Poly p 1.0101, Poly p 2, Poly p 5, Poly s 5, Poly s 5.0101), Pomatomus spp (Porn sa 1), Pongo spp (Pon ab HSA), Pontastacus spp (Pon I 4, Pon I 4.0101, Pon I 7, Pon I 7.0101), Portunus spp (Por s 1, Por s 1.0101, Por s 1.0102, Por tr 1, Por tr 1.0101), Protortonia spp (Pro ca 38 kD), Procumbarus spp (Pro cl 1, Pro cl 1.0101, Pro cl 21 kD), Prosopis spp (Pro j 20 kD), Prunus spp (Pru ar 1, Pru ar 1.0101, Pru ar 3, Pru ar 3.0101, Pru av 1, Pru av 1.0101, Pru av 1.0201, Pru av 1.0202, Pru av 1.0203, Pru av 2, Pru av 2.0101, Pru av 3, Pru av 3.0101, Pru av 4, Pru av 4.0101, Pru c 1, Pru d 1, Pru d 2, Pru d 3, Pru d 3.0101, Pru d 4, Pru du 1, Pru du 2, Pru du 2S Albumin, Pru du 3, Pru du 3.0101, Pru du 4, Pru du 4.0101, Pru du 4.0102, Pru du 5, Pru du 5.0101, Pru du 6, Pru du 6.0101, Pru du 6.0201, Pru du Conglutin, Pru p 1, Pru p 1.0101, Pru p 2, Pru p 2.0101, Pru p 2.0201, Pru p 2.0301, Pru p 3, Pru p 3.0101, Pru p 3.0102, Pru p 4, Pru p 4.0101, Pru p 4.0201, Pru sa 3), Psilocybe spp (Psi c 1, Psi c 1.0101, Psi c 2, Psi c 2.0101), Psoroptes spp (Pso o 1, Pso o 10, Pso o 10.0101, Pso o i l, Pso o 13, Pso o 14, Pso o 2, Pso o 21, Pso o 3, Pso o 5, Pso o 7), Puma spp (Pum c 1), Punica spp (Pun g 3), Pyrus spp (Pyr c 1, Pyr c 1.0101, Pyr c 3, Pyr c 3.0101, Pyr c 4, Pyr c 4.0101, Pyr c 5, Pyr c 5.0101, Pyr py 2), Quercus spp (Que a 1, Que a 1.0101, Que a 1.0201, Que a 1.0301, Que a 1.0401, Que a 2, Que a 4), Rachycentron spp (Rac ca 1), Rana spp (Ran e 1, Ran e 1.0101, Ran e 2, Ran e 2.0101), Ranina spp (Ran ra 1), Rangifer spp (Ran t BLG), Rattus spp (Rat n 1, Rat n 1.0101, Rat n Casein, Rat n Gelatin, Rat n IgG, Rat n Phosvitin, Rat n RSA, Rat n Transferrin), Rhizomucor spp (Rhi m AP), Rhizopus spp (Rhi nv Lipase, Rhi o Lipase), Rhomboplites spp (Rho au 1), Rhodotorula spp (Rho m 1, Rho m 1.0101, Rho m 2, Rho m 2.0101), Ricinus spp (Ric c 1, Ric c 1.0101, Ric c 2,Ric c 3, Ric c 8, Ric c RIP), Rivulus spp (Riv ma 1), Robinia spp (Rob p 2, Rob p 4, Rob p Glucanase), Rosa spp (Ros r 3), Roystonea spp (Roy e 2), Rubus spp (Rub i 1, Rub i 1.0101, Rub i 3, Rub i 3.0101, Rub i Chitinase, Rub i CyP), Saccharomyces spp (Sac c Carboxypeptidase Y, Sac c CyP, Sac c Enolase, Sac c Glucosidase, Sac c Invertase, Sac c MnSOD, Sac c P2, Sac c Profilin), Salvelinus spp (Sal f 1), Salsola spp (Sal k 1, Sal k 1.0101, Sal k 1.0201, Sal k 1.0301, Sal k 1.0302, Sal k 2, Sal k 2.0101, Sal k 3, Sal k 3.0101, Sal k 4, Sal k 4.0101, Sal k 4.0201, Sal k 5, Sal k 5.0101), Salvelinus spp (Sal le Vitellogenin), Salmo spp (Sal s 1, Sal s 1.0101, Sal s 1.0201, Sal s 2, Sal s 2.0101, Sal s Gelatin), Sambucus spp (Sam n 1), Sander spp (San lu 1), Saponaria spp (Sap o RIP), Sardinops spp (Sar m l), Sarkidiornis spp (Sar ml 1), Sardina spp (Sar p l), Sarcoptes spp (Sar s 1, Sar s 14, Sar s 3, Sar s GST, Sar s PM), Sardinops spp (Sar sa 1, Sar sa 1.0101), Schistosoma spp (Sch j GST, Sch j PM, Sch j Sj22, Sch j Sj67, Sch ma Sm20, Sch ma Sm21, Sch ma Sm22, Sch ma Sm31), Sciaenops spp (Sci oc 1), Scomber spp (Sco a 1), Scombermorus spp (Sco ca 1), Scomberomorus spp (Sco g 1), Scomber spp (Sco j 1, Sco ma 1, Sco s 1), Scolopendra spp (Sco y 7, Sco y 7.0101), Scylla spp (Scy o 1, Scy o 1.0101, Scy o 2, Scy pa 1, Scy pa 2, Scy s 1, Scy s 1.0101, Scy s 2), Sebastes spp (Seb fa 1, Seb in 1, Seb m 1, Seb m 1.0101, Seb m 1.0201), Secale spp (Sec c 1, Sec c 12, Sec c 13, Sec c 2, Sec c 20, Sec c 20.0101, Sec c 20.0201, Sec c 28, Sec c 3, Sec c 4, Sec c 4.0101, Sec c 4.0201, Sec c 5, Sec c 5.0101, Sec c akTI, Sec c akTI.0101), Senecio spp (Sen j MDH, Sen j PL), Sepia spp (Sep e 1, Sep e 1.0101), Sepioteuthis spp (Sep 11, Sep I 1.0101), Sepia spp (Sep m 1), Seriola spp (Ser d 1, Ser la 1), Sergestes spp (Ser lu 1), Seriola spp (Ser q 1, Ser ri 1), Sesamum spp (Ses i 1, Ses i 1.0101, Ses i 2, Ses i 2.0101, Ses i 3, Ses i 3.0101, Ses i 4, Ses i 4.0101, Ses i 5, Ses i 5.0101, Ses i 6, Ses i 6.0101, Ses i 7, Ses i 7.0101, Ses i 8), Shigella spp (Shi bo GST, Shi dy GST), Simulia spp (Sim vi 1, Sim vi 2, Sim vi 3, Sim vi 4, Sim vi 70 kD), Sinapis spp (Sin a 1, Sin a 1.0101, Sin a 1.0104, Sin a 1.0105, Sin a 1.0106, Sin a 1.0107, Sin a 1.0108, Sin a 2, Sin a 2.0101, Sin a 3, Sin a 3.0101, Sin a 4, Sin a 4.0101), Sinonovacula spp (Sin c 1, Sin c 1.0101), Solenopsis spp (Sol g 2, Sol g 2.0101, Sol g 3, Sol g 3.0101, Sol g 4, Sol g 4.0101, Sol g 4.0201, Sol i 1, Sol i 1.0101, Sol i 2, Sol i 2.0101, Sol i 3, Sol i 3.0101, Sol i 4, Sol i 4.0101), Solenocera spp (Sol me 1), Solenopsis spp (Sol r 1, Sol r 2, Sol r 2.0101, Sol r 3, Sol r 3.0101, Sol s 2, Sol s 2.0101, Sol s 3, Sol s 3.0101, Sol s 4), Solea spp (Sol so 1, Sol so TPI), Solanum spp (Sola t 1, Sola t 1.0101, Sola t 2, Sola t 2.0101, Sola t 3, Sola t 3.0101, Sola t 3.0102, Sola t 4, Sola t 4.0101, Sola t 8, Sola t Glucanase), Sorghum spp (Sor b 1, Sor h 1, Sor h 1.0101, Sor h 12, Sor h 7), Sparus spp (Spa a l), Sphyrna spp (Sph ti 1), Spirulina spp (Spi mx beta Phy cocyanin), Spinacia spp (Spi o 2, Spi o RuBisCO), Squilla spp (Squ ac 1, Squ ac 1.0101, Squ o 1, Squ o 1.0101), Staphylococcus spp (Sta a FBP, Sta a SEA, Sta a SEB, Sta a SEC, Sta a SED, Sta a SEE, Sta a TSST), Stachybotrys spp (Sta c 3, Sta c 3.0101, Sta c Cellulase, Sta c Hemolysin, Stac SchS34, Sta c Stachyrase A), Stemphylium spp (Ste b 1, Ste c 1, Ste v 1), Stolephorus spp (Sto i 1), Struthio spp (Str c 1, Str c 2, Str c 3), Streptococcus spp (Str dy Streptokinase), Streptomyces spp (Str g Pronase), Streptococcus spp (Str pn PspC), Strongylocentrotus spp (Str pu 18 kD, Str pu Vitellogenin), Streptococcus spp (Str py SPEA, Str py SPEC, Str py Streptokinase), Strongyloides spp (Str st 45 kD), Streptomyces spp (Str v PAT), Styela spp (Sty p 1), Suidasia spp (Sui m 1, Sui m 13, Sui m 2, Sui m 3, Sui m 5, Sui m 5.01, Sui m 5.02, Sui m 5.03, Sui m 6, Sui m 7, Sui m 8, Sui m 9), Sus spp (Sus s ACTH, Sus s ALA, Sus s Amylase, Sus s BLG, Sus s Casein, Sus s Casein alphaS 1, Sus s Casein alphaS2, Sus s Casein beta, Sus s Casein kappa, Sus s Gelatin, Sus s HG, Sus s Insulin, Sus s Lipase, Sus s Pepsin, Sus s Phosvitin, Sus s PRVB, Sus s PSA, Sus s TCTP), Syntelopodeuma spp (Syn y 7, Syn y 7.0101), Syringa spp (Syr v 1, Syr v 1.0101, Syr v 1.0102, Syr v 1.0103, Syr v 2, Syr v 3, Syr v 3.0101), Tabanus spp (Tab y 1, Tab y 1.0101, Tab y 2, Tab y 2.0101, Tab y 5, Tab y 5.0101), Tadorna spp (Tad ra 1), Talaromyces spp (Tai st 22, Tai st 3, Tai st 8), Taraxacum spp (Tar o 18 kD), Taxodium spp (Tax d 2), Tegenaria spp (Teg d Hemocyanin), Teladorsagia spp (Tel ci 3), Thaumetopoea spp (Tha p 1, Tha p 1.0101, Tha p 2, Tha p 2.0101), Theragra spp (The c l), Thermomyces spp (The I Lipase, The sp Lipase, The sp Xylanase), Thunnus spp (Thu a 1, Thu a 1.0101, Thu a Collagen, Thu al 1, Thu at 1, Thu o 1, Thu o Collagen), Thuja spp (Thu oc 3, Thu p l), Thunnus spp (Thu t 1, Thu to 1), Thyr sites spp (Thy at 1), Thyrophygus spp (Thy y 7, Thy y 7.0101), Todarodes spp (Tod p 1, Tod p 1.0101, Tod p 1.0102), Toxoptera spp (Tox c 7, Tox c 7.0101), Toxocara spp (Tox ca TES120, Tox ca TES26, Tox ca TES30), Toxoplasma spp (Tox g HSP70), Trachypenaeus spp (Tra c l), Trachinotus spp (Tra ca 1), Trachurus spp (Tra j 1, Tra j Gelatin, Tra tr Gelatin), Triticum spp (Tri a 1, Tri a 10 kD, Tri a 12, Tri a 12.0101, Tri a 12.0102, Tri a 12.0103, Tri a 12.0104, Tri a 13, Tri a 14, Tri a 14.0101, Tri a 14.0201, Tri a 15, Tri a 15.0101, Tri a 18, Tri a 18.0101, Tri a 19, Tri a 19.0101, Tri a 2, Tri a 21, Tri a 21.0101, Tri a 23kd, Tri a 25, Tri a 25.0101, Tri a 26, Tri a 26.0101, Tri a 27, Tri a 27.0101, Tri a 28, Tri a 28.0101, Tri a 29, Tri a 29.0101, Tri a 29.0201, Tri a 3, Tri a 30, Tri a 30.0101, Tri a 31, Tri a 31.0101, Tri a 32, Tri a 32.0101, Tri a 33, Tri a 33.0101, Tri a 34, Tri a 34.0101, Tri a 35, Tri a 35.0101, Tri a 36, Tri a 36.0101, Tri a 37, Tri a 37.0101, Tri a 4, Tri a 4.0101, Tri a 4.0201, Tri a 5, Tri a 7, Tri a aA SI, Tri a alpha Gliadin, Tri a bA, Tri a Bd36K, Tri a beta Gliadin, Tri a Chitinase, Tri a CM16, Tri a DH, Tri a Endochitinase, Tri a gamma Gliadin, Tri a Germin, Tri a Gliadin, Tri a GST, Tri a LMW Glu, Tri a LMW-GS Bl 6, Tri a LMW-GS P42, Tri a LMW-GS P73, Tri a LTP2, Tri a omega2_Gliadin, Tri a Peroxidase, Tri a Peroxidase 1, Tri a SPI, Tri a TLP, Tri a Tritin, Tri a XI), Tritirachium spp (Tri al Proteinase K), Tribolium spp (Tri ca 17, Tri ca 17.0101, Tri ca 7, Tri ca 7.0101), Trichostrongylus spp (Tri co 3, Tri co 3.0101), Trichophyton spp (Tri eq 4), Trigonella spp (Tri fg 1, Tri fg 2, Tri fg 3, Tri fg 4), Trichosanthesspp (Tri k RIP), Trichiurus spp (Tri le 1), Triticum spp (Tri m Peroxidase), Trichophyton spp (Tri me 2, Tri me 4), Trisetum spp (Tri p 1, Tri p 5), Trichinella spp (Tri ps 3, Tri ps 3.0101), Trichophyton spp (Tri r 2, Tri r 2.0101, Tri r 4, Tri r 4.0101), Trichoderma spp (Tri rs Cellulase), Triticum spp (Tri s 14), Trichophyton spp (Tri sc 2, Tri sc 4, Tri so 2), Trichinella spp (Tri sp 3, Tri sp 3.0101, Tri sp 3.0102, Tri sp 3.0103, Tri sp 3.0104, Tri sp 3.0105, Tri sp 3.0106), Trichophyton spp (Tri t 1, Tri t 1.0101, Tri t 4, Tri t 4.0101), Triticum spp (Tri td 14, Tri td akTI), Trichoderma spp (Tri v Cellulase), Trichophyton spp (Tri ye 4), Triatoma spp (Tria p 1, Tria p 1.0101), Triplochiton spp (Trip s 1), Turbo spp (Tur c 1, Tur c PM), Tyrophagus spp (Tyr p 1, Tyr p 10, Tyr p 10.0101, Tyr p 10.0102, Tyr p 13, Tyr p 13.0101, Tyr p 2, Tyr p 2.0101, Tyr p 24, Tyr p 24.0101, Tyr p 3, Tyr p 3.0101, Tyr p 4, Tyr p 5, Tyr p 5.01, Tyr p 5.02, Tyr p 5.03, Tyr p 7, Tyr p alpha Tubulin), Ulocladium spp (Ulo a 1, Ulo at 1, Ulo b 1, Ulo c 1, Ulo co 1, Ulo cu 1, Ulo mu 1, Ulo ob 1, Ulo se 1, Ulo su 1, Ulo to 1), Uncia spp (Unc u 1), Urophycis spp (Uro to 1), Vaccinium spp (Vac m 3), Varroa spp (Var j 13 kD), Venerupis spp (Ven ph 1, Ven ph 1.0101), Vespula spp (Ves f 1, Ves f 2, Ves f 5, Ves f 5.0101, Ves g 1, Ves g 2, Ves g 5, Ves g 5.0101, Ves m 1, Ves m 1.0101, Ves m 2, Ves m 2.0101, Ves m 5, Ves m 5.0101, Ves m MLT, Ves p 1, Ves p 2, Ves p 5, Ves p 5.0101, Ves s 1, Ves s 1.0101, Ves s 2, Ves s 5, Ves s 5.0101, Ves v 1, Ves v 1.0101, Ves v 2, Ves v 2.0101, Ves v 2.0201, Ves v 3, Ves v 3.0101, Ves v 5, Ves v 5.0101, Ves v 5-Pol a 5, Ves vi 5, Ves vi 5.0101), Vespa spp (Vesp c 1, Vesp c 1.0101, Vesp c 2, Vesp c 5, Vesp c 5.0101, Vesp c 5.0102, Vesp m 1, Vesp m 1.0101, Vesp m 5, Vesp m 5.0101, Vesp ma 1, Vesp ma 2, Vesp ma 5, Vesp ma MLT, Vesp v MLT), Vigna spp (Vig r 1, Vig r 1.0101, Vig r 17 kD, Vig r 5, Vig r 8S Globulin, Vig r Albumin, Vig r beta-Conglycinin), Vitis spp (Vit v 1, Vit v 1.0101, Vit v 4, Vit v 5, Vit v Glucanase, Vit v TLP), Xiphias spp (Xip g 1, Xip g 1.0101, Xip g 25 kD), Zea spp (Zea m 1, Zea m 1.0101, Zea m i l, Zea m 12, Zea m 12.0101, Zea m 12.0102, Zea m 12.0103, Zea m 12.0104, Zea m 12.0105, Zea m 13, Zea m 14, Zea m 14.0101, Zea m 14.0102, Zea m 2, Zea m 20S, Zea m 22, Zea m 25, Zea m 25.0101, Zea m 27 kD Zein, Zea m 3, Zea m 4, Zea m 5, Zea m 50 kD Zein, Zea m 7, Zea m Chitinase, Zea m Gl, Zea m G2, Zea m PAO, Zea m Zml3), Zeus spp (Zeu fa 1), Ziziphus spp (Ziz m 1, Ziz m 1.0101), Zoarces spp (Zoa a ISP III), and Zygophyllum spp (Zyg f 2).Heterologous Antigens

[0149] The compositions herein described can comprise a plurality of presenting peptides derived from heterologous antigens (e.g, a plurality of disparate presenting peptide). In some embodiments, “heterologous antigens” are antigens that are of different origins, such as derived from pathogens of different taxonomic groups such as different strains, species, subgenera, genera, subfamilies or families and / or from antigenically divergent pathogens (e.g., variants thereof). Classification of viruses into various taxonomic groups is well understood bythose skilled in the art. Each of the disparate presenting peptide of the plurality of disparate presenting peptide can differ with respect to each other.

[0150] At least two of the APCs of the plurality of APCs can be different from each other with respect to the presenting peptide, and wherein the population of APVs thereby display a plurality of disparate presenting peptide. The population of APVs can comprise one or more homotypic APVs, wherein the plurality of APCs of a homotypic APV can be the same as each other with respect to the presenting peptide, and wherein a homotypic APV thereby does not display a plurality of disparate presenting peptide. The population of APVs can comprise one or more heterotypic APVs, wherein at least two of the APCs of a heterotypic APV can be different from each other with respect to the presenting peptide, and wherein a heterotypic APV thereby displays a plurality of disparate presenting peptide. The population of APVs can comprise a mixture of two or more homotypic APVs that differ from each other with respect to the presenting peptide of the plurality of APCs present in said two or more homotypic APVs, and wherein the population of APVs thereby displays a plurality of disparate presenting peptide. The population of APVs can comprise a mixture of two or more heterotypic APVs that differ from each other with respect to the presenting peptide of the plurality of APCs of said two or more heterotypic APVs. The population of APVs can comprise a mixture of heterotypic APVs and homotypic APVs. Heterotypic APVs can be capable of eliciting heterologous antibody responses against an additional antigen, and wherein said heterotypic APVs do not display presenting peptide derived from said additional antigen.

[0151] In some embodiments, the plurality of disparate presenting peptide comprises: between about 2 and about 500 (e.g., 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 30, 35, 40, 45, 50, 60, 70, 80, 90, 100, 110, 120, 128, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, 260, 270, 280, 290, 300, 310, 320, 330, 340, 350, 360, 370, 380, 390, 400, 410, 420, 430, 440, 450, 460, 470, 480, 490, 500, or a number or a range between any two of these values) presenting peptides that differ from each other; presenting peptide of a same protein type; and / or presenting peptide of different protein types.

[0152] The plurality of presenting peptide can be of a same protein type or corresponding proteins. Presenting peptide of a same protein type may or may not have identical amino acid sequences, but generally share some sequence homology. For example, the coronavirus S proteins of different coronaviruses are of a same protein type or corresponding proteins. As another example, envelope proteins from different coronaviruses are considered the same protein type or corresponding proteins. In some embodiments, proteins of different coronavirus taxonomic groups having the same function are considered the same protein type or corresponding proteins.

[0153] Alternatively, in some embodiments the plurality of presenting peptide can derive from antigens of different protein types. Antigens of different protein types typically have different functions. For example, the plurality of presenting peptide can derive from coronavirus S proteins or portions thereof as well as other coronavirus proteins such as a coronavirus N protein or a portion thereof, a coronavirus HE protein or a portion thereof, a coronavirus papainlike protease or a portion thereof, a coronavirus 3CL protease or a portion thereof, and / or a coronavirus M protein or a portion thereof.

[0154] The number of the first presenting peptides (e.g., derived from the first antigen molecules) and the number of the second presenting peptides (e.g., derived from the second antigen molecules) can be in a ratio from 1:100 to 100:1 (e.g., 1:1, 1:1.1, 1:1.2, 1:1.3, 1:1.4, 1:1.5, 1:1.6, 1:1.7, 1:1.8, 1:1.9, 1:2, 1:2.5, 1:3, 1:4, 1:5, 1:6, 1:7, 1:8, 1:9, 1:10, 1:11, 1:12, 1:13, 1:14, 1:15, 1:16, 1:17, 1:18, 1:19, 1:20, 1:21, 1:22, 1:23, 1:24, 1:25, 1:26, 1:27, 1:28, 1:29,1:30, 1:31, 1:32, 1:33, 1:34, 1:35, 1:36, 1:37, 1:38, 1:39, 1:40, 1:41, 1:42, 1:43, 1:44, 1:45, 1:46,1:47, 1:48, 1:49, 1:50, 1:51, 1:52, 1:53, 1:54, 1:55, 1:56, 1:57, 1:58, 1:59, 1:60, 1:61, 1:62, 1:63,1:64, 1:65, 1:66, 1:67, 1:68, 1:69, 1:70, 1:71, 1:72, 1:73, 1:74, 1:75, 1:76, 1:77, 1:78, 1:79, 1:80,1:81, 1:82, 1:83, 1:84, 1:85, 1:86, 1:87, 1:88, 1:89, 1:90, 1:91, 1:92, 1:93, 1:94, 1:95, 1:96, 1:97,1:98, 1:99, 1:100 to 1:1, 1.1:1, 1.2:1, 1.3:1, 1.4:1, 1.5:1, 1.6:1, 1.7:1, 1.8:1, 1.9:1, 2:1, 2.5:1, 3:1, 4:1, 5:1, 6:1, 7:1, 8:1, 9:1, 10:1, 11:1, 12:1, 13:1, 14:1, 15:1, 16:1, 17:1, 18:1, 19:1, 20:1, 21:1, 22:1, 23:1, 24:1, 25:1, 26:1, 27:1, 28:1, 29:1, 30:1, 31:1, 32:1, 33:1, 34:1, 35:1, 36:1, 37:1, 38:1,39:1, 40:1, 41:1, 42:1, 43:1, 44:1, 45:1, 46:1, 47:1, 48:1, 49:1, 50:1, 51:1, 52:1, 53:1, 54:1, 55:1,56:1, 57:1, 58:1, 59:1, 60:1, 61:1, 62:1, 63:1, 64:1, 65:1, 66:1, 67:1, 68:1, 69:1, 70:1, 71:1, 72:1,73:1, 74:1, 75:1, 76:1, 77:1, 78:1, 79:1, 80:1, 81:1, 82:1, 83:1, 84:1, 85:1, 86:1, 87:1, 88:1, 89:1,90:1, 91:1, 92:1, 93:1, 94:1, 95:1, 96:1, 97:1, 98:1, 99:1, 100:1, or a number or a range between any of these values). The plurality of cancer-related antigens can comprise three, four, five, size seven, or eight cancer-related antigens, each of the cancer-related antigens different from one another.Supplemental Polypeptides

[0155] In some embodiments, the supplemental polypeptides comprise costimulatory molecules. The co-stimulatory molecules cannot activate T cells independently, but are critical to the functional naive T cell response, the nature of which depends upon the outcome of integration of these stimulatory or inhibitory signals. For example, in the absence of CD28 ligation, stimulation of naive T cells induces T cell anergy in vitro, precluding an effective T cell response and promoting tolerance.

[0156] In some embodiments, the APVs comprise one or more supplemental polypeptide(s) (e.g., immunosuppressive polypeptide(s), immunostimulatory polypeptide(s),costimulatory polypeptide(s), cell adhesion polypeptide(s), anti-phagocytic polypeptide(s), tissue-homing polypeptide(s), or any combination thereof). The one or more supplemental polypeptide(s) can comprise cell-surface-molecule binding polypeptide(s), optionally antibody polypeptide(s), antibody-like polypeptide(s) and / or receptor ligand(s). In some embodiments, the use of APV-displayed antibodies / nanobodies / receptor ligands can result in targeting of the APVs to specific cell types (e.g., as a way to control tropism).

[0157] In some embodiments, the supplemental polypeptide molecules are selected from CD3s, CD3< CD4, CD5, CD8a, CD9, CD16, CD22, CD27, CD28, CD33, CD37, CD45, CD64, CD80, CD86, CD 134, CD137, CD152, CD 154, PD1, CARD11, CD2, CD7, CD27, CD28, CD30, CD40, CD54 (ICAM), CD3, CD3y, CD35, CD25, CD39, GITR, LRRC32, Neuropilin-1, CCR6, CD83, CD134 (0X40), CD137 (4-1BB), CD150 (SLAMF1), CD152 (CTLA4), CD223 (LAG3), CD270 (HVEM), CD273 (PD-L2), CD274 (PD-L1), CD278 (ICOS), DAP 10, LAT, NKD2C SLP76, TRIM, ZAP70, CD73, LFA-1, CD47, CCR7, derivatives thereof, or any combination thereof.

[0158] CD80 (Cluster of differentiation 80, B7-1) is a 254 residue type 1 transmembrane protein, consisting of an extracellular IgV-like domain that binds to it’s functional partners (e.g., PD-L1, CTLA-4 (cytotoxic T lymphocyte-associated protein 4) and CD28 (Cluster of differentiation 28)), followed by a membrane proximal IgC-like domain. CD80 plays a key regulatory role within the immune synapse. CD80 can form heterodimers with PD-L1 on the same cell membrane (in cis). The formation of CD80 / PD-L1 heterodimers inhibits PD-L1 binding to PD-1, as both CD80 and PD-1 share overlapping binding sites on PD-L1. PD- L1 shows widespread expression in tumor cells, whereas CD80 is expressed primarily on antigen-presenting cells, including dendritic cells, and is upregulated after these cells are activated. Therefore, CD80 can play a key role in antitumor immune response.

[0159] The CD83 molecule has been identified to be expressed on numerous activated immune cells, including B and T lymphocytes, monocytes, dendritic cells, microglia, and neutrophils. CD83 has two isoforms, the membrane-bound and soluble isoforms. Several studies revealed that CD83 plays a critical role in controlling and resolving immune responses. Moreover, CD83 is an essential factor during the differentiation of T and B lymphocytes, and the development and maintenance of tolerance. Orthologs of CD83 have been detected in more than 50 vertebrates including fish, reptiles, birds, and mammals. Both, murine (muCD83) and human CD83 (hCD83) are composed of an extracellular V-type Ig-like domain, a transmembrane domain, and a cytoplasmic tail.

[0160] PD-L1, also known as CD274 or B7H1, stands for programmed cell death ligand 1. It is a type I transmembrane protein that is thought to repress immune responses bybinding to its receptor (PD-1), thus inhibiting T-cell activation, proliferation, and cytokine production. It contains V-like and C-like immunoglobulin domains. PD-L1 expression is regulated by various cytokines, such as TNF-a or LPS. CD274 is a checkpoint ligand, which is expressed by various immune cells and antigen presenting cells, but also overexpressed in different cancer cells. 3 The latter results in a reduced elimination of tumour cells by CD8+ cytotoxic T lymphocytes (CTL) thereby promoting tumour progression. Increased expression of this protein in certain types of cancers, e.g., renal cell carcinoma or colon cancer, correlates with poor prognosis.

[0161] In some embodiments, the supplemental polypeptide(s) is: (i) associated with an APC-assembly domain; and / or (ii) not associated with an APC-assembly domain. In some embodiments, the nucleic acid composition comprises one or more second polynucleotide(s) encoding the one or more supplemental polypeptide(s).Antisen Presentation Complex (APC)

[0162] In some embodiments, the APC comprises or consists of components of the APC. In some embodiments, the APC comprises all or a portion of a major histocompatibility complex (MHC), a MHC-like protein (e.g., a MHC memetic, a MHC mimetic), or a derivative thereof. In some embodiments, the APC comprises all or a portion of MHC class I (MHC -I) or MHC class II (MHC-II).

[0163] In some embodiments, the APC comprises a single fusion protein. In some embodiments, the single fusion protein comprises one or more linker(s), the presenting peptide, the antigen presentation polypeptide(s), and the APC-assembly domain. In some embodiments, the antigen presentation polypeptide(s) is covalently connected to the APC-assembly domain and the presenting peptide. In some embodiments, the antigen presentation polypeptide(s) is situated between the APC-assembly domain and the presenting peptide. In some embodiments, at least one of the antigen presentation polypeptide(s) is situated between the APC-assembly domain and the presenting peptide. In some embodiments, the antigen presentation polypeptide(s) comprise two or more antigen presentation polypeptides with the presenting peptide situated between said two or more antigen presentation polypeptides. In some embodiments, the antigen presentation polypeptide(s) comprise MHC -I a chain and beta-2 microglobulin (P2M). In some embodiments, the components of the APC are connected in the order from N-terminus to C-terminus: the presenting peptide, beta-2 microglobulin (P2M), MHC-I a chain and the APC-assembly domain; or the APC-assembly domain, MHC-I a chain, beta-2 microglobulin (P2M) and the presenting peptide. In some embodiments, the antigen presentation polypeptide(s) comprise MHC-II a chain and MHC-II P chain. In some embodiments, the components of the APC are connected in the order from N-terminus to C-terminus: the APC-assembly domain, MHC-II P chain, the presenting peptide and the MHC-II a chain; the APC-assembly domain, MHC-II a chain, the presenting peptide and the MHC-II P chain; the MHC-II a chain, the presenting peptide, MHC-II P chain and the APC-assembly domain; or the MHC-II P chain, the presenting peptide, MHC-II a chain and the APC-assembly domain.

[0164] In some embodiments, the APC comprises two or more separate polypeptides. In some embodiments, the APC comprises two separate polypeptides. In some embodiments, at least two of the two or more separate polypeptides comprise an APC-assembly domain. In some embodiments, at least one of the two or more separate polypeptides is a fusion protein. In some embodiments, the fusion protein comprises one or more linker(s), the antigen presentation polypeptide(s), and the APC-assembly domain. In some embodiments, the fusion protein comprises (i) a linker, a first antigen presentation polypeptide, and the APC-assembly domain; or (ii) a linker, a second antigen presentation polypeptide, and the presenting peptide. In some embodiments, the first antigen presentation polypeptide is covalently connected to the APC-assembly domain, and the second antigen presentation polypeptide is covalently connected to the presenting peptide, optionally via a peptide bond. In some embodiments, the first antigen presentation polypeptide is capable of binding to the second antigen presentation polypeptide. In some embodiments, the first antigen presentation polypeptide comprises MHC-I a chain and the second antigen presentation polypeptide comprises beta-2 microglobulin (P2M). In some embodiments, the first antigen presentation polypeptide comprises beta-2 microglobulin (P2M) and the second antigen presentation polypeptide comprises MHC-I a chain. In some embodiments, the first antigen presentation polypeptide comprises MHC-II a chain and the second antigen presentation polypeptide comprises MHC-II P chain. In some embodiments, the first antigen presentation polypeptide comprises MHC-II P chain and the second antigen presentation polypeptide comprises MHC-II a chain. In some embodiments, MHC-I a chain is capable of forming a binding site that binds the presenting peptide. In some embodiments, MHC-II a chain and the MHC-II P chain are capable of forming a binding site that binds the presenting peptide.

[0165] In some embodiments, at least two components of the APC are derived from different species. In some embodiments, the antigen presentation polypeptides comprises peptides derived from at at least two species. In some embodiments, the antigen presentation polypeptides comprises a peptide derived from human and a peptide derived from mouse. In some embodiments, the antigen presentation polypeptides comprises at least one peptide derived from at at least two species. In some embodiments, the antigen presentation polypeptides comprises a peptide comprising a portion derived from human and a portion derived frommouse.Antisen Presentins Vesicles (APV)

[0166] In some embodiments, the APVs are derived from expression of the nucleic acid composition disclosed herein in a cell. In some embodiments, the cell is: a cell of a subject; an in vivo cell, an ex vivo cell, or an in situ cell; and / or an adherent cell or a suspension cell. In some embodiments, the cell: is not an immune cell; or is an immune cell. In some embodiments, the APVs comprise a lipid bilayer. In some embodiments, the APVs comprise a lipid bilayer derived from the cell from which the APVs was budded.

[0167] The APVs can comprise at least about 2-fold (e.g., 2-fold, 3-fold, 4-fold, 5- fold, 6-fold, 7-fold, 8-fold, 9-fold, 10-fold, 20-fold, 30-fold, 40-fold, 50-fold, 60-fold, 70-fold, 80-fold, 90-fold, 100-fold, or a number or a range between any of these values) more of the presenting peptide and / or can be at least as immunogenic (e.g., 1-fold, 1.5-fold, 2-fold, 3-fold, 4- fold, 5-fold, 6-fold, 7-fold, 8-fold, 9-fold, 10-fold, 20-fold, 30-fold, 40-fold, 50-fold, 60-fold, 70-fold, 80-fold, 90-fold, 100-fold, or a number or a range between any of these values) as compared to the presenting peptide or complex of presenting peptide and antigen presentation polypeptide that are not assembled into vesicles.

[0168] The APVs can comprise at least about 2-fold (e.g., 2-fold, 3-fold, 4-fold, 5- fold, 6-fold, 7-fold, 8-fold, 9-fold, 10-fold, 20-fold, 30-fold, 40-fold, 50-fold, 60-fold, 70-fold, 80-fold, 90-fold, 100-fold, or a number or a range between any of these values) more of the presenting peptide, an at least about 2-fold (e.g., 2-fold, 3-fold, 4-fold, 5-fold, 6-fold, 7-fold, 8- fold, 9-fold, 10-fold, 20-fold, 30-fold, 40-fold, 50-fold, 60-fold, 70-fold, 80-fold, 90-fold, 100- fold, or a number or a range between any of these values) higher density of the presenting peptide, and / or can be at least as immunogenic (e.g., 1-fold, 1.5-fold, 2-fold, 3-fold, 4-fold, 5- fold, 6-fold, 7-fold, 8-fold, 9-fold, 10-fold, 20-fold, 30-fold, 40-fold, 50-fold, 60-fold, 70-fold, 80-fold, 90-fold, 100-fold, or a number or a range between any of these values), as compared to the presenting peptide or complex of presenting peptide and antigen presentation polypeptide that are not assembled into vesicles.

[0169] The APVs can have one or more dimensions of a eukaryotic virus. In some embodiments, less than about 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, or 10%, of the APVs of the population of APVs have a particle size smaller than about 10 nm. In some embodiments, less than about 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, or 10%, of the APVs of the population of APVs have a particle size exceeding about 80 nm. In some embodiments, the average diameter of the APVs of the population of APVs range from about 5 nm to about 80 nm, from about 15 nm to about 50 nm, or from about 20 nm to about 40 nm. The average diameter of the APVs of the population of APVs can be about 10 nm, about 12 nm, about 14 nm, about 16 nm,about 18 nm, about 20 nm, about 22 nm, about 24 nm, about 26 nm, about 28 nm, about 30 nm, about 32 nm, about 34 nm, about 36 nm, about 38 nm, about 40 nm, about 42 nm, about 44 nm, about 46 nm, about 48 nm, or about 50 nm, optionally the average is the mean, median or mode, optionally the mean is the arithmetic mean, geometric mean, and / or harmonic mean.

[0170] In some embodiments, the APVs have a minimum diameter of about 10 nm, about 12 nm, about 14 nm, about 16 nm, about 18 nm, about 20 nm, about 22 nm, about 24 nm, about 26 nm, about 28 nm, about 30 nm, about 32 nm, about 34 nm, about 36 nm, about 38 nm, about 40 nm, about 42 nm, about 44 nm, about 46...

Claims

WHAT IS CLAIMED IS:

1. A composition, comprising: a nucleic acid composition comprising one or more polynucleotides encoding components of an antigen presentation complex (APC), wherein the components of the APC are capable of assembling into an antigen-presenting vesicle (APV) budded from a cell in which the APC components are expressed, wherein the APV comprises a plurality of APCs, and wherein the APC comprises an APC-assembly domain, one or more antigen presentation polypeptide(s) and a presenting peptide.

2. A composition, comprising: a population of an antigen-presenting vesicles (APVs), wherein each of the APVs comprises a plurality of antigen presentation complexes (APCs), and wherein the APC comprises an APC-assembly domain, one or more antigen presentation polypeptide(s) and a presenting peptide.

3. The composition of claim 2, wherein the APVs are derived from expression of the nucleic acid composition of claim 1 in a cell, and wherein the APC comprises or consists of components of the APC.

4. The composition of any one of claims 1-3, wherein the APC comprises all or a portion of a major histocompatibility complex (MHC), a MHC mimetic, or a derivative thereof.

5. The composition of any one of claims 1-4, wherein the APC comprises all or a portion of MHC class I (MHC-I) or MHC class II (MHC-II).

6. The composition of any one of claims 4-5, wherein the MHC comprises human leukocyte antigen (HLA) and / or mouse MHC.

7. The composition of any one of claims 1-6, wherein the antigen presentation polypeptide(s) are selected from the group consisting of MHC-I a chain, beta-2 microglobulin (P2M), MHC-II a chain, MHC-II P chain, a classical HLA Class I molecule, a non-classical HLA Class I molecule, a classical HLA Class II molecule, a non-classical HLA Class II molecule, HL A- A, HLA-B, HLA-C, HLA-E, HLA-F, HLA-G, HLA-DRA, HLA-DRB1, HLA- DRB3, HLA-DRB4, HLA-DRB5, HLA-DQA1, HLA-DQB1, HLA-DPA1, HLA-DPB1, HLA- DMA, HLA-DMB, HLA-DOA, HLA-DOB, derivatives thereof, homologs thereof, or any combination thereof.

8. The composition of any one of claims 1-7, wherein the HLA class I is selected from an HLA allele selected from the group consisting of HLA-A*01:01, HLA-A*02:01, HLA-A*02:03, HLA-A*02:06, HLA-A*03:01, HLA-A* 11:01, HLA-A*23:01, HLA-A*24:02, HLA- A*26:01, HLA-A*30:01, HLA-A*30:02, HLA-A*31:01, HLA-A*32:01, HLA-A*33:01, HLA- A*68:01, HLA-A*68:02, HLA-B*07:02, HLA-B*08:01, HLA-B*15:01, HLA-B*35:01, HLA- B*40:01, HLA-B*44:02, HLA-B*44:03, HLA-B*51:01, HLA-B*53:01, HLA-B*57:01, and HLA-B*58:01.

9. The composition of any one of claims 1-8, wherein the HLA class II is selected from an HLA allele selected from the group consisting of HLA-DRBl*01:01, HLA- DRBl*15:01, HLA-DRB 1*03:01, HLA-DRB 1*04:01, HLA-DRBl*ll:01, HLA-DRBl*13:01, HLA-DRB 1*07:01, HLA-DRBl*01:01, HLA-DRB 1*01:02, HLA-DRB 1*04: 02, HLA- DRBl*04:05, HLA-DRB 1*04: 07, HLA-DRB 1*04: 08, HLA-DRB 1*08:04, HLA-DRB 1*09:01, HLA-DRBl*10:01, HLA-DRB1*11:O2, HLA-DRBl*l l:03, HLA-DRB1*11:O4, HLA- DRB1*15:O2, HLA-DRB1* 15:03, HLA-DRB1*16:O1, HLA-DRB 1*16:02, HLA-DRB3 *02:02,HLA-DRB3*03:01, HLA-DRB5*01:01, HLA-DQAl*01:01 / DQBl*05:01, HLA-DQAl*05:01 / DQBl*02:01, HLA-DQAl*01:02 / DQBl*05:02, HLA-DQA1 *01 :02 / DQB 1*06:02, HLA-DQAl*03:01 / DQBl*03:02, HLA-DQA1 *01 :02 / DQB 1*06:04, HLA-DQAl*05:01 / DQBl*03:01, HLA-DQAl*02:01 / DQB 1*02:02, HLA-DQA1 *03 :01 / DQB 1*03:01, HLA-DQAl*02:01 / DQB 1*03:03, HLA-DQA1 *03 :03 / DQB 1*03:03, HLA-DPAl*01:03 / DPBl*01:01, HLA-DPAl*01:03 / DPBl*02:01, HLA-DPAl*01:03 / DPBl*03:01, HLA-DPAl*01:03 / DPBl*04:01, HLA-DPA1 *01 :03 / DPB 1*04:02, HLA-DPAl*01:03 / DPBl*05:01, HLA-DPAl*02:01 / DPBl*01:01, HLA-DPAl*02:01 / DPBl*02:01, HLA-DPAl*02:01 / DPBl*03:01, HLA-DPAl*02:01 / DPB 1*04:01, HLA-DPAl*02:01 / DPBl*04:02, HLA-DPAl*02:01 / DPBl*05:01, HLA-DPAl*02:01 / DPBl*06:01, HLA-DPAl*02:01 / DPBl*09:01, HLA-DPAl*02:01 / DPBl*l l:01, HLA-DPAl*02:01 / DPBl*13:01, HLA-DPAl*02:01 / DPBl*14:01, HLA-DPAl*02:01 / DPBl*15:01, and HLA-DPA1*O2:O1 / DPB1*17:OL10. The composition of any one of claims 1-9, wherein at least two components of the APC are derived from different species.

11. The composition of any one of claims 1-10, wherein the APC comprises at least one mutation at positions equivalent to Y84 and A139 of HLA-A, optionally Y84A and / or A139C.

12. The composition of any one of claims 1-11, wherein the antigen presentation polypeptide(s) is capable of forming a binding site that binds the presenting peptide.

13. The composition of any one of claims 1-12, wherein: the presence of the antigen presentation polypeptide(s) does not induce animmune response in a subject, optionally a subject from which the cell was derived; and / or wherein the presence of the antigen presentation polypeptide(s) induces an immune response in a subject, optionally a subject from which the cell was derived.

14. The composition of any one of claims 1-13, wherein the antigen presentation polypeptide(s) comprises an amino acid sequence having at least 65%, 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% sequence identity to an amino acid sequence selected from the group consisting of SEQ ID NOs: 53-54, 57-58, 61-62, 81-86, 112-113, 120-121, 144-145, and 152- 153.

15. The composition of any one of claims 1 and 3-14, wherein the cell is: a cell of a subject; an in vivo cell, an ex vivo cell, or an in situ cell; and / or an adherent cell or a suspension cell.

16. The composition of any one of claims 1 and 3-15, wherein the cell: is not an immune cell; or is an immune cell.

17. The composition of any one of claims 1-16, wherein the APC-assembly domain recruits one or more endosomal sorting complex required for transport (ESCRT) proteins to the cytoplasmic tail of the APC, optionally the recruitment of ESCRT proteins via the APC- assembly domain induces the self-assembly and budding of APV.

18. The composition of any one of claims 1-17, wherein the cytoplasmic portion of the APC comprises the APC-assembly domain, optionally the cytoplasmic tail of the APC comprises the APC-assembly domain.

19. The composition of any one of claims 1-18, wherein the APC-assembly domain interacts with the ESCRT proteins TSG101, NEDD4, and / or ALIX.

20. The composition of any one of claims 1-19, wherein the APC-assembly domain comprises or is derived from: the ESCRT and ALIX binding region (EABR) of the human CEP55 protein, optionally residues 160-217; a nonhuman protein, optionally a nonmammalian protein, further optionally a chicken protein, a mouse protein, a lizard protein, a reptile protein, a hamster protein, or a goldfish protein;Syntenin-1, rat Galectin-3 (rGalectin-3), Hrs, and / or CD2AP; a viral protein, optionally a fragment of a viral protein, further optionally a retroviral protein, herpes simplex viral protein, vaccinia viral protein, hepadnaviralprotein, togaviral protein, flaviviral protein, arenaviral protein, coronaviral protein, orthomyxoviral protein, paramyxoviral protein, bunyaviral protein, bornaviral protein, rhabdoviral protein or filoviral protein, optionally a Gag protein, further optionally derived from EIAV, HTLV-1, MLV, or MPMV, optionally EIAV p9 and / or HIV-1 p6; and / or an Ebola protein, optionally EBOV VP40.

21. The composition of any one of claims 1-20, wherein the APC-assembly domain comprises an amino acid sequence having at least 65%, 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% sequence identity to an amino acid sequence of SEQ ID NO: 33.

22. The composition of any one of claims 1-21, wherein the presenting peptide, or a portion thereof, is displayed on the surface of the APV.

23. The composition of any one of claims 1-22, wherein the presenting peptide: is about 1 amino acid to about 10000 amino acids in length, optionally 5-20 amino acids in length, further optionally 5, 6, 7, 8, 9, 10, 11, or 12 amino acids in length; comprises or is derived from an antigenic protein associated with a disease or disorder, optionally an immunogenic variant and / or an immunogenic fragment of said antigenic protein; comprises or is derived from a conserved portion of said antigenic protein; and / or comprises or is derived from at least about 0.001 percent, about 0.01 percent, about 0.05 percent, about 0.1 percent, about 0.2 percent, about 0.4 percent, about 0.6 percent, about 0.8 percent, about 1 percent, about 2 percent, about 3 percent, about 4 percent, or about 5 percent of the full length of said antigenic protein.

24. The composition of claim 23, wherein the disease or disorder is an infectious disease or disorder caused by an infectious agent, wherein the presenting peptide comprises or is derived from an antigenic protein of said infectious agent, and wherein the antigenic protein of said infectious agent is a pathogenic antigen; wherein the disease or disorder is a disease associated with expression of a tumor-associated antigen, and wherein the antigenic protein is a tumor-associated antigen; wherein the disease or disorder is a disease associated with expression of a cancer-associated antigen, and wherein the antigenic protein is a cancer-associated antigen; wherein the disease or disorder is an autoimmune disease or disorder, and wherein the antigenic protein is an autoimmune antigen;wherein the disease or disorder is a metabolic disorder, optionally the metabolic disorder is diabetes; and / or wherein the disease or disorder is an allergic disease or disorder, and wherein the antigenic protein is an allergenic antigen.

25. The composition of claim 24, wherein the infectious agent is: a bacterium, a fungus, a virus, or a protist; and / or a coronavirus (CoV), optionally the CoV comprises an alphacoronavirus, a betacoronavirus, a gammacoronavirus, or a deltacoronavirus.

26. The composition of claim 24 or 25, wherein the infectious agent is selected from the group consisting of Acinetobacter baumannii, Anaplasma genus, Anaplasma phagocytophilum, Ancylostoma braziliense, Ancylostoma duodenale, Arcanobacterium haemolyticum, Ascaris lumbricoides, Aspergillus genus, Astroviridae, Babesia genus, Bacillus anthracis, Bacillus cereus, Bartonella henselae, BK virus, Blastocystis hominis, Blastomyces dermatitidis, Bordetella pertussis, Borrelia burgdorferi, Borrelia genus, Borrelia spp, Brucella genus, Brugia malayi, Bunyaviridae family, Burkholderia cepacia and other Burkholderia species, Burkholderia mallei, Burkholderia pseudomallei, Caliciviridae family, Campylobacter genus, Candida albicans, Candida spp, Chlamydia trachomatis, Chlamydophila pneumoniae, Chlamydophila psittaci, CJD prion, Clonorchis sinensis, Clostridium botulinum, Clostridium difficile, Clostridium perfringens, Clostridium perfringens, Clostridium spp, Clostridium tetani, Coccidioides spp, coronaviruses, Corynebacterium diphtheriae, Coxiella burnetii, Crimean-Congo hemorrhagic fever virus, Cryptococcus neoformans, Cryptosporidium genus, Cytomegalovirus (CMV), Dengue viruses (DEN-1, DEN- 2, DEN-3 and DEN-4), Dientamoeba fragilis, Ebolavirus (EBOV), Echinococcus genus, Ehrlichia chaffeensis, Ehrlichia ewingii, Ehrlichia genus, Entamoeba histolytica, Enterococcus genus, Enterovirus genus, Enteroviruses, mainly Coxsackie A virus and Enterovirus 71 (EV71), Epidermophyton spp, Epstein-Barr Virus (EBV), Escherichia coli O157:H7, 0111 and 0104 :H4, Fasciola hepatica and Fasciola gigantica, FFI prion, Filarioidea superfamily, Filoviruses, Flaviviruses, Francisella tularensis, Fusobacterium genus, Geotrichum candidum, Giardia intestinalis, Gnathostoma spp, GSS prion, Guanarito virus, Haemophilus ducreyi, Haemophilus influenzae, Helicobacter pylori, Henipavirus (Hendra virus Nipah virus), Hepatitis A Virus, Hepatitis B Virus (HBV), Hepatitis C Virus (HCV), Hepatitis D Virus, Hepatitis E Virus, Herpes simplex virus 1 and 2 (HSV-1 and HSV-2), Histoplasma capsulatum, HIV (Human immunodeficiency virus), Hortaea werneckii, Human bocavirus (HBoV), Human herpesvirus 6 (HHV-6) and Human herpesvirus 7 (HHV-7), Human metapneumovirus (hMPV), Human papillomavirus (HPV), Human parainfluenza viruses(HPIV), Japanese encephalitis virus, JC virus, Junin virus, Kingella kingae, Klebsiella granulomatis, Kuru prion, Lassa virus, Legionella pneumophila, Leishmania genus, Leptospira genus, Listeria monocytogenes, Lymphocytic choriomeningitis virus (LCMV), Machupo virus, Malassezia spp, Marburg virus, Measles virus, Metagonimus yokagawai, Microsporidia phylum, Molluscum contagiosum virus (MCV), Mumps virus, Mycobacterium leprae and Mycobacterium lepromatosis, Mycobacterium tuberculosis, Mycobacterium ulcerans, Mycoplasma pneumoniae, Naegleria fowleri, Necator americanus, Neisseria gonorrhoeae, Neisseria meningitidis, Nocardia asteroides, Nocardia spp, Onchocerca volvulus, Orientia tsutsugamushi, Orthomyxoviridae family (Influenza), Paracoccidioides brasiliensis, Paragonimus spp, Paragonimus westermani, Parvovirus Bl 9, Pasteurella genus, Plasmodium genus, Pneumocystis jirovecii, Poliovirus, Rabies virus, Respiratory syncytial virus (RSV), Rhinovirus, rhinoviruses, Rickettsia akari, Rickettsia genus, Rickettsia prowazekii, Rickettsia rickettsii, Rickettsia typhi, Rift Valley fever virus, Rotavirus, Rubella virus, Sabia virus, Salmonella genus, Sarcoptes scabiei, SARS coronavirus, Schistosoma genus, Shigella genus, Sin Nombre virus, Hantavirus, Sporothrix schenckii, Staphylococcus genus, Staphylococcus genus, Streptococcus agalactiae, Streptococcus pneumoniae, Streptococcus pyogenes, Strongyloides stercoralis, Taenia genus, Taenia solium, Tick-borne encephalitis virus (TBEV), Toxocara canis or Toxocara cati, Toxoplasma gondii, Treponema pallidum, Trichinella spiralis, Trichomonas vaginalis, Trichophyton spp, Trichuris trichiura, Trypanosoma brucei, Trypanosoma cruzi, Ureaplasma urealyticum, Varicella zoster virus (VZV), Variola major or Variola minor, vCJD prion, Venezuelan equine encephalitis virus, Vibrio cholerae, West Nile virus, Western equine encephalitis virus, Wuchereria bancrofti, Yellow fever virus, Yersinia enterocolitica, Yersinia pestis, and Yersinia pseudotuberculosis.

27. The composition of any one of claims 1-26, wherein the presenting peptide is derived from one or more of MART-1; NYESO1; neuropilin (NRP); IGRP; CD 19; CD 123; CD22; CD30; CD171; CS-1 (also referred to as CD2 subset 1, CRACC, SLAMF7, CD319, and 19A24); C-type lectin-like molecule- 1 (CLL-1 or CLECL1); CD33; epidermal growth factor receptor variant III (EGFRvIII); ganglioside G2 (GD2); ganglioside GD3 (aNeu5Ac(2- 8)aNeu5Ac(2-3)bDGalp(l-4)bDGlcp(l-l)Cer); TNF receptor family member B cell maturation (BCMA); Tn antigen ((Tn Ag) or (GalNAca-Ser / Thr)); prostate-specific membrane antigen (PSMA); Receptor tyrosine kinase-like orphan receptor 1 (R0R1); Fms-Like Tyrosine Kinase 3 (FLT3); Tumor-associated glycoprotein 72 (TAG72); CD38; CD44v6; Carcinoembryonic antigen (CEA); Epithelial cell adhesion molecule (EPCAM); B7H3 (CD276); KIT (CD117); Interleukin- 13 receptor subunit alpha-2 (IL-13Ra2 or CD213A2); Mesothelin; Interleukin 11receptor alpha (IL-l lRa); prostate stem cell antigen (PSCA); Protease Serine 21 (Testisin or PRSS21); vascular endothelial growth factor receptor 2 (VEGFR2); Lewis(Y) antigen; CD24; Platelet-derived growth factor receptor beta (PDGFR-beta); Stage-specific embryonic antigen-4 (SSEA-4); CD20; Folate receptor alpha; Receptor tyrosine-protein kinase ERBB2 (Her2 / neu); Mucin 1, cell surface associated (MUC1); epidermal growth factor receptor (EGFR); neural cell adhesion molecule (NCAM); Prostase; prostatic acid phosphatase (PAP); elongation factor 2 mutated (ELF2M); Ephrin B2; fibroblast activation protein alpha (FAP); insulin-like growth factor 1 receptor (IGF -I receptor), carbonic anhydrase IX (CAIX); Proteasome (Prosome, Macropain) Subunit, Beta Type, 9 (LMP2); glycoprotein 100 (gplOO); oncogene fusion protein consisting of breakpoint cluster region (BCR) and Abelson murine leukemia viral oncogene homolog 1 (Abl) (bcr-abl); tyrosinase; ephrin type-A receptor 2 (EphA2); Fucosyl GM1; sialyl Lewis adhesion molecule (sLe); ganglioside GM3 (aNeu5Ac(2-3)bDGalp(l-4)bDGlcp(l-l)Cer); transglutaminase 5 (TGS5); high molecular weight-melanoma-associated antigen (HMWMAA); o-acetyl-GD2 ganglioside (OAcGD2); Folate receptor beta; tumor endothelial marker 1 (TEM1 / CD248); tumor endothelial marker 7-related (TEM7R); claudin 6 (CLDN6); thyroid stimulating hormone receptor (TSHR); G protein-coupled receptor class C group 5, member D (GPRC5D); chromosome X open reading frame 61 (CXORF61); CD97; CD179a; anaplastic lymphoma kinase (ALK); Polysialic acid; placenta-specific 1 (PLAC1); hexasaccharide portion of globoH glycoceramide (GloboH); mammary gland differentiation antigen (NY-BR-1); uroplakin 2 (UPK2); Hepatitis A virus cellular receptor 1 (HAVCR1); adrenoceptor beta 3 (ADRB3); pannexin 3 (PANX3); G protein-coupled receptor 20 (GPR20); lymphocyte antigen 6 complex, locus K 9 (LY6K); Olfactory receptor 51E2 (OR51E2); TCR Gamma Alternate Reading Frame Protein (TARP); Wilms tumor protein (WT1); Cancer / testis antigen 1 (NY- ESO-1); Cancer / testis antigen 2 (LAGE-la); Melanoma-associated antigen 1 (MAGE-A1); ETS translocation-variant gene 6, located on chromosome 12p (ETV6-AML); sperm protein 17 (SPA17); X Antigen Family, Member 1A (XAGE1); angiopoietin-binding cell surface receptor 2 (Tie 2); melanoma cancer testis antigen-1 (MAD-CT-1); melanoma cancer testis antigen-2 (MAD-CT-2); Fos-related antigen 1; tumor protein p53 (p53); p53 mutant; prostein; survivin; telomerase; prostate carcinoma tumor antigen- 1 (PCTA-1 or Galectin 8), melanoma antigen recognized by T cells 1 (MelanA or MARTI); Rat sarcoma (Ras) mutant; human Telomerase reverse transcriptase (hTERT); sarcoma translocation breakpoints; melanoma inhibitor of apoptosis (ML-IAP); ERG (transmembrane protease, serine 2 (TMPRSS2) ETS fusion gene); N- Acetyl glucosaminyl-transferase V (NA17); paired box protein Pax-3 (PAX3); Androgen receptor; Cyclin Bl; v-myc avian myelocytomatosis viral oncogene neuroblastoma derived homolog (MYCN); Ras Homolog Family Member C (RhoC); Tyrosinase-related protein 2(TRP-2); Cytochrome P450 1B1 (CYP1B1); CCCTC-Binding Factor (Zinc Finger Protein)-Like (BORIS or Brother of the Regulator of Imprinted Sites), Squamous Cell Carcinoma Antigen Recognized By T Cells 3 (SART3); Paired box protein Pax-5 (PAX5); proacrosin binding protein sp32 (OY-TES1); lymphocyte-specific protein tyrosine kinase (LCK); A kinase anchor protein 4 (AKAP-4); synovial sarcoma, X breakpoint 2 (SSX2); Receptor for Advanced Glycation Endproducts (RAGE-1); renal ubiquitous 1 (RU1); renal ubiquitous 2 (RU2); legumain; human papilloma virus E6 (HPV E6); human papilloma virus E7 (HPV E7); intestinal carboxyl esterase; heat shock protein 70-2 mutated (mut hsp70-2); CD79a; CD79b; CD72; Leukocyte-associated immunoglobulin-like receptor 1 (LAIR1); Fc fragment of IgA receptor (FCAR or CD89); Leukocyte immunoglobulin-like receptor subfamily A member 2 (LILRA2); CD300 molecule-like family member f (CD300LF); C-type lectin domain family 12 member A (CLEC12A); bone marrow stromal cell antigen 2 (BST2); EGF-like module-containing mucinlike hormone receptor-like 2 (EMR2); lymphocyte antigen 75 (LY75); Glypican-3 (GPC3); Fc receptor-like 5 (FCRL5); and immunoglobulin lambda-like polypeptide 1 (IGLL1).

28. The composition of any one of claims 1-27, wherein the APC comprises one or more linker(s), and wherein the one or more linker(s): comprise one or more flexible amino acid residue(s), optionally about 1 to about 50 flexible amino acid residues, further optionally the flexible amino acid residues comprise glycine, serine, or a combination thereof; is a glycine-serine (GS) linker, optionally 1-25 amino acids in length; and / or is situated between the APC-assembly domain and the presenting peptide, between the APC-assembly domain and the antigen presentation polypeptide, between the antigen presentation polypeptide and the presenting peptide, and / or between two of the one or more antigen presentation polypeptides.

29. The composition of claim 28, wherein the linker comprises an amino acid sequence selected from the group consisting of GSGSGSG (SEQ ID NO: 1), GGGGS (SEQ ID NO: 2), GSGSG (SEQ ID NO: 3), GGGG (SEQ ID NO: 4), GGG, GG, GS, GSGS (SEQ ID NO: 8), GGGS (SEQ ID NO: 9), GGS, GTS, GGSGGS (SEQ ID NO: 12), GGG, GGGGGG (SEQ ID NO: 14), GGGGGGGGG (SEQ ID NO: 15), GGGGGGGGGGGG (SEQ ID NO: 16), GGGGGGGGGGGGGGG (SEQ ID NO: 17), GGS, GGSGGS (SEQ ID NO: 19), GGSGGSGGS (SEQ ID NO: 20), GGSGGSGGSGGS (SEQ ID NO: 21), GGSGGSGGSGGSGGS (SEQ ID NO: 22), GSG, GSGGSG (SEQ ID NO: 24), GSGGSGGSG (SEQ ID NO: 25), GSGGSGGSGGSG (SEQ ID NO: 26), GS GGS GGS GGS GGS G (SEQ ID NO: 27), (GGGGS)n (SEQ ID NO: 28), GGGGSGGGGS (SEQ ID NO: 29), GGGGSGGGGSGGGGS (SEQ ID NO: 30), GGGGSGGGGSGGGGSGGGGS (SEQ ID NO:31), and GGGGSGGGGSGGGGSGGGGSGGGGS (SEQ ID NO: 32).

30. The composition of any one of claims 28-29, wherein the linker: comprises an amino acid sequence of GGGGS (SEQ ID NO: 2) or GGGS (SEQ ID NO: 9); and / or comprises n GGGGS (SEQ ID NO: 2) or GGGS (SEQ ID NO: 9), wherein n is an integer from 1 to 10, optionally n is 3 or 4.

31. The composition of any one of claims 1-30, wherein the APC comprises a single fusion protein.

32. The composition of claim 31, wherein the single fusion protein comprises one or more linker(s), the presenting peptide, the antigen presentation polypeptide(s), and the APC- assembly domain.

33. The composition of claim 32, wherein the antigen presentation polypeptide(s) is covalently connected to the APC-assembly domain and the presenting peptide.

34. The composition of any one of claims 31-33, wherein: the antigen presentation polypeptide(s) is situated between the APC-assembly domain and the presenting peptide; at least one of the antigen presentation polypeptide(s) is situated between the APC-assembly domain and the presenting peptide; the antigen presentation polypeptide(s) comprise two or more antigen presentation polypeptides with the presenting peptide situated between said two or more antigen presentation polypeptides; and / or the antigen presentation polypeptide(s) comprise MHC-I a chain and beta-2 microglobulin (P2M).

35. The composition of claim 34, wherein the components of the APC are connected in the order from N-terminus to C-terminus: the presenting peptide, beta-2 microglobulin (P2M), MHC-I a chain and the APC-assembly domain; or the APC-assembly domain, MHC-I a chain, beta-2 microglobulin (P2M) and the presenting peptide.

36. The composition of any one of claims 31-35, wherein the antigen presentation polypeptide(s) comprise MHC-II a chain and MHC-II P chain.

37. The composition of claim 36, wherein the components of the APC are connected in the order from N-terminus to C-terminus: the APC-assembly domain, MHC-II P chain, the presenting peptide and the MHC-II a chain; the APC-assembly domain, MHC-II a chain, the presenting peptide and the MHC-II P chain; the MHC-II a chain, the presenting peptide, MHC-II P chain and the APC-assembly domain; or the MHC-II P chain, the presenting peptide, MHC-II a chain and the APC-assembly domain.

38. The composition of any one of claims 1-37, wherein the APC comprises two or more separate polypeptides, optionally two separate polypeptides, further optionally at least two of the two or more separate polypeptides comprise an APC-assembly domain.

39. The composition of claim 38, wherein at least one of the two or more separate polypeptides is a fusion protein.

40. The composition of claim 39, wherein the fusion protein comprises one or more linker(s), the antigen presentation polypeptide(s), and the APC-assembly domain.

41. The composition of any one of claims 38-40, wherein the fusion protein comprises (i) a linker, a first antigen presentation polypeptide, and the APC-assembly domain; or (ii) a linker, a second antigen presentation polypeptide, and the presenting peptide.

42. The composition of claim 41, wherein the first antigen presentation polypeptide is covalently connected to the APC-assembly domain, and the second antigen presentation polypeptide is covalently connected to the presenting peptide, optionally via a peptide bond.

43. The composition of any one of claims 41-42, wherein the first antigen presentation polypeptide is capable of binding to the second antigen presentation polypeptide.

44. The composition of any one of claims 41-43, wherein the first antigen presentation polypeptide comprises MHC-I a chain and the second antigen presentation polypeptide comprises beta-2 microglobulin (P2M); wherein the first antigen presentation polypeptide comprises beta-2 microglobulin (P2M) and the second antigen presentation polypeptide comprises MHC-I a chain; wherein the first antigen presentation polypeptide comprises MHC-II a chain and the second antigen presentation polypeptide comprises MHC-II P chain; or wherein the first antigen presentation polypeptide comprises MHC-II P chain and the second antigen presentation polypeptide comprises MHC-II a chain.

45. The composition of claim 44, wherein MHC-I a chain is capable of forming a binding site that binds the presenting peptide.

46. The composition of claim 44, wherein MHC-II a chain and the MHC-II P chain are capable of forming a binding site that binds the presenting peptide.

47. The composition of any one of claims 1-46, wherein the APC comprises an amino acid sequence having at least 65%, 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% sequence identity to an amino acid sequence selected from the group consisting of SEQ ID NOs: 37-52, 55-56, 59-60, 63-80, 114-119, 122-143, 146-151, and 154-159.

48. The composition of any one of claims 1-47, wherein the APVs comprise one or more supplemental polypeptide(s), optionally immunosuppressive polypeptide(s),immunostimulatory polypeptide(s), costimulatory polypeptide(s), cell adhesion polypeptide(s), anti -phagocytic polypeptide(s), tissue-homing polypeptide(s), cell-surface-molecule binding polypeptide(s), or any combination thereof.

49. The composition of any one of claims 1-48, wherein the supplemental polypeptide(s) are selected from the group consisting of CD3s, CD3(^, CD4, CD5, CD8a, CD9, CD16, CD22, CD27, CD28, CD33, CD37, CD45, CD64, CD80, CD86, CD 134, CD137, CD 152, CD 154, PD1, CARD11, CD2, CD7, CD27, CD28, CD30, CD40, CD54 (ICAM), CD83, CD134 (0X40), CD137 (4-1BB), CD150 (SLAMF1), CD152 (CTLA4), CD223 (LAG3), CD270 (HVEM), CD273 (PD-L2), CD274 (PD-L1), CD278 (ICOS), DAP10, LAT, NKD2C SLP76, TRIM, ZAP70, CD73, LFA-1, CD47, CCR7, CD3, CD3y, CD35, CD25, CD39, GITR, LRRC32, Neuropilin- 1, CCR6, derivatives thereof, or any combination thereof.

50. The composition of any one of claims 1-49, wherein the supplemental polypeptide(s) is: (i) associated with an APC-assembly domain; and / or (ii) not associated with an APC-assembly domain.

51. The composition of any one of claims 1 and 3-50, wherein the nucleic acid composition comprises one or more second polynucleotide(s) encoding the one or more supplemental polypeptide(s).

52. The composition of any one of claims 1 and 3-51, wherein the APVs comprise a lipid bilayer, optionally a lipid bilayer derived from the cell from which the APVs was budded.

53. The composition of any one of claims 1-52, wherein at least two of the APCs of the plurality of APCs are different from each other with respect to the presenting peptide, and wherein the population of APVs thereby display a plurality of disparate presenting peptides.

54. The composition of any one of claims 2-53, wherein the population of APVs comprise: one or more homotypic APVs, wherein the plurality of APCs of a homotypic APV are the same as each other with respect to the presenting peptide, and wherein a homotypic APV thereby does not display a plurality of disparate presenting peptides; one or more heterotypic APVs, wherein at least two of the APCs of a heterotypic APV are different from each other with respect to the presenting peptide, and wherein a heterotypic APV thereby displays a plurality of disparate presenting peptides; a mixture of two or more homotypic APVs that differ from each other with respect to the presenting peptide of the plurality of APCs present in said two or more homotypic APVs, and wherein the population of APVs thereby displays a plurality of disparate presenting peptides; a mixture of two or more heterotypic APVs that differ from each other with respect to the presenting peptide of the plurality of APCs of said two or more heterotypic APVs; and / ora mixture of one or more homotypic APVs and one or more heterotypic APVs, and wherein the population of APVs thereby displays a plurality of disparate presenting peptides.

55. The composition of any one of claims 2-54, wherein the plurality of disparate presenting peptides comprises: between about 2 and about 500 antigenic peptides that differ from each other; presenting peptide of a same protein type; and / or presenting peptide of different protein types.

56. The composition of any one of claims 2-55, wherein: less than about 10% of the APVs of the population of APVs have a particle size smaller than about 30 nm; less than about 10% of the APVs of the population of APVs have a particle size exceeding about 100 nm; the average diameter of the APVs of the population of APVs range from about 30 nm to about 250 nm, from about 50 nm to about 125 nm, or from about 60 nm to about 80 nm; and / or the average diameter of the APVs of the population of APVs is about 50 nm, about 52 nm, about 54 nm, about 56 nm, about 58 nm, about 60 nm, about 62 nm, about 64 nm, about 66 nm, about 68 nm, 70 nm, about 72 nm, about 74 nm, about 76 nm, about 78 nm, about 80 nm, about 82 nm, about 84 nm, about 86 nm, about 88 nm, or about 90 nm, optionally the average is the mean, median or mode, optionally the mean is the arithmetic mean, geometric mean, and / or harmonic mean.

57. The composition of any one of claims 2-56, wherein the APVs: have a minimum diameter of about 10 nm, about 12 nm, about 14 nm, about 16 nm, about 18 nm, about 20 nm, about 22 nm, about 24 nm, about 26 nm, about 28 nm, about 30 nm, about 32 nm, about 34 nm, about 36 nm, about 38 nm, about 40 nm, about 42 nm, about 44 nm, about 46 nm, about 48 nm, or about 50 nm; and / or have a maximum diameter of about 250 nm, about 252 nm, about 254 nm, about 256 nm, about 258 nm, about 260 nm, about 262 nm, about 264 nm, about 266 nm, about 268 nm, about 270 nm, about 272 nm, about 274 nm, about 276 nm, about 278 nm, or about 280 nm.

58. The composition of any one of claims 1-57, wherein the APV and / or the APC is capable of inducing immunogenic responses against the presenting peptide in a subject without the administration of exogenous antigen presenting cells and / or exogenous antigen presenting components other than the APV and / or the APC.

59. The composition of any one of claims 1-58, wherein the nucleic acid composition is complexed or associated with one or more lipids or lipid-based carriers, thereby forming liposomes, lipid nanoparticles (LNPs), lipoplexes, and / or nanoliposomes, optionallyencapsulating the nucleic acid composition.

60. The composition of any one of claims 1-59, wherein the nucleic acid composition is, comprises, or further comprises, one or more vectors, optionally at least one of the one or more vectors is a viral vector, a plasmid, a transposable element, a naked DNA vector, a lipid nanoparticle (LNP), or any combination thereof, optionally the viral vector is an AAV vector, a lentivirus vector, a retrovirus vector, an adenovirus vector, a herpesvirus vector, a herpes simplex virus vector, a cytomegalovirus vector, a vaccinia virus vector, a MVA vector, a baculovirus vector, a vesicular stomatitis virus vector, a human papillomavirus vector, an avipox virus vector, a Sindbis virus vector, a VEE vector, a Measles virus vector, an influenza virus vector, a hepatitis B virus vector, an integrationdeficient lentivirus (IDLV) vector, or any combination thereof, and optionally the transposable element is piggybac transposon or sleeping beauty transposon.

61. The composition of any one of claims 1-60, wherein the polynucleotide(s) encoding components of the APC are comprised in the one or more vectors, optionally the polynucleotide(s) encoding components of the APC are comprised in the same vector and / or different vectors, optionally the polynucleotide(s) encoding components of the APC are situated on the same nucleic acid and / or different nucleic acids.

62. The composition of any one of claims 1-61, wherein the one or more vectors is a DNA vaccine, optionally the polynucleotide(s) encoding components of the APC are operably linked to one or more promoters capable of inducing transcription of said polynucleotide(s), optionally the DNA vaccine is a plasmid-based DNA vaccine, a minicircle-based DNA vaccine, a bacmid-based DNA vaccine, a minigene-based DNA vaccine, a ministring DNA (linear covalently closed DNA vector) vaccine, a closed-ended linear duplex DNA (CELiD or ceDNA) vaccine, a doggybone™ DNA vaccine, a dumbbell shaped DNA vaccine, or a minimalistic immunological-defmed gene expression (MIDGE)-vector DNA vaccine.

63. The composition of any one of claims 1-62, wherein: the promoter comprises a ubiquitous promoter, an inducible promoter, a tissue-specific promoter and / or a lineage-specific promoter, optionally the ubiquitous promoter is selected from the group consisting of a cytomegalovirus (CMV) immediate early promoter, a CMV promoter, a viral simian virus 40 (SV40) (e.g., early or late), a Moloney murine leukemia virus (MoMLV) LTR promoter, a Rous sarcoma virus (RSV) LTR, an RSV promoter, a herpes simplex virus(HSV) (thymidine kinase) promoter, H5, P7.5, and Pl l promoters from vaccinia virus, an elongation factor 1 -alpha (EFla) promoter, early growth response 1 (EGR1), ferritin H (FerH), ferritin L (FerL), Glyceraldehyde 3 -phosphate dehydrogenase (GAPDH), eukaryotic translation initiation factor 4A1 (EIF4A1), heat shock 70 kDa protein 5 (HSPA5), heat shock protein 90 kDa beta, member 1 (HSP90B1), heat shock protein 70 kDa (HSP70), P-kinesin (P-KIN), the human ROSA 26 locus, a Ubiquitin C promoter (UBC), a phosphoglycerate kinase-1 (PGK) promoter, 3 -phosphoglycerate kinase promoter, a cytomegalovirus enhancer, human P-actin (HBA) promoter, chicken P-actin (CBA) promoter, a CAG promoter, a CASI promoter, a CBH promoter, or any combination thereof; the polynucleotide(s) encoding components of the APC are operably linked to a tandem gene expression element, optionally the tandem gene expression element is an internal ribosomal entry site (IRES), foot-and-mouth disease virus 2A peptide (F2A), equine rhinitis A virus 2A peptide (E2A), porcine teschovirus 2A peptide (P2A) or Thosea asigna virus 2A peptide (T2A), or any combination thereof; and / or the polynucleotide(s) encoding components of the APC comprises a transcript stabilization element, optionally the transcript stabilization element comprises woodchuck hepatitis post-translational regulatory element (WPRE), bovine growth hormone polyadenylation (bGH-polyA) signal sequence, human growth hormone polyadenylation (hGH- polyA) signal sequence, or any combination thereof.

64. The composition of any one of claims 1-63, wherein the one or more polynucleotides comprise the nucleotide sequence of any one of SEQ ID NOs: 90-111 and 160- 183 or a sequence that is at least 80%, 85%, 90%, 95%, 98%, 99%, or 100% identical to any one of SEQ ID NOs: 90-111 and 160-183.

65. The composition of any one of claims 1-64, wherein the nucleic acid composition is or comprises mRNA, optionally the mRNA is formulated in a lipid nanoparticle (LNP).

66. The composition of any one of claims 1-65, wherein the mRNA comprises: a 5' untranslated region (UTR), a 3' UTR, and / or a cap; one or more modified nucleotides selected from the group consisting of pseudouridine, N-l-methyl-pseudouridine, 2-aminoadenosine, 2-thiothymidine, inosine, pyrrolo-pyrimidine, 3-methyl adenosine, 5-methylcytidine, C-5 propynyl-cytidine, C-5 propynyl-uridine, 2-aminoadenosine, C5-bromouridine, C5-fluorouridine, C5- iodouridine, C5-propynyl-uridine, C5-propynyl-cytidine, C5-methylcytidine, 2- aminoadenosine, 7-deazaadenosine, 7-deazaguanosine, 8-oxoadenosine, 8-oxoguanosine, 0(6)-methylguanine, and 2-thiocytidine; and / ora modified nucleotide in place of one or more uridines, optionally the modified nucleoside is selected from pseudouridine (y), N 1-methyl-pseudouridine (m IT), and 5- methyl-uridine (m5U).

67. The composition of any one of claims 59-66, wherein the LNP comprises: one or more of an ionizable cationic lipid, a non-cationic lipid, a sterol, and a PEG-modified lipid, optionally the non-cationic lipid is a neutral lipid;0.5-15 mol% PEG-modified lipid, 5-25 mol% non-cationic lipid, 25-55 mol% sterol, and 20-60 mol% ionizable cationic lipid; and / or40-55 mol% ionizable cationic lipid, 5-15 mol% neutral lipid, 35-45 mol% sterol, and 1-5 mol% PEG-modified lipid.

68. The composition of any one of claims 59-67, wherein the LNP comprises:47 mol% ionizable cationic lipid, 11.5 mol% neutral lipid, 38.5 mol% sterol, and 3.0 mol% PEG-modified lipid;48 mol% ionizable cationic lipid, 11 mol% neutral lipid, 38.5 mol% sterol, and 2.5 mol% PEG-modified lipid;49 mol% ionizable cationic lipid, 10.5 mol% neutral lipid, 38.5 mol% sterol, and 2.0 mol% PEG-modified lipid;50 mol% ionizable cationic lipid, 10 mol% neutral lipid, 38.5 mol% sterol, and 1.5 mol% PEG-modified lipid; or51 mol% ionizable cationic lipid, 9.5 mol% neutral lipid, 38.5 mol% sterol, and 1.0 mol% PEG-modified lipid.

69. The composition of any one of claims 66-68, wherein: the ionizable cationic lipid is heptadecan-9-yl 8 ((2 hydroxyethyl)(6 oxo 6- (undecyloxy)hexyl)amino)octanoate; the neutral lipid is 1,2 distearoyl sn glycero-3 phosphocholine (DSPC); the sterol is cholesterol; and / or the PEG-modified lipid is l-monomethoxypolyethyleneglycol-2,3- dimyristylglycerol with polyethylene glycol of average molecular weight 2000 (PEG2000 DMG).

70. The composition of any one of claims 1-69, wherein: the wt / wt ratio of lipid to mRNA is from about 1 : 100 to about 100: 1; and / or the composition is a lyophilized composition, optionally the lyophilized composition has a water content of less than about 10%.

71. The composition of any one of claims 1-70, wherein the composition is formulated or is to be formulated:as a liquid, a solid, or a combination thereof; for infusion; for injection; for intramuscular administration, intranasal administration, transdermal administration, aerosol delivery, nasal delivery, vaginal delivery, rectal delivery, buccal delivery, ocular delivery, local delivery, topical delivery, intraci sternal delivery, intraperitoneal delivery, oral delivery, intramuscular injection, intravenous injection, subcutaneous injection, intranodal injection, intratumoral injection, intraperitoneal injection, intradermal injection; and / or as particles, optionally the particles are iron oxide particles, liposomes, micelles, polymer complexes, cationic peptide nanoemulsions, virus-like particles (VLPs), lipid nanoparticles (LNP) and / or lipoplex (LPX) particles.

72. The composition of any one of claims 1-71, wherein the nucleic acid composition and the LNP-forming components are in separate vials.

73. The composition of any one of claims 1-72, wherein the composition is a pharmaceutical composition, wherein the pharmaceutical composition further comprises one or more pharmaceutically acceptable carriers, diluents and / or excipients.

74. The composition of any one of claims 1-73, further comprising instructions for use of the composition for: stimulating an immune response in a subject in need thereof; treating or preventing a disease or disorder in a subject in need thereof; and / or treating or preventing a cancer or an autoimmune disorder in a subject in need thereof.

75. A kit, comprising the composition of any one of claims 1-74.

76. A cell comprising the nucleic acid composition of any one of claims 1-74.

77. A method of stimulating an immune response in a subject in need thereof, comprising: administering to the subject a therapeutically effective amount of the composition of any one of claims 1-74 or the cell of claim 76, thereby stimulating an immune response in the subject.

78. A method of treating or preventing a disease or disorder in a subject in need thereof, comprising: administering to the subject a therapeutically effective amount of the composition of any one of claims 1-74 or the cell of claim 76, thereby treating or preventing the disease or disorder in the subj ect,optionally the disease or disorder is a cancer or an autoimmune disorder.

79. A method for treating or preventing a cancer or an autoimmune disorder in a subject in need thereof, comprising: administering to the subject a therapeutically effective amount of the composition of any one of claims 1-74 or the cell of claim 76, thereby treating or preventing a cancer or the autoimmune disorder in the subject.

80. The method of any one of claims 77-79, wherein immunogenic levels of the APC and / or APV are produced in serum of the subject at about 1 hour to about 6 months post administration of the composition.

81. The method of any one of claims 77-80, wherein a cytokine is released in the serum of the subject at about 1 hour to about 6 months post administration of the composition, optionally wherein the cytokine is JFN-y.

82. The method of any one of claims 77-80, wherein:T cells are activated in the subject at about 1 hour to about 6 months post administration of the composition; and / orT cells are induced to change from one type of T cell to another type of T cell, optionally the regulatory T cell type, in the subject at about 1 hour to about 6 months post administration of the composition.

83. The method of any one of claims 77-82, wherein the method comprises administering to the subject at least two doses of the composition, optionally: the second dose of the composition is administered to the subject at least 7 days after a first dose of the composition is administered to the subject; the method comprises administering to the subject at least 3, 4, 5, 6, 7, 8, 9, 10, 12, 15, 20, or 25, doses of the composition; and / or the method comprises administering a dose of the composion to the subject on a periodic basis, optionally at least once every hour, every two hours, every four hours, every six hours, every eight hours, every ten hours, every 12 hours, every 16 hours, every 24 hours, every 36 hours, every 48 hours, every 72 hours, every 96 hours, every 5 days, every week, every 2 weeks, every 3 weeks, every 4 weeks, every 5 weeks, every 6 weeks, every 8 weeks, every 10 weeks, every 12 weeks, every 15 weeks, every 20 weeks, every 25 weeks, every 30 weeks, every 40 weeks, every year, every 2 years, or every 3 years.

84. The method of any one of claims 77-83, wherein: the composition elicits an at least 10% higher T cell activation and / or cytokine release as compared to an approach comprising administration of a soluble version of thepresenting peptide; or the composition elicits an at least 10% lower T cell activation and / or cytokine release as compared to an approach comprising administration of a soluble version of the presenting peptide.

85. The method of any one of claims 77-84, wherein: administration of the composition elicits protective and long-lasting immunity against the disease or disorder associated with the presenting peptide thereof; or administration of the composition elicits protective and long-lasting immunosuppression, optionally associated with the presenting peptide.

86. The method of any one of claims 77-85, wherein: an at least as low dose of the composition is needed to generate a comparable immune response as compared to an approach comprising administration of a soluble version of the presenting peptide; or an at least as low dose of the composition is needed to generate a comparable immunosuppression as compared to an approach comprising administration of a soluble version of the presenting peptide.

87. The method of any one of claims 77-86, wherein following administration of the composition, the composition induces an at least as potent T cell activation and / or cytokine release against the presenting peptide or variants thereof as compared to an approach comprising administration of a soluble version of the presenting peptide, optionally the composition comprises a population of APVs; or the composition induces an at least as potent immunosuppression, optionally against the presenting peptide or variants thereof, as compared to an approach comprising administration of a soluble version of the presenting peptide, optionally the composition comprises a population of APVs.

88. The method of any one of claims 77-87, wherein the subject: is a human subject; is a newborn or infant of an age of not more than 3 years, of not more than 2 years, of not more than 1.5 years, of not more than 1 year (12 months), of not more than 9 months, 6 months or 3 months, or is between 6 months and 2 years; is immunocompromised, has a pulmonary disease, and / or is 65 years of age or older; has a cancer, optionally melanoma, ovarian cancer, esophageal cancer, lung cancer, hepatocellular cancer, prostate cancer, or breast cancer; and / or has an underlying comorbid condition, optionally selected from heart disease, diabetes,and lung disease.

89. The method of any one of claims 77-88, wherein the composition is administered in an effective amount to: elicit a robust CD4 and / or CD8 T cell response against the presenting peptide in the subject; and / or elicit a cytokine release against the presenting peptide in the subject, optionally IFN-y release.

90. The method of any one of claims 77-89, wherein the composition is: (i) coadministered with an adjuvant; or (ii) not co-administered with an adjuvant.

91. The method of any one of claims 77-90, wherein the disease or disorder is a blood disease, an immune disease, a neurological disease or disorder, a cancer, an infectious disease, a genetic disease, a disorder caused by aberrant mtDNA, a metabolic disease, a disorder caused by aberrant cell cycle, a disorder caused by aberrant angiogenesis, a disorder cause by aberrant DNA damage repair, or any combination thereof, optionally a solid tumor.

92. The method of any one of claims 77-91, wherein: the disease is associated with expression of a tumor-associated antigen, optionally the disease associated with expression of a tumor antigen-associated is selected from the group consisting of a proliferative disease, a precancerous condition, a cancer, and a non-cancer related indication associated with expression of the tumor antigen; the cancer is selected from the group consisting of colon cancer, rectal cancer, renal-cell carcinoma, liver cancer, non-small cell carcinoma of the lung, cancer of the small intestine, cancer of the esophagus, melanoma, bone cancer, pancreatic cancer, skin cancer, cancer of the head or neck, cutaneous or intraocular malignant melanoma, uterine cancer, ovarian cancer, rectal cancer, cancer of the anal region, stomach cancer, testicular cancer, uterine cancer, carcinoma of the fallopian tubes, carcinoma of the endometrium, carcinoma of the cervix, carcinoma of the vagina, carcinoma of the vulva, Hodgkin's Disease, non-Hodgkin lymphoma, cancer of the endocrine system, cancer of the thyroid gland, cancer of the parathyroid gland, cancer of the adrenal gland, sarcoma of soft tissue, cancer of the urethra, cancer of the penis, solid tumors of childhood, cancer of the bladder, cancer of the kidney or ureter, carcinoma of the renal pelvis, neoplasm of the central nervous system (CNS), primary CNS lymphoma, tumor angiogenesis, spinal axis tumor, brain stem glioma, pituitary adenoma, Kaposi's sarcoma, epidermoid cancer, squamous cell cancer, T-cell lymphoma, environmentally induced cancers, combinations of said cancers, and metastatic lesions of said cancers; and / or the cancer is a hematologic cancer chosen from one or more of chronic lymphocytic leukemia (CLL), acute leukemias, acute lymphoid leukemia (ALL), B-cell acute lymphoidleukemia (B-ALL), T-cell acute lymphoid leukemia (T-ALL), chronic myelogenous leukemia (CML), B cell prolymphocytic leukemia, blastic plasmacytoid dendritic cell neoplasm, Burkitt's lymphoma, diffuse large B cell lymphoma, follicular lymphoma, hairy cell leukemia, small cell- or a large cell-follicular lymphoma, malignant lymphoproliferative conditions, MALT lymphoma, mantle cell lymphoma, marginal zone lymphoma, multiple myeloma, myelodysplasia and myelodysplastic syndrome, non-Hodgkin's lymphoma, Hodgkin's lymphoma, plasmablastic lymphoma, plasmacytoid dendritic cell neoplasm, Waldenstrom macroglobulinemia, or pre-leukemia.

93. The method of any one of claims 77-92, wherein administering comprises aerosol delivery, nasal delivery, vaginal delivery, rectal delivery, buccal delivery, ocular delivery, local delivery, topical delivery, intracistemal delivery, intraperitoneal delivery, oral delivery, intramuscular injection, intravenous injection, infusion, subcutaneous injection, intranodal injection, intratumoral injection, intraperitoneal injection, intradermal injection, or any combination thereof, optionally the composition is administered intramuscularly, further optionally into a deltoid region of an arm.

94. A method of modulating an immune cell, comprising: contacting the immune cell with the composition of any one of claims 1-74.

95. The method of claim 94, wherein modulating comprising activating, regulating, stimulating, and / or suppressing.

96. A method of isolating an immune cell of interest, comprising: contacting a population of cells suspected of comprising of an immune cell of interest with the composition of any one of claims 1-74.

97. The method of any one of claims 94-96, wherein the contacting step: is performed in vitro is performed in a compartment loaded with the composition of any one of claims 1-74, optionally a nanovial; and / or is performed in a cavity of a particle, optionally a nanovial.

98. The method of claim 97, wherein: the particle comprises at least one opening; the particle comprises a single opening; the particle is composed of hydrogel; a longest dimensional length of the particle is less than about 100 micrometers; the APVs are disposed on the surface of the cavity; the APVs are disposed on the surface of the cavity through a binding moiety, optionally the binding moiety comprises an antibody or fragment thereof capable ofspecifically binding the APV, optionally capable of specifically binding to one or more selected from the group consisting of CD274, CD83, CD80, CD54, MHC, the presenting peptide, the APC-assembly domain, and a fragment thereof; and / or one or more capture agent(s) are disposed on the surface of the cavity, optionally the capture agent(s) comprise an antibody or fragment thereof capable of specifically binding to a cytokine, optionally to one or more selected from the group consisting of IL- 2, TNF-a, IFN- y, and fragments thereof.

99. The method of any one of claims 94-98, wherein the immune cell comprises a B cell, a plasmablast, a plasma cell, a T cell, or an NK cell; further comprising isolating immune cell(s) of interest; wherein activation of the immune cell is at least about 1.1 -fold higher as compared to a method of activating the immune cell using the antigen presentation polypeptide and the presenting peptide without forming the APV; wherein level of cytokine secretion is at least about 1.1 -fold higher as compared to a method of activating the immune cell using the antigen presentation polypeptide(s) and the presenting peptide without forming the APV, optionally the cytokine is IFN- y; and / or wherein the presence of the supplemental polypeptide(s) increases the activation of the immune cell and / or the level of cytokine secretion by at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80% or 90%.

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