Lipid gb3 as adjuvant for vaccination

Abstract

Provided herein are uses for an immunostimulatory compound for stimulating an immune response when administered either alone or as an adjuvant in a vaccine. Also provided herein are kits, compositions, and methods of administration for the compound described.

Description

[0001]LIPID GB3 AS ADJUVANT FOR VACCINATION RELATED APPLICATION This application claims the benefit under 35 U.S.C. § 119(e) of U.S. Provisional Application No.63 / 452,962, filed March 17, 2023, entitled “LIPID GB3 AS ADJUVANT FOR VACCINATION”, the entire contents of which are incorporated herein by reference. REFERENCE TO AN ELECTRONIC SEQUENCE LISTING The contents of the electronic sequence listing (C123370218WO00-SEQ-VLJ.xml; Size: 13,406 bytes; and Date of Creation: March 12, 2024) is herein incorporated by reference in its entirety. BACKGROUND The immune response is crucial to the health of many species, including humans, by playing a key role in defense against microbial pathogens and cancers. Pathogens, such as influenza virus, can evade the host immune response because they have surface antigens that display a high frequency of point mutations (antigenic drift). Certain molecules can modulate the immune system and are of particular interest as they may be used in vaccination strategies aimed at broader humoral responses. The molecules may be administered to either treat or protect against disease. SUMMARY Provided herein are compositions and methods for enhancing an immune response in a subject by administering an effective amount of globotriaosylceramide (Gb3) or an analog thereof. Therapeutic and / or prophylactic uses of Gb3 or an analog thereof are described. In some embodiments, Gb3 or an analog thereof is used alone to stimulate immunity in a subject. In some embodiments, the compound is used as an adjuvant in compositions including vaccines for diseases, e.g., proliferative disease, inflammatory disease, autoimmune disease, infectious disease, or chronic disease, in a subject in need thereof. Adjuvants can enhance, prolong, and modulate immune responses to vaccinal antigens to maximize protective immunity. In some embodiments, using Gb3 or an analog thereof as a vaccine adjuvant enables effective immunization in vulnerable populations (e.g., neonates, the elderly, or immunocompromised individuals). In some embodiments, the compound enhances adaptive immune responses. Accordingly, some aspects of the present disclosure provide methods of enhancing an immune response in a subject in need thereof, the method comprising administering to the subject an effective amount of a compound of Gb3 or an analog thereof. In some embodiments, the subject has or is at risk of developing a disease. In some embodiments, the disease is caused by a bacterium, a virus, a parasite, or a fungi. In some embodiments, the disease is a disease caused by a virus. In some embodiments, the virus is an adenovirus, a coronavirus, polio virus, dengue virus, Ebola virus, a herpes viruses such as herpes simplex virus, cytomegalovirus and varicella-zoster, measles, mumps, rubella, hepatitis A virus, hepatitis B virus, hepatitis C virus, human papilloma virus, influenza virus, rabies, Japanese encephalitis, rotavirus, human immunodeficiency virus (HIV), respiratory syncytial virus (RSV), smallpox, yellow fever, or Zika virus. In some embodiments, the virus is an influenza virus. In some embodiments, the virus is a human influenza A or a human influenza B virus. In some embodiments, the virus is from a group 1 or group 2 influenza A virus. In some embodiments, the virus is a beta coronavirus. In some embodiments, the virus is MERS-CoV, SARS-CoV-1, or SARS-CoV-2. In some embodiments, the disease is a cancer. In some embodiments, the cancer is a hematological cancer, lung cancer, breast cancer, brain cancer, gastrointestinal cancer, liver cancer, kidney cancer, bladder cancer, pancreatic cancer, ovarian cancer, testicular cancer, prostate cancer, endometrial cancer, muscle cancer, bone cancer, neuroendocrine cancer, connective tissue cancer, head and neck cancer, or skin cancer. In some embodiments, the subject is a human. In some embodiments, the subject is a human neonate, infant, adult, or an elderly human. In some embodiments, the subject is a companion animal or a research animal. In some embodiments, the immune response comprises a humoral response. In some embodiments, the immune response comprises binding of Gb3 or an analog thereof to Cluster of Differentiation 19 (CD19). In some embodiments, the immune response comprises activation of the PI3K-Akt-mTOR pathway. In some embodiments, the immune response comprises a reduction of transcription mediated by Forkhead box protein O1 (FOXO-1). In some embodiments, the immune response comprises enhanced B cell receptor (BCR) signaling. In some embodiments, the administration induces the expansion of germinal center B cells in the subject. In some embodiments, the administration induces the production of an antibody in the subject. In some embodiments, the antibody is an immunoglobulin G (IgG). In some embodiments, the IgG is a subclass 1 IgG (IgG1) or a subclass 2 IgG (IgG2). In some embodiments, the IgG is a subclass 2c IgG (IgG2c). Some aspects of the present disclosure provide methods and compositions of enhancing the immune response in a subject by administering an effective amount of Gb3 or an analog thereof. In some embodiments, administering an effective amount of Gb3 or an analog thereof further comprises administering to the subject an antigen. In some embodiments, the antigen is administered before, after, or concurrently with Gb3 or an analog thereof. In some embodiments, the administration induces the production of an antibody in the subject that is specific for the antigen. In some embodiments, the antigen is an antigen from a bacterium, a virus, a parasite, or a fungus. In some embodiments, the antibody is an antibody that neutralizes the bacterium, virus, parasite, or fungus. In some embodiments, the administration confers heterotypic protection in the subject. In some embodiments, the antigen is an antigen from a cancer. In some embodiments, the antibody is an antibody that promotes immunity against the cancer. In some embodiments, the administration occurs intramuscularly, intradermally, orally, intravenously, topically, intranasally, or sublingually. In some embodiments, the administration occurs more than once. In some embodiments, the administration treats a disease in the subject. In some embodiments, the administration prevents a disease in the subject. In some embodiments, the disease is caused by a bacterium, a virus, a parasite, or a fungi. In some embodiments, the disease is a cancer. Some aspects of the present disclosure provide compositions comprising an antigen and Gb3 or an analog thereof. In some embodiments, the antigen comprises a protein or polypeptide. In some embodiments, the antigen comprises a nucleic acid encoding a protein or a polypeptide. In some embodiments, the nucleic acid is DNA or RNA. In some embodiments, the antigen is a viral antigen. In some embodiments, the virus is an adenovirus, a coronavirus, an enterovirus such as polio virus, dengue virus, Ebola virus, a herpes viruses such as herpes simplex virus, cytomegalovirus and varicella-zoster, measles, mumps, rubella, hepatitis A virus, hepatitis B virus, hepatitis C virus, human papilloma virus, influenza virus, rabies, Japanese encephalitis, rotavirus, human immunodeficiency virus (HIV), respiratory syncytial virus (RSV), smallpox, yellow fever, or Zika virus. In some embodiments, the antigen is an antigen from an influenza virus. In some embodiments, the antigen is an antigen from a human influenza A or a human influenza B virus. In some embodiments, the antigen is an antigen from a group 1 or group 2 influenza A virus. In some embodiments, the antigen comprises a group 1 or group 2 influenza A hemagglutinin (HA) protein, or an immunogenic fragment thereof. In some embodiments, the antigen is from a beta coronavirus. In some embodiments, the antigen is an antigen from MERS-CoV, SARS-CoV-1, or SARS-CoV-2. In some embodiments, the antigen comprises a MERS-CoV, SARS-CoV-1, or SARS-CoV-2 spike protein, or an immunogenic fragment thereof. In some embodiments, the antigen comprises a viral particle, a killed or inactivated virus, or a live attenuated virus. In some embodiments, the virus is an influenza virus. In some embodiments, the virus is a human influenza A or a human influenza B virus. In some embodiments, the virus is a group 1 or group 2 influenza A virus. In some embodiments, the virus is a beta coronavirus. In some embodiments, the virus is MERS-CoV, SARS-CoV-1, or SARS- CoV-2. In some embodiments, the composition of the present disclosure further comprises a pharmaceutically acceptable carrier. In some embodiments, wherein the composition is a vaccine composition. In some embodiments, the Gb3 or an analog thereof acts as an adjuvant. In some embodiments, the vaccine composition further comprises a second adjuvant. In some embodiments, the second adjuvant is alum or an emulsion. In some embodiments, the vaccine composition is a subunit vaccine, an attenuated vaccine, or a conjugate vaccine. Some aspects of the present disclosure provide methods of enhancing an immune response to an antigen in a subject in need thereof, the method comprising administering to the subject an effective amount of the composition of the present disclosure. In some embodiments, the antigen is a viral antigen. In some embodiments, the subject is infected with a virus. In some embodiments, the subject is at risk for infection by a virus. In some embodiments, the virus is an adenovirus, a coronavirus, an enterovirus such as polio virus, dengue virus, Ebola virus, a herpes viruses such as herpes simplex virus, cytomegalovirus and varicella- zoster, measles, mumps, rubella, hepatitis A virus, hepatitis B virus, hepatitis C virus, human papilloma virus, influenza virus, rabies, Japanese encephalitis, rotavirus, human immunodeficiency virus (HIV), respiratory syncytial virus (RSV), smallpox, yellow fever, dengue virus, or Zika virus. In some embodiments, the virus is an influenza virus. In some embodiments, the virus is a human influenza A or a human influenza B virus. In some embodiments, the virus is a group 1 or group 2 influenza A virus. In some embodiments, the virus is a beta coronavirus. In some embodiments, the virus is MERS-CoV, SARS-CoV-1, or SARS-CoV-2. In some embodiments, the subject is a human. In some embodiments, the subject is a human adult or an elderly human. In some embodiments, the subject is a companion animal or a research animal. In some embodiments, the immune response comprises a humoral response. In some embodiments, the immune response comprises binding of Gb3 or an analog thereof to Cluster of Differentiation 19 (CD19). In some embodiments, the immune response comprises activation of the PI3K-Akt-mTOR pathway. In some embodiments, the immune response comprises a reduction of transcription mediated by Forkhead box protein O1 (FOXO-1). In some embodiments, the immune response comprises enhanced B cell receptor (BCR) signaling. In some embodiments, administration of the composition induces the expansion of germinal center B cells in the subject. In some embodiments, administration of the composition induces the production of an antibody in the subject. In some embodiments, the antibody is specific for the antigen. In some embodiments, the antibody is an immunoglobulin G (IgG). In some embodiments, the IgG is a subclass 1 IgG (IgG1) or a subclass 2 IgG (IgG2). In some embodiments, the IgG is a subclass 2c IgG (IgG2c). In some embodiments, the antibody is a neutralizing antibody. In some embodiments, the antibody inhibits binding between the antigen and an antigen-binding receptor of the subject. In some embodiments, the antigen is a group 1 or group 2 influenza A hemagglutinin (HA) protein and the antigen-binding receptor is a glycoprotein or glycolipid of the subject that is modified by sialic acid. In some embodiments, the antigen is a MERS-CoV, SARS-CoV-1, or a SARS-CoV-2 spike protein and the antigen-binding receptor is an angiotensin converting enzyme 2 (ACE2) protein of the subject. In some embodiments, administration of the composition confers heterotypic protection in the subject. In some embodiments, administration of the composition enhances heterotypic protection in the subject, compared with administration of the antigen alone. In some embodiments, administration of the composition occurs intramuscularly, intradermally, orally, intravenously, topically, intranasally, or sublingually. In some embodiments, administration of the composition treats a disease in the subject. In some embodiments, administration of the composition prevents a disease in the subject. In some embodiments, the disease is a disease caused by a virus. In some embodiments, the disease is influenza, Middle East respiratory syndrome (MERS), sudden acute respiratory syndrome (SARS), or coronavirus disease 2019 (COVID-19). BRIEF DESCRIPTION OF DRAWINGS The accompanying drawings are not intended to be drawn to scale. In the drawings, each identical or nearly identical component that is illustrated in various figures is represented by a like numeral. For purposes of clarity, not every component may be labeled in every drawing. In the drawings: FIGs.1A-1J show Gb3 promotes the formation of germinal centers and antibody maturation. FIG.1A is a diagrammatic representation of the experimental set-up. WT, Gla-KO, or A4galt-KO mice were immunized with NP-OVA adsorbed on alum. FIG.1B shows confocal microscopy of frozen sections from the spleen on day 10 post immunization. IgD (naive B cells), CD3 (T cells), and GL7 (GC B cells). FIG.1C shows representative FACS plots and percentage of GC B cells and plasma cells in the spleen on day 10 post NP-OVA immunization. Each dot represents one mouse (7 or 8 mice per group), and the experiment was repeated three times. FIG.1D shows the serological analysis of immunoglobulin concentrations of indicated isotypes based on end-point titers using ELISA on day 13 post immunization. Experiment was repeated three times with 8 mice per group. FIG.1E shows avidity of NP-OVA-specific IgG was measured by ELISA and expressed as the ratio between the end-point titer values obtained with or without sodium thiocyanate treatment (2 M) on day 13 after immunization. Experiment was repeated twice with 8 mice per group. FIG.1F is an antibody affinity assay. Serum was analyzed by ELISA and high- affinity antibodies were measured as a ratio of antibodies binding to BSA conjugated with NP4 (low valency) to NP30 (high valency). Experiment was repeated twice with 8 mice per group. FIG.1G shows pie charts representing the distribution of productive VH1-72 clonotypes in the GCs of each mouse (3 mice in WT and Gla-KO groups and 4 in A4galt-KO). Colors indicate the dominant clonotypes found among three different mouse genotypes. FIGs.1H-1I show the SHM profile of VH1-72 segments of the dominant clonotypes and intrinsic mutation pattern. Data are plotted as the mutation rate at each nucleotide with representative junctional structure of each IgH clonotype shown at the top, while bar graphs depict individual mice for the frequency of the NP- specific high-affinity mutation (W33L). FIG.1J shows violin plots of VH mutation per base for all clonotypes (left graph) as well as for singleton (found once) and expanded (found at least twice) clones (right graph) from the three genotypes. Each dot in left graph depicts a single clone, while in right graph, each dot represents a single mouse. p-values in graph c, d, e, f, and h were calculated by using one-way ANOVA, while in graph i student’s t-test was used. FIGs.2A-2K show Gb3 binds to CD19 and controls BCR downstream signaling. FIG.2A is a diagrammatic representation of the experimental set-up. WT, Gla-KO, or A4galt-KO mice were immunized with NP-OVA adsorbed on alum. FIG.2B shows representative FACS plots and percentages of centroblasts (CB) and centrocytes (CC) in the spleen on day 10 post immunization. Each dot represents one mouse (7 or 8 mice per group), and the experiment was repeated three times. FIG.2C is an immunoblot showing BCR and CD19 downstream signaling molecules and transcription factors. Anti-BCR antibodies (F(ab)2) were used to stimulate FACS-sorted GC B cells for 2 or 5 minutes. U = unstimulated. FIG.2D shows proximity ligation assay (PLA) performed on GC B cells to probe for vicinity between BCR and CD19, and CD19 and PI3K (bottom panel; U = unstimulated). To test PI3K recruitment, FACS-sorted GC B cells were stimulated with anti-BCR antibodies (F(ab)2) and were probed with specific antibodies. In all panels, experiments were repeated at least three times, and PLA signal on more than 30 cells in different fields was calculated for statistical analysis. FIG.2E shows PLA performed on FACS- sorted GC B cells to probe for proximity between CD19 and Gb3. PLA signal was captured by confocal microscopy, and images were processed and analyzed by Image J software. Experiment was repeated at least three times, and PLA signal on more than 30 cells in different fields was calculated for statistical analysis. FIG.2F show Structures of different lipids and Gb3 analog used in the study. FIG.2G shows phospho-flow was used to examine the effect of lipid reconstitution on Akt phosphorylation in GC B cells from A4galt-KO mice. Pictorial representation of experimental set-up (top panel) and representative histogram overlay and mean fluorescence intensity (MFI) of pAkt staining in GC B cells cultured with different lipids (bottom panel). FACS-sorted GC B cells from A4galt-KO mice were seeded with a complex of lipid and BSA for 2 hours at 37°C (see methods), and Akt phosphorylation was quantified after stimulation of GC B cells with F(ab)2. FIG.2H shows a protein lipid overlay assay to assess the CD19 binding capability of different lipids. Lipids were deposited on a PVDF membrane and their binding to CD19 (containing histidine) was tested by using anti-His-HRP secondary antibody using chemiluminescence. FIG.2I shows isothermal titration calorimetry (ITC) to measure the binding between Gb3 and CD19. CD19 and the Gb3 analog were dissolved in PBS, and thermodynamic analysis of their binding was carried out at 25°C on a MicroCal ITC 200 instrument. Top panel: x- axis depicts time, and y-axis represents rate of heat release (μcal / sec). Bottom panel: x-axis represents molar ratio between CD19 and Gb3-analog, and y-axis depicts change in enthalpy. FIG.2J depicts site-directed mutagenesis of CD19 and putative Gb3 binding sites. CD19-negative A20 B cells were transfected with WT or mutant CD19 (M1: F122A, M2: W124A, M3: G198T), and Gb3 interaction with CD19 was quantified by PLA using confocal microscopy. Images were processed and analyzed by Image J software. PLA signal on more than 30 cells in different fields was calculated for statistical analysis. FIG.2K depicts a mechanistic scheme of the effect of Gb3 on the CD19 downstream signaling pathway. The p-values in all graphs were calculated by one- way ANOVA. FIGs.3A-3J show Gb3 facilitates the selection of subdominant epitopes. FIG.3A depicts a schematic representation of the experimental set-up. WT, Gla-KO, or A4galt-KO mice were immunized with NP-OVA adsorbed on alum. FIG.3B is rarefaction curves showing the clonotype diversity for the three genotypes. The solid dark curves and light shades show the mean and SEM (standard error of the mean) of the calculated diversity for each genotype (N=3 for WT and Gla- KO, and N=4 for A4galt-KO). Welch's t-tests were used to test the difference in diversity across different genotypes at the number of reads 1000, 3000, and 5000 (n=3 for WT and Gla-KO, n=4 for A4galt-KO). FIG.3C shows a representative FACS plots and percentages of OVA-FITC+and NP-PE+GC B cells in the spleen on day 16 post immunization. Each dot represents one mouse (4 mice per group), and the experiment was repeated at least three times. FIG.3D shows histogram overlays depicting the MHC-II expression on naive B cells, centroblasts, and centrocytes as quantified by flow cytometry. Each dot represents a single mouse with 5 mice per group. Experiment was repeated at least three times. FIG.3E depicts an experimental set-up of NP-OVA immunization and OT-II T cell transfer (top panel). Representative plots and percentages of OT-II Tfh cells in the spleen on day 10 post immunization as quantified by flow cytometry (bottom panel). Dots in bar graphs represent individual mice (5-6 mice per group) and the experiment was at least repeated two times. FIG.3F depicts an experimental set-up of NP-OVA immunization using different mouse models. FIG.3G shows MHC-II expression on GC B cells on day 16 after immunization. Data is plotted as mean fluorescence intensity (MFI) as quantified by flow cytometry (n=5 mice per group). FIG.3H shows representative FACS plots and percentages of OVA-FITC+and NP-PE+GC B cells in the spleen on day 16 post immunization. The experiment was repeated three times (5 mice per group). FIG.3I-3J show the serological analysis of indicated antigen-specific immunoglobulin concentrations as detected by ELISA on day 16 post immunization. The experiment was repeated three times (5 mice per group). The p-values in graphs c to k were calculated by one-way ANOVA. FIGs.4A-4O show exogenous Gb3 broadens the antibody response in influenza infection. FIG. 4A is an experimental set-up depicting animal groups, timeline of immunization, and sample collection schedule for rHA immunization. FIGs.4B-4D show serological analysis of immunoglobulin concentrations of indicated isotypes specific for rHA was performed by ELISA. Graphs represent mean±SD with 5 mice in each group. The experiment was repeated three times. FIG.4E shows avidity of rHA-specific IgG was measured by ELISA and expressed as the ratio between the end-point titer values obtained with or without sodium thiocyanate treatment (2 M). Graphs represent mean±SD with 5 mice in each group. FIG.4F shows serum concentrations of anti-rHA stalk immunoglobulins were detected by ELISA. Graphs represent mean±SD with 5 mice in each group. FIG.4G shows enzyme-linked immunosorbent spot (ELISPOT) showing IgG1- and IgG2c-producing plasma cells recognizing rHA on day 60 post immunization. Dots in bar graphs represent individual mice (n=4 for each group), and the experiment was repeated three times. FIG.4H shows serum concentrations of immunoglobulins against rHA of heterotypic influenza strains were detected by ELISA. Dots in bar graphs represent individual mice (n=6 for each group), and the experiment was repeated three times. FIGs.4I-4J show H1N1 or H3N2 neutralizing antibody (NA) immunoglobulin titers in serum on day 28 post rHA immunization. Serum concentrations of immunoglobulins against rHA of heterotypic influenza strains were detected by ELISA. Dots in bar graphs represent individual mice (n=5 for each group), and the experiment was repeated at least three times. FIG.4K is an experimental set-up depicting immunization and infection regimen. Immunized mice were challenged intranasally with 103PFU of either H1N1 or H3N2 on day 28. PFU = plaque forming units; i.n. = intranasal. (l, m) Weight loss curve following H1N1 (PR8) or H3N2 (HK68, X-31) infection. Data shown in graphs represent three independent experiments with 5 mice in each group, and the experiment was repeated twice. FIGs.4N-4O show H1N1 or H3N2 PFUs in lungs on day 5 post infection. Dots in bar graphs represent individual mice, and the experiment was repeated twice. The p-values were calculated by one-way ANOVA, and in graph l and m, p-values of ≤0.05 and ≤0.01 were marked with * and **, respectively. FIGs.5A-5I show the expression pattern of Gb3 in cell lineages, modulation in enzyme-deficient mouse models, and differentiation of Tfh and plasma cells. FIG.5A shows enzymatic pathways of the synthesis and degradation of Gb3. FIG.5B depicts the experimental set-up. WT mice were immunized with NP-OVA adsorbed on alum, and spleens were harvested 10 days later. FIG.5C shows the gating strategy used to identify splenic B cell subsets by flow cytometry. FIG.5D show representative FACS plots and percentages of Gb3-positive B cells on day 10 post NP-OVA immunization. Each dot represents one mouse (5 mice per group), and the experiment was repeated three times. FIG.5E show representative histogram overlays depicting Gb3 expression on splenic myeloid and lymphocyte subsets on day 10 post immunization quantified by flow cytometry. Each dot represents a single mouse (n=4), and the experiment was repeated twice. FIG.5F is a schematic representation of the experimental set-up. WT, Gla-KO, or A4galt-KO mice were immunized with NP-OVA adsorbed on alum. FIG.5G shows representative FACS plots and percentages of Gb3-positive GC B cells on day 10 post NP-OVA immunization. Each dot represents one mouse (6 mice per group), and the experiment was repeated twice. FIG.5H shows quantification of plasma cells secreting NP-specific total IgG and NP4-specific high- affinity IgG by ELISPOT. Each dot represents one mouse (3 mice per group), and the experiment was repeated at least three times. FIG.5I shows representative FACS plots and percentages of Tfh cells in the spleen on day 10 post NP-OVA immunization were quantified by flow cytometry. Each dot represents one mouse (5 mice per group), and the experiment was repeated at least three times. The p-values in all the data sets were calculated by one-way ANOVA. FIG.6 shows Gb3 abundance does not affect VH usage in germinal centers. Shown are the VHrepertoire of productive V(D)J junctions in splenic GC B cells versus naive B cells in WT, Gla- KO, or A4galt-KO mice immunized with NP-OVA. The data are plotted as mean ± SEM (N=3 for WT and Gla-KO, and N=4 for A4galt-KO). VH segments are each ordered linearly based on their chromosome coordinates with respect to relative proximity to the D segments. Student’s t-test was performed to compare BCR usage between GC and naïve B cells, and p-values of ≤0.05 were marked with *. FIGs.7A-7F show Gb3 abundance on GC B cells provides competitive advantage during GC reaction in a B cell-intrinsic manner. FIG.7A is an experimental scheme depicting generation of congenic BM chimeric mice. WT.SJL recipient mice were lethally irradiated and intravenously transferred with WT CD45.1 (SJL) and CD45.2 (C57BL / 6, Gla-KO, or A4galt-KO) BM cells at a ratio of 2:1. FIG.7B shows representative FACS plots and relative percentages of CD45.1+and CD45.2+GC B cells in the spleen on day 10 post NP-OVA immunization. Each dot represents one mouse (5 mice per group), and the experiment was repeated twice. FIG.7C shows representative FACS plots and relative IgG2c-positive CD45.1+and CD45.2+GC B cells in the spleen on day 10 post NP-OVA immunization. Each dot represents one mouse (5 mice per group), and the experiment was repeated twice. FIG.7D is an experimental set-up showing adoptive B cell transfer and NP-OVA immunization strategy. muMT-KO mice were injected with 1 × 107B cells intravenously and were immunized on day 7 with NP-OVA adsorbed on alum. FIG.7E shows representative FACS plots and percentages of GC B cells in the spleen. Experiment was repeated twice (n=4 mice per group). FIG.7F shows the serological analysis of immunoglobulin concentrations of indicated isotypes as detected by end-point titer measurements using ELISA on day 21 after immunization. Experiment was repeated twice with 4-5 mice per group. The p-values were calculated by one-way ANOVA in all graphs. FIGs.8A-8D show binding competition between CD19 and STxB to Gb3, putative Gb3 binding site, and generation of CD19 mutants. FIG.8A shows a competitive ELISA used to quantify the relative binding affinities of CD19 and STxB for Gb3. Hydrophobic binding plates were coated with Gb3, followed by incubation with either CD19 or STxB, prior to sequential incubation with primary antibodies to detect CD19 or STxB, respectively. To assess binding competition, Gb3- coated plates were additionally pre-incubated with either 1 mM CD19 (detection of STxB) or STxB (detection of CD19). FIG.8B shows sequence similarity between STxB, human CD19, and mouse CD19 ectodomain. M1 (F122A), M2 (W124A), and M3 (G198T) are the selected amino acid residues for site-directed mutagenesis. FIG.8C depicts a representative gating strategy for FACS-sorting of CD19-negative A20 B cells, and histogram overlays depicting Gb3 expression on CD19-positive and CD19-negative A20 B cells. FIG.8D is pictorial representation generating site-directed mutations in CD19. CD19-negative A20 B cells were transfected with WT or mutant CD19 plasmids and subsequently tested for productive CD19 expression. Representative FACS plots and relative percentages show CD19-expressing A20 B cells after transfection with WT or mutant CD19. A20 B cells were matched for the same level of CD19 expression (indicated by boxes labeled “A”), prior to FACS-sorting and subsequent PLA assay. FIGs.9A-9H show Gb3-mediated IgG2c isotype switch is IFNAR1-dependent. FIG.9A is an experimental set-up depicting immunization and anti-IFNAR1 antibody treatment. Mice were immunized with NP-OVA adsorbed on alum, and blocking antibodies were administered on day 6 and 8 after immunization. FIG.9B shows representative FACS plots and frequencies of GC B cells in the spleen on day 10 post immunization. Each dot represents one mouse (4 mice per group), and the experiment was repeated at least three times. FIG.9C shows anti-NP-OVA immunoglobulin titers of indicated isotypes in the serum were measured by ELISA. Each dot represents one mouse (4 mice per group), and the experiment was repeated at least three times. FIG.9D is an experimental set-up depicting NP-OVA immunization of Gla- and Ifnar-deficient mice. FIG.9E shows representative FACS plots and percentages of IgG1+and IgG2c+GC B cells in the spleen were quantified by flow cytometry. Dots in bar graphs depict individual mice (n=5 mice per group). FIG.9F shows the ratio of IgG2c to IgG1 titers in the serum. Bar graph shows the ratio of endpoint titers for IgG2c and IgG1, and each point in the graph depicts an individual mouse (n=5 mice per group). FIG.9G depicts PLA performed on GC B cells to probe for proximity between Gb3 and IFNAR1. Images were captured by confocal microscopy. Experiments were repeated at least three times, and PLA signal on more than 30 cells in different fields was calculated for statistical analysis. FIG.9H is an immunoblot showing IFNAR1 downstream signaling. IFNα was used to stimulate B cells for 5 or 15 minutes. U = unstimulated. The p-values in graph b and g were calculated by one-way ANOVA, while two-sided Mann- Whitney U test was used for analysis in FIGs.9C, 9E, and 9F. FIGs.10A-10I show Gb3 facilitates B cell responses to subdominant epitopes. FIG.10A is an experimental set-up depicting animal groups, timeline of immunization, and sample collection schedule. FIG.10B shows Serological analysis of immunoglobulin concentrations of indicated isotypes specific for OVA was performed by ELISA. Graphs represent mean ± SD with 5 mice in each group. The experiment was repeated twice. FIG.10C shows IgG-producing plasma cells recognizing OVA in the bone marrow on day 60 after immunization using ELISPOT. The experiment was repeated three times (3 mice per group). FIG.10D is an experimental set-up showing adoptive B cell transfer and NP-OVA immunization strategy. muMT-KO mice were injected with 1 × 107B cells intravenously and immunized on day 7 with NP-OVA adsorbed on alum. FIG.10E shows representative FACS plots and percentages of OVA-FITC binding by GC B cells in the spleen. Each dot represents one mouse (4 mice per group), and the experiment was repeated at least three times. FIG.10F shows the concentration of anti-OVA IgG titers in the serum. Experiment was repeated at least three times (n=4-5). FIG.10G is an experimental set-up of NP-OVA immunization in MHC-II-haplosufficient mouse strains. FIG.10H shows representative FACS plots and percentage of GC B cells in the spleen on day 10 post NP-OVA immunization. The experiment was repeated three times (5 mice per group). FIG.10I shows representative FACS plots and percentages of Tfh cells in the spleen on day 16 post NP-OVA immunization. Bar graph shows data from individual mice (5 mice per group with experiment repeated at least three times). p-values in all the graphs were calculated by one-way ANOVA. FIGs.11A-11L show Gb3 drives protection against heterotypic influenza infection. FIG.11A shows an experimental schedule of H1N1 infection (PR8; 102PFU) of different mouse strains. PFU = plaque forming units; i.n. = intranasal. FIG.11B show representative FACS plots and percentages of GC B cells in mediastinal draining lymph node. Bar graph depicts individual mice (5 mice per group), and experiment was repeated at least three times. FIG.11C shows serological analysis of immunoglobulin concentrations of indicated isotypes as performed by end-point titer measurements using ELISA. Graph depicts individual mice (5 mice per group), and experiment was repeated at least three times. FIG.11D shows the serum concentration of anti-rHA stalk immunoglobulins was detected by ELISA. Graph depicts individual mice (5 mice per group), and experiment was repeated at least three times. FIG.11E shows serum concentrations of immunoglobulins against rH3 (from H3N2) were detected by ELISA. Graph depicts individual mice (5 mice per group), and experiment was repeated at least three times. (f, g) H1N1 and H3N2 neutralizing antibody (NA) immunoglobulin titers in serum on day 24 post infection. Graphs depict individual mice (5 mice per group), and experiments were repeated at least three times. FIG.11H shows experimental set-up of H1N1 (PR8) or H3N2 (HK68, X-31) influenza infection. H1N1-primed mice were challenged with 103PFU of either H1N1 or H3N2. PFU = plaque forming units; i.n. = intranasal. FIGs.11I-11J show the weight loss curve following H1N1 or H3N2 infection. Data shown represent three independent experiments with 5 mice in each group. FIGs.11K-11L show H1N1 or H3N2 PFUs in lungs on day 5 post infection. Dots in bar graphs represent individual mice, and the experiments were repeated twice. p-values in all graphs were calculated by one-way ANOVA and in FIGs.11I and 11J, p-values of ≤0.05, ≤0.01, and ≤0.001 were marked with *, **, or ***, respectively. FIGs.12A-12D show GC B cells acquire exogenous Gb3 upon immunization to deploy its adjuvant functions. FIG.12A shows an experimental set-up for immunization of A4galt-KO mice with NP-OVA in the presence of Gb3. FIG.12B shows representative FACS plots and graph showing Gb3-positive GC B cells after immunization of A4galt-deficient mice with Gb3. Graph depicts data from 3 mice per group, and the experiment was repeated twice. FIG.12C shows serum concentrations of immunoglobulins against NP-OVA were detected by ELISA. Each dot represents one mouse. FIG.12D shows representative histogram overlay and bar graph showing the expression of phospho-Akt in GC B cells after BCR stimulation. Each dot represents one mouse, and the experiment was repeated twice. p-values for all graphs were calculated by two- sided Mann-Whitney U test. FIGs.13A-13F show one-shot vaccination with Gb3 and serum transfer from Gb3-adjuvanted mice mediate protection against influenza. FIG.13A shows an experimental set-up depicting animal groups, timeline of rHA immunization, sample collection schedule, and H1N1 infection (103PFU). PFU = plaque forming units; i.n. = intranasal. FIG.13B shows representative FACS plots and percentages of GC B cells in the draining lymph nodes on day 10 post immunization. Each dot represents one mouse, and the experiment was repeated twice. FIG.13C shows hemagglutination inhibition (HI) titers on day 28 post immunization. Each dot represents one mouse, and the experiment was repeated twice. FIG.13D shows the weight loss curve following H1N1 (PR8) infection. Data from 5 mice in each group represent mean ± SD, and the experiment was repeated three times. FIG.13E shows H1N1 PFUs in lungs on day 5 after infection. Each dot represents one mouse, and the experiment was repeated twice. FIG.13F is an experimental set-up depicting passive serum transfer and H1N1 infection regimen. Serum was taken from mice previously immunized with rHA and the corresponding adjuvants. Graph shows weight loss curves after H1N1 infection. Data are mean ± SD and represent two independent experiments with 4-5 mice in each group. Data in all graphs were analysed using one-way ANOVA, and p- values of ≤0.05, ≤0.01, and ≤0.001 were marked with *, **, or ***, in FIGs.13D and 13F. FIGs.14A-14G show Gb3 interacts with CD19 in human GC B cells to facilitate downstream signaling and serves as adjuvant in human tonsil organoids. FIG.14A are representative FACS plots showing gating strategy to identify B cell subsets among human tonsil cells. GC B cells (CD38+); plasma cells (CD27+, IgD-). CD77-positive and CD77-negative GC B cells were sorted from human tonsils, and CD77-negative GC B cells were subsequently cultured with Gb3. FACS analysis shows Gb3-positivity after culture (bottom panel). CD77 = Gb3. FIG.14B shows the proximity ligation assay (PLA) performed on GC B cells to probe for vicinity between Gb3 and CD19. CD77-negative, CD77-positive, and CD77-negative B cells reconstituted with Gb3 were used for PLA. FIG.14C is an immunoblot showing CD19 downstream signaling molecules (Akt) and transcription factors (Foxo1). CD77-negative, CD77-positive, and CD77-negative B cells reconstituted with Gb3 were used for immunoblot analysis. Anti-BCR antibodies (F(ab)2) were used to stimulate B cells. U = unstimulated. FIG.14D depicts the workflow for stimulation of human tonsil organoids with antigens and adjuvants. FIG.14E shows representative FACS plots and graphs depicting GC B cell and plasma cell percentages from unstimulated or antigen / adjuvant-stimulated tonsil organoids on day 10 post treatment. Each dot in bar graph represents a separate human tonsil donor (n=7). FIG.14F shows IgG1 secretion from unstimulated or antigen / adjuvant-stimulated tonsil organoids on day 21 post treatment. Each dot in graph represents a different human tonsil donor (n=7). In all graphs, data were analyzed using one-way ANOVA. FIG.14G is an illustration that depicts the regulation of the GC B cell response by Gb3 (left panel) and its translation as an adjuvant against influenza infection (right panel). Gb3 binds to CD19 to promote BCR downstream signaling and Foxo1 modulation, driving the cycling of GC B cells to the light zone. Moreover, Gb3 regulates MHC-II antigen presentation to Tfh cells to facilitate selection of antibodies against subdominant epitopes. Use of Gb3 as an adjuvant induces IgG2c class switch and selects antibodies recognizing the stalk region of hemagglutinin. Collectively, these mechanisms provide superior protection against heterologous influenza infection. GC = germinal center; Tfh = T follicular helper cell; TCR = T cell receptor; FDC = follicular dendritic cell; rHA = recombinant hemagglutinin; dLN = draining lymph node; H1N1 / H3N2 = influenza virus strains. FIGs.15A-15U shows the adjuvant Gb3 broadens the antibody response against influenza virus and spike protein of SARS-CoV-2. FIG.15A shows an Experimental schedule for prime / boost influenza model. FIGs.15B-15D show IgG, IgG1, IgG2c titers against rHA. FIG.15E shows an antibody avidity assay, by using NaSCN as denaturing agent. FIG.15F shows anti-rHA stalk IgG titers. FIG.15G shows IgG1 and IgG2c-producing plasma cells recognizing rHA at day 60 post immunization, as measured by ELISPOT. FIG.15H shows IgG titers against HA stalks of heterotypic influenza strains. FIGs.15I-15J: H1N1 and H3N2 neutralizing antibody (NA) IgG titers. FIGs.15K-15L show the weight loss curve following H1N1 or H3N2 infection. FIGs. 15M-15N show H1N1 or H3N2 PFU in lungs. FIG.15O shows an experimental set-up for prime / boost S-protein immunization. FIGs.15P-15R show IgG, IgG1, IgG2c titers against spike (S) protein. FIG.15S shows the frequencies of memory B cells recognizing receptor binding domain (RBD) on S-protein. FIG.15T shows IgG-producing plasma cells recognizing S-protein at day 72 post immunization, as measured by ELISPOT. FIG.15U: Inhibition of S-protein and RBD interaction by serum isolated from immunized mice. * p<0.05, ** p<0.01, *** p<0.001 using ANOVA. FIG.16 shows Gb3 abrogates tumor growth. Indicated mouse strains were subcutaneously inoculated with tumor cells (MCA101-OVA). Tumors were measured up to 16 days. * p<0.05, ** p<0.01, *** p<0.001 using ANOVA. DETAILED DESCRIPTION Some aspects of the present disclosure are based, at least in part, on the finding that Globotriaosylceramide (Gb3) or an analog thereof disclosed herein induces selection of high- affinity and broadly neutralizing antibodies and act as adjuvants in mice in vivo. As described herein, Gb3 or an analog thereof may be used for modifying an immune response. In some embodiments, Gb3 or an analog thereof is used as an adjuvant in vaccines. Adjuvants can enhance, prolong, and modulate immune responses to vaccinal antigens to maximize protective immunity. In some embodiments, Gb3 or an analog thereof is used in the treatment (both prophylactically or therapeutically) of diseases or cancers. The present disclosure, in some aspects, provides methods and compositions of enhancing an immune response in a subject by administering Gb3 or an analog thereof. In some embodiments, a method described herein comprises administering to the subject an effective amount of Gb3 or an analog thereof. In some embodiments, a composition described herein comprises an antigen and Gb3 or an analog thereof. In some embodiments, a method described herein comprises administering to the subject an effective amount of a composition of an antigen and Gb3 or an analog thereof. Globotriaosylceramide (Gb3) In some embodiments, the Gb3 described herein is used in methods of enhancing an immune response in a subject, comprising administering to the subject an effective amount of Gb3. As described herein, the term “globotriaosylceramide” or “Gb3” or “Gb3 analog” or “Gb3 analogs” or “Gb3 or an analog thereof” may refer to a molecule that is a glycosphingolipid, also referred to as “CD77”. As described herein, the term globotriaosylceramide (Gb3), also referred to as Burkitt’s lymphoma antigen CD77, is a molecule containing a ceramide lipid chain connected with an oligosaccharide (galactose α-1,4 galactose β-1,4 glucose) via an ether bond. Gb3 analogs are molecules containing the same trisaccharide structure but different lipid chains. The lipid component in Gb3 analogs may contain either ceramide, a sphingosine base only, or another hydrocarbon chain. In addition, Gb3 analogs may have different lengths of hydrocarbon chains and various degrees of saturation. In some embodiments, Gb3 or an analog thereof is a modified Gb3 or analog thereof. Modifications may be any modification commonly known in the art. Non-limiting examples of modifications include, but are not limited to, addition of hydroxyl or acetyl groups. In some embodiments, the modification is made to the sugar group. In some embodiments, the modification is made to the trisaccharide. Gb3 in the immune system is a recognized B cell marker. Additionally, Gb3 is in membranes of endothelial cells and tubular epithelial cells in the kidney. Gb3 is present on germinal center (GC) B cells and is important for the selection of high-affinity and broadly neutralizing antibodies. Gb3 binds to CD19 and amplifies the activation of the PI3-kinase / Akt / Foxo1 pathway and subsequent cycling of B cells through the GC. Moreover, Gb3 regulates MHC-II expression for productive antigen presentation to generate T follicular helper (Tfh) cells and GC B lymphocytes reactive with subdominant epitopes. In some embodiments, Gb3 is an adjuvant. In one aspect, the Gb3 is shown in Formula (I): Provided herein are uses for the compound of Formula (I) as an adjuvant in a vaccine and / or for use in enhancing an immune response in a subject in need thereof. In some embodiments, the compound of Formula (I) described herein is for use as an adjuvant in a vaccine. In some embodiments, the compound of Formula (I) described herein is for use in enhancing an immune response in a subject in need thereof. In some embodiments, a Gb3 analog is an adjuvant. As previously described, a Gb3 analog may broadly encompass a molecule with the same sugar (e.g., trisacchride) structure, with different hydrophobic lipid chain. Non-limiting examples or Gb3 analogs are included as Formula (II). In one aspect, the Gb3 analog is shown in Formula (II): Provided herein are uses for the compound of Formula (II) as an adjuvant in a vaccine and / or for use in enhancing an immune response in a subject in need thereof. In some embodiments, the compound of Formula (II) described herein is for use as an adjuvant in a vaccine. In some embodiments, the compound of Formula (II) described herein is for use in enhancing an immune response in a subject in need thereof. Methods of enhancing an immune response The present disclosure, in some aspects, provides methods and compositions of enhancing an immune response in a subject by administering Gb3 or an analog thereof. In some embodiments, the methods comprise administering to the subject an effective amount of Gb3 or an analog thereof described herein. In some embodiments, the methods comprise administering to the subject an effective amount of Gb3 or an analog thereof and an antigen (e.g., for enhancing an antigen-specific immune response). In some embodiments, the methods comprise administering to the subject an effective (e.g., therapeutically effective) amount of the Gb3 or an analog thereof. In some embodiments, the Gb3 or an analog thereof is administered separately from the antigen. In some embodiments, the Gb3 or an analog thereof is administered prior to administering the antigen. In some embodiments, the Gb3 or an analog thereof is administered after administering the antigen. In some embodiments, the Gb3 or an analog thereof and the antigen are administered simultaneously (e.g., concurrently). In some embodiment, the Gb3 or an analog thereof and the antigen are administered as an admixture. The antigen and / or the Gb3 or an analog thereof (e.g., the antigen alone, the Gb3 or an analog thereof alone, or the antigen and the Gb3 or an analog thereof together) described herein elicits an immune response in the subject. In some embodiments, the immune response is an adaptive immune response specific to the antigen in the composition or vaccine. In some embodiments, the antigen and / or the Gb3 or an analog thereof activates B cell immunity. In some embodiments, the antigen and / or the Gb3 or an analog thereof elicits antibody production. In some embodiments, the administration of the Gb3 or analog thereof and the antigen induces production of antibodies that are specific for the antigen. In some embodiments, the antibodies neutralize the bacterium, virus, parasite, or fungus from which the antigen is from. In some embodiments, the immune response comprises a humoral immune response. As described herein, the term “humoral” immune response refers to an immune response that is mediated by antibody molecules. In some embodiments, the immune response comprises binding of the Gb3 or an analog thereof to Cluster Differentiation 19 (CD19). As described herein, “CD19” refers to a 95 kd transmembrane glycoprotein in the immunoglobulin superfamily. The CD19 protein has the following domains: a single transmembrane domain, a cytoplasmic C-terminus, and extracellular N-terminus. CD19 is involved in establishing intrinsic B cell signaling thresholds through modulating both B cell receptor-dependent and independent signaling. In some embodiments, the Gb3 or an analog thereof binds to CD19. In some embodiments, the binding affinity of Gb3 or an analog thereof to CD19 is about 3.5-6.5 (e.g., 3.5-6.5, 3.5-5.5, 3.5-5, 3.5-4.5, 4.5-6.5, 4.5-5.5, 4.5- 5, 5-6.5, 5-5.5, 5.5-6.5) µM. In some embodiments, the binding affinity of Gb3 or an analog thereof to CD19 is about 3.5 µM, about 4.5 µM, about 5 µM, about 5.5 µM, about 6.5 µM. In some embodiments, the binding affinity of Gb3 or an analog thereof to CD19 is about 4.8µM. In some embodiments, the immune response comprises activation of the PI3K-Akt-mTOR pathway. As described herein, the “PI3K-Akt-mTOR pathway” refers to an intracellular signaling pathway. The PI3K-AKT-mTOR pathway that consists of two parts: (1) phosphatidylinositol 3- kinase (PI3K) and (2) its downstream molecule serine / threonine protein kinase B (PKB; also known as AKT). The PI3K-AKT-mTOR pathway is stimulated by RTK and cytokine receptor activation. The PI3K-AKT-mTOR pathway has important biological effects on cells, such as improving viability and inhibiting senescence, ageing and death and is associated with normal and abnormal physiological activity. In some embodiments, activation of the PI3K-Akt-mTOR pathway may be increased by at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 100%, at least 2-fold, at least 5-fold, at least 10- fold, at least 100-fold, at least 1000-fold or more, in the presence of the Gb3 or an analog thereof, compared to the absence of the Gb3or when the antigen is administered alone. In some embodiments, the immune response comprises a reduction of transcription mediated by Forkhead box protein O1 (FOXO-1). As described herein, the term “Forkhead box protein O1 (FOXO-1)” refers to a group of transcription factors that are known to be involved in many physiological and pathological processes. For example, apoptosis, cell cycle arrest, stress resistance, glucose metabolism, cellular differentiation and development, and tumor suppression. FOXO-1 regulates germinal center B cell proliferation in the dark zone in response to BCR activation. FOXO-1 is a major transcription factor that dominates the gene expression maintaining the dark zone of the germinal center, and consequently, PI3K activation and FOXO-1 degradation are a prerequisite for centroblast transition to the light zone. In some embodiments, transcription mediated by FOXO-1 may be reduced by at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 100%, at least 2-fold, at least 5-fold, at least 10-fold, at least 100-fold, at least 1000-fold or more, in the presence of the Gb3 or an analog thereof, compared to the absence of the Gb3 or when the antigen is administered alone. In some embodiments, the immune response comprises enhanced B cell receptor (BCR) signaling. As described herein, the term “B cell receptor (BCR) signaling” refers to signaling through the BCR that is essential for B cell survival and development, and antibody production in both physiological and pathological conditions. The nature of BCR signaling is varied in different subpopulations and developmental stages of B cells. In some embodiments, enhanced B cell receptor (BCR) signaling may be increased by at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 100%, at least 2-fold, at least 5-fold, at least 10-fold, at least 100-fold, at least 1000-fold or more, in the presence of the Gb3 or an analog thereof, compared to the absence of the Gb3 or when the antigen is administered alone. In some embodiments, the administration induces the expansion of germinal center (GC) B cells in the subject. B cells provide humoral immunity against infection by generating high- affinity antibodies in microanatomical structures called germinal centers (GC). During an infection or immunization, B cells enter the GC and differentiate into antibody-secreting plasma or memory B cells. Within GCs, B cells recognize and acquire antigens based on B cell receptor (BCR) affinities and compete for limiting amounts of T cell help, which is necessary for survival, proliferation, and selection of affinity-matured plasma and memory B cells. In some embodiments, expansion of GC B cells in the subject is measured by performing cell surface staining for antibody isotypes. In some embodiments, Gb3 or an analog thereof enhances heterologous immunity (e.g., cross-reactive antibodies) that provides broad protection against a range of viruses. In some embodiments, the heterologous immunity (e.g., cross-reactive antibodies) is increased by at least 20% in the presence of Gb3 or an analog thereof, compared to the absence of Gb3 or an analog thereof or when the antigen is administered alone. For example, the innate immune memory may be increased by at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 100%, at least 2-fold, at least 5-fold, at least 10-fold, at least 100-fold, at least 1000-fold or more, in the presence of Gb3 or an analog thereof , compared to the absence of Gb3 or an analog thereof or when the antigen is administered alone. In some embodiments, Gb3 or an analog thereof, when administered as an admixture with an antigen (e.g., the vaccine composition described herein), enhances the antigen-specific immune response against the antigen or against the invading agent from which the antigen is derived (e.g., a microbial pathogen or cancer), compared the absence of Gb3 or an analog thereof, e.g., when the antigen is administered alone. In some embodiments, Gb3 or an analog thereof enhances the production of antibodies (i.e., immunoglobulins) in the subject. In some embodiments, Gb3 or an analog thereof induces or enhances the production of antibodies (i.e., immunoglobulins) in the subject (e.g., by at least 20%), compared to the absence of Gb3 or an analog thereof, e.g., when the antigen is administered alone. For example, Gb3 or an analog thereof may enhance the production of antibodies (i.e., immunoglobulins) by at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 100%, at least 2-fold, at least 5-fold, at least 10-fold, at least 100-fold, at least 1000-fold or more in the subject, compared to the absence of Gb3 or an analog thereof , e.g., when the antigen is administered alone. In some embodiments, Gb3 or an analog thereof induces or enhances the production of antibodies (i.e., immunoglobulins) by 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100%, 2-fold, 5-fold, 10- fold, 100-fold, 1000-fold or more, compared the absence of Gb3 or an analog thereof, e.g., when the antigen is administered alone. Antibodies may be of any isotype, such as immunoglobulin A (IgA), immunoglobulin D (IgD), immunoglobulin E (IgE), immunoglobulin G (IgG), or immunoglobulin M (IgM). Antigen-specific antibodies that are IgGs may be those of any subclass, such as IgG1, IgG2, IgG3, or IgG4. In some embodiments, the production of antibody is an IgG. In some embodiments, the IgG is a subclass 1 IgG (IgG1) or a subclass 2 IgG (IgG2). In some embodiments, the production of antibody is an IgG. In some embodiments, the IgG is a subclass 2 IgG (IgG2). In some embodiments, the antibody promotes immunity against a cancer. One skilled in the art is familiar with how to evaluate the level of an antibody titer, e.g., by enzyme-linked immunosorbent assay (ELISA). In some embodiments, Gb3 or an analog thereof prolongs the effect of a vaccine (e.g., by at least 20%) in the subject, compared to without Gb3 or an analog thereof (e.g., when the antigen is administered alone). For example, Gb3 or an analog thereof may prolong the effect of a vaccine by at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 100%, at least 2-fold, at least 5-fold, at least 10-fold, at least 100- fold, at least 1000-fold or more, in the subject, compared to the absence of Gb3 or an analog thereof , e.g., when the antigen is administered alone. In some embodiments, Gb3 or an analog thereof prolongs the effect of a vaccine by 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100%, 2-fold, 5-fold, 10-fold, 100-fold, 1000-fold or more, compared to the absence of Gb3 or an analog thereof, e.g., when the antigen is administered alone. In some embodiments, Gb3 or an analog thereof increases rate of (accelerates) an immune response, compared to the absence of Gb3 or an analog thereof, e.g., when the antigen is administered alone. For example, Gb3 or an analog thereof may increase the rate of an immune response by at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 100%, at least 2-fold, at least 5-fold, at least 10-fold, at least 100- fold, at least 1000-fold or more in the subject, compared to the absence of Gb3 or an analog thereof , e.g., when the antigen is administered alone. In some embodiments, Gb3 or an analog thereof increases the rate of an immune response by 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100%, 2-fold, 5-fold, 10-fold, 100-fold, 1000-fold or more, compared to the absence of Gb3 or an analog thereof, e.g., when the antigen is administered alone. “Increase the rate of immune response” means it takes less time for the immune system of a subject to react to an invading agent (e.g., a microbial pathogen). In some embodiments, the antigen produces a same level of immune response against the antigen at a lower dose in the presence of Gb3 or an analog thereof, compared to the absence of Gb3 or an analog thereof, e.g., when the antigen is administered alone. In some embodiments, the amount of antigen needed to produce the same level of immune response is reduced by at least 20% in the presence of Gb3 or an analog thereof, compared to the absence of Gb3 or an analog thereof, e.g., when the antigen is administered alone. For example, the amount of antigen needed to produce the same level of immune response may be reduced by at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 99% or more, in the presence of Gb3 or an analog thereof, compared to the absence of Gb3 or an analog thereof, e.g., when the antigen is administered alone. In some embodiments, the amount of antigen needed to produce the same level of immune response is reduced by at 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 99% or more, in the presence of Gb3 or an analog thereof, compared to without Gb3 or an analog thereof, e.g., when the antigen is administered alone. The prophylactic or therapeutic use of Gb3 or an analog thereof, or the composition or vaccine composition described herein is also within the scope of the present disclosure. In some embodiments, the composition or vaccine composition described herein are used in methods of vaccinating a subject by prophylactically administering to the subject an effective amount of the composition or vaccine composition described herein. “Vaccinating a subject” refers to a process of administering an immunogen, typically an antigen formulated into a vaccine, to the subject in an amount effective to increase or activate an immune response against the antigen and, thus, against a pathogen displaying the antigen. In some embodiments, the terms do not require the creation of complete immunity against the pathogen. In some embodiments, the terms encompass a clinically favorable enhancement of an immune response toward the antigen or pathogen. Methods for immunization, including formulation of a vaccine composition and selection of doses, routes of administration and the schedule of administration (e.g., primary dose and one or more booster doses), are well known in the art. In some embodiments, vaccinating a subject reduces the risk of developing a disease (e.g., an infectious disease or cancer) in a subject. In some embodiments, a composition or vaccine composition comprising Gb3 or an analog thereof and optionally an antigen, as described herein, is used in methods of treating a disease (e.g., an infectious disease, allergy, or cancer) by administering to the subject an effective amount of the composition or vaccine composition described herein. In some embodiments, the disease is an infectious disease. An “infectious disease” refers to an illness caused by a pathogenic biological agent that results from transmission from an infected person, animal, or reservoir to a susceptible host, either directly or indirectly, through an intermediate plant or animal host, vector, or inanimate environment. See Last J M. ed. A dictionary of epidemiology.4th ed., New York: Oxford University Press, 1988. Infectious disease is also known as transmissible disease or communicable disease. In some embodiments, infectious diseases may be asymptomatic for much or even all of their course in a given host. Infectious pathogens include some viruses, bacteria, fungi, protozoa, multicellular parasites, and aberrant proteins known as prions. In some embodiments, the infectious disease is caused by any of the microbial pathogens (e.g., a bacterium, a mycobacterium, a fungus, a virus, a parasite or a prion) described herein or known to one skilled in the art. In some embodiments, the infectious disease is caused by bacteria such as, but not limited to, Bacillus anthracis (anthrax), Bordetella pertussis (whooping cough), Chlamydia spp., Corynebacterium diphtheriae (diphtheria), Clostridium tetani (tetanus), Haemophilus influenzae type b, Pneumococcus (pneumococcal infections), Streptococcus spp. including Group A or B streptococci, Staphylococci spp., Mycobacterium spp. (e.g., Mycobacterium tuberculosis), Neiserria spp. (e.g., Neiserria meningitidis - meningococcal disease), Salmonella typhi (typhoid), Vibrio cholerae (Cholera), or Yersinia pestis (plague). In some embodiments, the infectious disease is caused by a virus such as, but not limited to, adenovirus, enterovirus such as polio virus, coronavirus, dengue virus, Ebola virus, herpes viruses such as herpes simplex virus, cytomegalovirus and varicella-zoster (chickenpox and shingles), measles, mumps, rubella, hepatitis A virus, hepatitis B virus, hepatitis C virus, human papilloma virus, Influenza virus, rabies, Japanese encephalitis, rotavirus, human immunodeficiency virus (HIV), respiratory syncytial virus (RSV), smallpox, yellow fever, or Zika Virus. In some embodiments, the infectious disease is caused by a parasite such as, but not limited to, malaria (Plasmodium spp.), Leishmania spp., or a helminth. In some embodiments, the infectious disease is caused by a fungus such as, but not limited to, Candida spp., Aspergillus spp., Cryptococcus spp., Mucormycete spp., Blastomyces dermatitidis, Histoplasma capsulatum, or Sporothrix schenckii. In some embodiments, the infectious disease is caused by a prion. In some embodiments, the infectious disease is sepsis. In some embodiments, the composition or vaccine composition (e.g., a small molecule formulation or adjuvanted vaccine formulation) may be administered in combination with another therapeutic agent to prevent or treat an infectious disease. Such other therapeutic agents may be, without limitation: antibiotics, anti-viral agents, anti-fungal agents, or anti-parasitic agents. One skilled in the art is familiar with how to select or administer the additional therapeutic agent based on the disease to be treated. In some embodiments, the administration confers protection in the subject. The protection in a subject may be homotypic or heterotypic protection. Homotypic protection refers to the phenomenon whereby a history of an immune response against a stimulus or pathogen can provide a level of immunity to a related stimulus or pathogen. Heterotypic protection refers to the phenomenon whereby a history of an immune response against a stimulus or pathogen can provide a level of immunity to a second unrelated stimulus or pathogen. In some embodiments, the administration confers heterotypic protection in the subject. In some embodiments, the administration confers homotypic protection in the subject. In some embodiments, the disease is cancer. Vaccine compositions comprising cancer- specific antigens and the Gb3 or an analog thereof may be used in cancer immunotherapy by eliciting cancer-specific immune response against the cancer. The term “cancer” refers to a class of diseases characterized by the development of abnormal cells that proliferate uncontrollably and have the ability to infiltrate and destroy normal body tissues. See, e.g., Stedman’s Medical Dictionary, 25th ed.; Hensyl ed.; Williams & Wilkins: Philadelphia, 1990. Exemplary cancers include, but are not limited to, hematological malignancies. Additional exemplary cancers include, but are not limited to, lung cancer (e.g., bronchogenic carcinoma, small cell lung cancer (SCLC), non-small cell lung cancer (NSCLC), adenocarcinoma of the lung); kidney cancer (e.g., nephroblastoma, a.k.a. Wilms’ tumor, renal cell carcinoma); acoustic neuroma; adenocarcinoma; adrenal gland cancer; anal cancer; angiosarcoma (e.g., lymphangiosarcoma, lymphangioendotheliosarcoma, hemangiosarcoma); appendix cancer; benign monoclonal gammopathy; biliary cancer (e.g., cholangiocarcinoma); bladder cancer; breast cancer (e.g., adenocarcinoma of the breast, papillary carcinoma of the breast, mammary cancer, medullary carcinoma of the breast); brain cancer (e.g., meningioma, glioblastomas, glioma (e.g., astrocytoma, oligodendroglioma), medulloblastoma); bronchus cancer; carcinoid tumor; cervical cancer (e.g., cervical adenocarcinoma); choriocarcinoma; chordoma; craniopharyngioma; colorectal cancer (e.g., colon cancer, rectal cancer, colorectal adenocarcinoma); connective tissue cancer; epithelial carcinoma; ependymoma; endotheliosarcoma (e.g., Kaposi’s sarcoma, multiple idiopathic hemorrhagic sarcoma); endometrial cancer (e.g., uterine cancer, uterine sarcoma); esophageal cancer (e.g., adenocarcinoma of the esophagus, Barrett’s adenocarcinoma); Ewing’s sarcoma; ocular cancer (e.g., intraocular melanoma, retinoblastoma); familiar hypereosinophilia; gall bladder cancer; gastric cancer (e.g., stomach adenocarcinoma); gastrointestinal stromal tumor (GIST); germ cell cancer; head and neck cancer (e.g., head and neck squamous cell carcinoma, oral cancer (e.g., oral squamous cell carcinoma), throat cancer (e.g., laryngeal cancer, pharyngeal cancer, nasopharyngeal cancer, oropharyngeal cancer)); heavy chain disease (e.g., alpha chain disease, gamma chain disease, mu chain disease; hemangioblastoma; hypopharynx cancer; inflammatory myofibroblastic tumors; immunocytic amyloidosis; liver cancer (e.g., hepatocellular cancer (HCC), malignant hepatoma); leiomyosarcoma (LMS); mastocytosis (e.g., systemic mastocytosis); muscle cancer; myelodysplastic syndrome (MDS); mesothelioma; myeloproliferative disorder (MPD) (e.g., polycythemia vera (PV), essential thrombocytosis (ET), agnogenic myeloid metaplasia (AMM) a.k.a. myelofibrosis (MF), chronic idiopathic myelofibrosis, chronic myelocytic leukemia (CML), chronic neutrophilic leukemia (CNL), hypereosinophilic syndrome (HES)); neuroblastoma; neurofibroma (e.g., neurofibromatosis (NF) type 1 or type 2, schwannomatosis); neuroendocrine cancer (e.g., gastroenteropancreatic neuroendoctrine tumor (GEP-NET), carcinoid tumor); osteosarcoma (e.g., bone cancer); ovarian cancer (e.g., cystadenocarcinoma, ovarian embryonal carcinoma, ovarian adenocarcinoma); papillary adenocarcinoma; pancreatic cancer (e.g., pancreatic andenocarcinoma, intraductal papillary mucinous neoplasm (IPMN), Islet cell tumors); penile cancer (e.g., Paget’s disease of the penis and scrotum); pinealoma; primitive neuroectodermal tumor (PNT); plasma cell neoplasia; paraneoplastic syndromes; intraepithelial neoplasms; prostate cancer (e.g., prostate adenocarcinoma); rectal cancer; rhabdomyosarcoma; salivary gland cancer; skin cancer (e.g., squamous cell carcinoma (SCC), keratoacanthoma (KA), melanoma, basal cell carcinoma (BCC)); small bowel cancer (e.g., appendix cancer); soft tissue sarcoma (e.g., malignant fibrous histiocytoma (MFH), liposarcoma, malignant peripheral nerve sheath tumor (MPNST), chondrosarcoma, fibrosarcoma, myxosarcoma); sebaceous gland carcinoma; small intestine cancer; sweat gland carcinoma; synovioma; testicular cancer (e.g., seminoma, testicular embryonal carcinoma); thyroid cancer (e.g., papillary carcinoma of the thyroid, papillary thyroid carcinoma (PTC), medullary thyroid cancer); urethral cancer; vaginal cancer; and vulvar cancer (e.g., Paget’s disease of the vulva). In some embodiments, the cancer treated using the composition and methods of the present disclosure is melanoma. In some embodiments, additional anti-cancer agents may be administered in combination with the composition or vaccine composition described herein. In some embodiments, the anti- cancer agent is selected from the group consisting of: small molecules, oligonucleotides, polypeptides, and combinations thereof. In some embodiments, the anti-cancer agent is a chemotherapeutic agent. In some embodiments, the chemotherapeutic agent is selected from the group consisting of: Actinomycin, All-trans retinoic acid, Azacitidine, Azathioprine, Bleomycin, Bortezomib, Carboplatin, Capecitabine, Cisplatin, Chlorambucil, Cyclophosphamide, Cytarabine, Daunorubicin, Docetaxel, Doxifluridine, Doxorubicin, Epirubicin, Epothilone, Etoposide, Fluorouracil, Gemcitabine, Hydroxyurea, Idarubicin, Imatinib, Irinotecan, Mechlorethamine, Mercaptopurine, Methotrexate, Mitoxantrone, Oxaliplatin, Paclitaxel, Pemetrexed, Teniposide, Tioguanine, Topotecan, Valrubicin, Vinblastine, Vincristine, Vindesine, and Vinorelbine. In some embodiments, the chemotherapeutic agent is Doxorubicin. In some embodiments, the anti-cancer agent is an immune checkpoint inhibitor. An “immune checkpoint” is a protein in the immune system that either enhances an immune response signal (co-stimulatory molecules) or reduces an immune response signal. Many cancers protect themselves from the immune system by exploiting the inhibitory immune checkpoint proteins to inhibit the T cell signal. Exemplary inhibitory checkpoint proteins include, without limitation, Cytotoxic T-Lymphocyte-Associated protein 4 (CTLA-4), Programmed Death 1 receptor (PD-1), T-cell Immunoglobulin domain and Mucin domain 3 (TIM3), Lymphocyte Activation Gene-3 (LAG3), V-set domain-containing T-cell activation inhibitor 1 (VTVN1 or B7-H4), Cluster of Differentiation 276 (CD276 or B7-H3), B and T Lymphocyte Attenuator (BTLA), Galectin-9 (GAL9), Checkpoint kinase 1 (Chk1), Adenosine A2A receptor (A2aR), Indoleamine 2,3- dioxygenase (IDO), Killer-cell Immunoglobulin-like Receptor (KIR), Lymphocyte Activation Gene-3 (LAG3), and V-domain Ig suppressor of T cell activation (VISTA). Some of these immune checkpoint proteins need their cognate binding partners, or ligands, for their immune inhibitory activity. For example, A2AR is the receptor of adenosine A2A and binding of A2A to A2AR activates a negative immune feedback loop. As another example, PD-1 associates with its two ligands, PD-L1 and PD-L2, to down regulate the immune system by preventing the activation of T-cells. PD-1 promotes the programmed cell death of antigen specific T-cells in lymph nodes and simultaneously reduces programmed cell death of suppressor T cells, thus achieving its immune inhibitory function. As yet another example, CTLA4 is present on the surface of T cells, and when bound to its binding partner CD80 or CD86 on the surface of antigen-present cells (APCs), it transmits an inhibitory signal to T cells, thereby reducing the immune response. An “immune checkpoint inhibitor” is a molecule that prevents or weakens the activity of an immune checkpoint protein, for example, an immune checkpoint inhibitor may inhibit the binding of the immune checkpoint protein to its cognate binding partner, e.g., PD-1, CTLA-4, or A2aR. In some embodiments, the immune checkpoint inhibitor is a small molecule. In some embodiments, the immune checkpoint inhibitors are a nucleic acid aptamer (e.g., a siRNA targeting any one of the immune checkpoint proteins). In some embodiments, the immune checkpoint inhibitor is a recombinant protein. In some embodiments, the immune checkpoint inhibitor is an antibody. In some embodiments, the antibody comprises an anti-CTLA-4, anti-PD- 1, anti-PD-L1, anti-TIM3, anti-LAG3, anti-B7-H3, anti-B7-H4, anti-BTLA, anti-GAL9, anti-Chk, anti-A2aR, anti-IDO, anti-KIR, anti-LAG3, anti-VISTA antibody, or a combination of any two or more of the foregoing antibodies. In some embodiments, the immune checkpoint inhibitor is a monoclonal antibody. In some embodiments, the immune checkpoint inhibitor comprises anti- PD1, anti-PD-L1, anti-CTLA-4, or a combination of any two or more of the foregoing antibodies. For example, the anti-PD-1 antibody is pembrolizumab (Keytruda®) or nivolumab (Opdivo®) and the anti-CTLA-4 antibody is ipilimumab (Yervoy®). Thus, in some embodiments, the immune checkpoint inhibitor comprises pembrolizumab, nivolumab, ipilimumab, or any combination of two or more of the foregoing antibodies. The examples described herein are not meant to be limiting and that any immune checkpoint inhibitors known in the art and any combinations thereof may be used in accordance with the present disclosure. Additional exemplary agents that may be used in combination with the compositions described herein include, but are not limited to, anti-proliferative agents, anti-cancer agents, anti- angiogenesis agents, anti-inflammatory agents, immunosuppressants, anti-bacterial agents, anti- viral agents, cardiovascular agents, cholesterol-lowering agents, anti-diabetic agents, anti-allergic agents, contraceptive agents, pain-relieving agents, and a combination thereof. In some embodiments, the additional agent is an anti-proliferative agent (e.g., anti-cancer agent). In some embodiments, the additional pharmaceutical agent is an anti-leukemia agent. In some embodiments, the additional pharmaceutical agent is selected from ABITREXATE (methotrexate), ADE, Adriamycin RDF (doxorubicin hydrochloride), Ambochlorin (chlorambucil), ARRANON (nelarabine), ARZERRA (ofatumumab), BOSULIF (bosutinib), BUSULFEX (busulfan), CAMPATH (alemtuzumab), CERUBIDINE (daunorubicin hydrochloride), CLAFEN (cyclophosphamide), CLOFAREX (clofarabine), CLOLAR (clofarabine), CVP, CYTOSAR-U (cytarabine), CYTOXAN (cyclophosphamide), ERWINAZE (Asparaginase Erwinia Chrysanthemi), FLUDARA (fludarabine phosphate), FOLEX (methotrexate), FOLEX PFS (methotrexate), GAZYVA (obinutuzumab), GLEEVEC (imatinib mesylate), Hyper-CVAD, ICLUSIG (ponatinib hydrochloride), IMBRUVICA (ibrutinib), LEUKERAN (chlorambucil), LINFOLIZIN (chlorambucil), MARQIBO (vincristine sulfate liposome), METHOTREXATE LPF (methorexate), MEXATE (methotrexate), MEXATE-AQ (methotrexate), mitoxantrone hydrochloride, MUSTARGEN (mechlorethamine hydrochloride), MYLERAN (busulfan), NEOSAR (cyclophosphamide), ONCASPAR (Pegaspargase), PURINETHOL (mercaptopurine), PURIXAN (mercaptopurine), Rubidomycin (daunorubicin hydrochloride), SPRYCEL (dasatinib), SYNRIBO (omacetaxine mepesuccinate), TARABINE PFS (cytarabine), TASIGNA (nilotinib), TREANDA (bendamustine hydrochloride), TRISENOX (arsenic trioxide), VINCASAR PFS (vincristine sulfate), ZYDELIG (idelalisib), or a combination thereof. In some embodiments, the additional pharmaceutical agent is an anti-lymphoma agent. In some embodiments, the additional pharmaceutical agent is ABITREXATE (methotrexate), ABVD, ABVE, ABVE-PC, ADCETRIS (brentuximab vedotin), ADRIAMYCIN PFS (doxorubicin hydrochloride), ADRIAMYCIN RDF (doxorubicin hydrochloride), AMBOCHLORIN (chlorambucil), AMBOCLORIN (chlorambucil), ARRANON (nelarabine), BEACOPP, BECENUM (carmustine), BELEODAQ (belinostat), BEXXAR (tositumomab and iodine I 131 tositumomab), BICNU (carmustine), BLENOXANE (bleomycin), CARMUBRIS (carmustine), CHOP, CLAFEN (cyclophosphamide), COPP, COPP-ABV, CVP, CYTOXAN (cyclophosphamide), DEPOCYT (liposomal cytarabine), DTIC-DOME (dacarbazine), EPOCH, FOLEX (methotrexate), FOLEX PFS (methotrexate), FOLOTYN (pralatrexate), HYPER-CVAD, ICE, IMBRUVICA (ibrutinib), INTRON A (recombinant interferon alfa-2b), ISTODAX (romidepsin), LEUKERAN (chlorambucil), LINFOLIZIN (chlorambucil), Lomustine, MATULANE (procarbazine hydrochloride), METHOTREXATE LPF (methotrexate), MEXATE (methotrexate), MEXATE-AQ (methotrexate), MOPP, MOZOBIL (plerixafor), MUSTARGEN (mechlorethamine hydrochloride), NEOSAR (cyclophosphamide), OEPA, ONTAK (denileukin diftitox), OPPA, R-CHOP, REVLIMID (lenalidomide), RITUXAN (rituximab), STANFORD V, TREANDA (bendamustine hydrochloride), VAMP, VELBAN (vinblastine sulfate), VELCADE (bortezomib), VELSAR (vinblastine sulfate), VINCASAR PFS (vincristine sulfate), ZEVALIN (ibritumomab tiuxetan), ZOLINZA (vorinostat), ZYDELIG (idelalisib), or a combination thereof. In some embodiments, the additional pharmaceutical agent is REVLIMID (lenalidomide), DACOGEN (decitabine), VIDAZA (azacitidine), CYTOSAR-U (cytarabine), IDAMYCIN (idarubicin), CERUBIDINE (daunorubicin), LEUKERAN (chlorambucil), NEOSAR (cyclophosphamide), FLUDARA (fludarabine), LEUSTATIN (cladribine), or a combination thereof. In some embodiments, the additional pharmaceutical agent is ABITREXATE (methotrexate), ABRAXANE (paclitaxel albumin-stabilized nanoparticle formulation), AC, AC- T, ADE, ADRIAMYCIN PFS (doxorubicin hydrochloride), ADRUCIL (fluorouracil), AFINITOR (everolimus), AFINITOR DISPERZ (everolimus), ALDARA (imiquimod), ALIMTA (pemetrexed disodium), AREDIA (pamidronate disodium), ARIMIDEX (anastrozole), AROMASIN (exemestane), AVASTIN (bevacizumab), BECENUM (carmustine), BEP, BICNU (carmustine), BLENOXANE (bleomycin), CAF, CAMPTOSAR (irinotecan hydrochloride), CAPOX, CAPRELSA (vandetanib), CARBOPLATIN-TAXOL, CARMUBRIS (carmustine), CASODEX (bicalutamide), CEENU (lomustine), CERUBIDINE (daunorubicin hydrochloride), CERVARIX (recombinant HPV bivalent vaccine), CLAFEN (cyclophosphamide), CMF, COMETRIQ (cabozantinib-s-malate), COSMEGEN (dactinomycin), CYFOS (ifosfamide), CYRAMZA (ramucirumab), CYTOSAR-U (cytarabine), CYTOXAN (cyclophosphamide), DACOGEN (decitabine), DEGARELIX, DOXIL (doxorubicin hydrochloride liposome), DOXORUBICIN HYDROCHLORIDE, DOX-SL (doxorubicin hydrochloride liposome), DTIC- DOME (dacarbazine), EFUDEX (fluorouracil), ELLENCE (epirubicin hydrochloride), ELOXATIN (oxaliplatin), ERBITUX (cetuximab), ERIVEDGE (vismodegib), ETOPOPHOS (etoposide phosphate), EVACET (doxorubicin hydrochloride liposome), FARESTON (toremifene), FASLODEX (fulvestrant), FEC, FEMARA (letrozole), FLUOROPLEX (fluorouracil), FOLEX (methotrexate), FOLEX PFS (methotrexate), FOLFIRI , FOLFIRI- BEVACIZUMAB, FOLFIRI-CETUXIMAB, FOLFIRINOX, FOLFOX, FU-LV, GARDASIL (recombinant human papillomavirus (HPV) quadrivalent vaccine), GEMCITABINE- CISPLATIN, GEMCITABINE-OXALIPLATIN, GEMZAR (gemcitabine hydrochloride), GILOTRIF (afatinib dimaleate), GLEEVEC (imatinib mesylate), GLIADEL (carmustine implant), GLIADEL WAFER (carmustine implant), HERCEPTIN (trastuzumab), HYCAMTIN (topotecan hydrochloride), IFEX (ifosfamide), IFOSFAMIDUM (ifosfamide), INLYTA (axitinib), INTRON A (recombinant interferon alfa-2b), IRESSA (gefitinib), IXEMPRA (ixabepilone), JAKAFI (ruxolitinib phosphate), JEVTANA (cabazitaxel), KADCYLA (ado- trastuzumab emtansine), KEYTRUDA (pembrolizumab), KYPROLIS (carfilzomib), LIPODOX (doxorubicin hydrochloride liposome), LUPRON (leuprolide acetate), LUPRON DEPOT (leuprolide acetate), LUPRON DEPOT-3 MONTH (leuprolide acetate), LUPRON DEPOT-4 MONTH (leuprolide acetate), LUPRON DEPOT-PED (leuprolide acetate), MEGACE (megestrol acetate), MEKINIST (trametinib), METHAZOLASTONE (temozolomide), METHOTREXATE LPF (methotrexate), MEXATE (methotrexate), MEXATE-AQ (methotrexate), MITOXANTRONE HYDROCHLORIDE, MITOZYTREX (mitomycin c), MOZOBIL (plerixafor), MUSTARGEN (mechlorethamine hydrochloride), MUTAMYCIN (mitomycin c), MYLOSAR (azacitidine), NAVELBINE (vinorelbine tartrate), NEOSAR (cyclophosphamide), NEXAVAR (sorafenib tosylate), NOLVADEX (tamoxifen citrate), NOVALDEX (tamoxifen citrate), OFF, PAD, PARAPLAT (carboplatin), PARAPLATIN (carboplatin), PEG-INTRON (peginterferon alfa-2b), PEMETREXED DISODIUM, PERJETA (pertuzumab), PLATINOL (cisplatin), PLATINOL-AQ (cisplatin), POMALYST (pomalidomide), prednisone, PROLEUKIN (aldesleukin), PROLIA (denosumab), PROVENGE (sipuleucel-t), REVLIMID (lenalidomide), RUBIDOMYCIN (daunorubicin hydrochloride), SPRYCEL (dasatinib), STIVARGA (regorafenib), SUTENT (sunitinib malate), SYLATRON (peginterferon alfa-2b), SYLVANT (siltuximab), SYNOVIR (thalidomide), TAC, TAFINLAR (dabrafenib), TARABINE PFS (cytarabine), TARCEVA (erlotinib hydrochloride), TASIGNA (nilotinib), TAXOL (paclitaxel), TAXOTERE (docetaxel), TEMODAR (temozolomide), THALOMID (thalidomide), TOPOSAR (etoposide), TORISEL (temsirolimus), TPF, TRISENOX (arsenic trioxide), TYKERB (lapatinib ditosylate), VECTIBIX (panitumumab), VEIP, VELBAN (vinblastine sulfate), VELCADE (bortezomib), VELSAR (vinblastine sulfate), VEPESID (etoposide), VIADUR (leuprolide acetate), VIDAZA (azacitidine), VINCASAR PFS (vincristine sulfate), VOTRIENT (pazopanib hydrochloride), WELLCOVORIN (leucovorin calcium), XALKORI (crizotinib), XELODA (capecitabine), XELOX, XGEVA (denosumab), XOFIGO (radium 223 dichloride), XTANDI (enzalutamide), YERVOY (ipilimumab), ZALTRAP (ziv-aflibercept), ZELBORAF (vemurafenib), ZOLADEX (goserelin acetate), ZOMETA (zoledronic acid), ZYKADIA (ceritinib), ZYTIGA (abiraterone acetate), ENMD-2076, PCI-32765, AC220, dovitinib lactate (TKI258, CHIR-258), BIBW 2992 (TOVOKTM), SGX523, PF-04217903, PF-02341066, PF- 299804, BMS-777607, ABT-869, MP470, BIBF 1120 (VARGATEF®), AP24534, JNJ- 26483327, MGCD265, DCC-2036, BMS-690154, CEP-11981, tivozanib (AV-951), OSI-930, MM-121, XL-184, XL-647, and / or XL228), proteasome inhibitors (e.g., bortezomib (Velcade)), mTOR inhibitors (e.g., rapamycin, temsirolimus (CCI-779), everolimus (RAD-001), ridaforolimus, AP23573 (Ariad), AZD8055 (AstraZeneca), BEZ235 (Novartis), BGT226 (Novartis), XL765 (Sanofi Aventis), PF-4691502 (Pfizer), GDC0980 (Genetech), SF1126 (Semafoe) and OSI-027 (OSI)), oblimersen, gemcitabine, carminomycin, leucovorin, pemetrexed, cyclophosphamide, dacarbazine, procarbizine, prednisolone, dexamethasone, campathecin, plicamycin, asparaginase, aminopterin, methopterin, porfiromycin, melphalan, leurosidine, leurosine, chlorambucil, trabectedin, procarbazine, discodermolide, carminomycin,, aminopterin, and hexamethyl melamine, or a combination thereof. In some embodiments, the additional agent is a protein kinase inhibitor (e.g., tyrosine protein kinase inhibitor). In some embodiments, the additional agent is selected from the group consisting of epigenetic or transcriptional modulators (e.g., DNA methyltransferase inhibitors, histone deacetylase inhibitors (HDAC inhibitors), lysine methyltransferase inhibitors), antimitotic drugs (e.g., taxanes and vinca alkaloids), hormone receptor modulators (e.g., estrogen receptor modulators and androgen receptor modulators), cell signaling pathway inhibitors (e.g., tyrosine protein kinase inhibitors), modulators of protein stability (e.g., proteasome inhibitors), Hsp90 inhibitors, glucocorticoids, all-trans retinoic acids, and other agents that promote differentiation. In some embodiments, a composition or vaccine composition described herein is formulated for administration to a subject. In some embodiments, the composition or vaccine composition further comprises a pharmaceutically acceptable carrier. The phrase “pharmaceutically acceptable” is employed herein to refer to those compounds, materials, compositions, and / or dosage forms which are, within the scope of sound medical judgment, suitable for use in contact with the tissues of human beings and animals without excessive toxicity, irritation, allergic response, or other problem or complication, commensurate with a reasonable benefit / risk ratio. The phrase “pharmaceutically acceptable carrier” means a pharmaceutically acceptable material, composition or vehicle, such as a liquid or solid filler, diluent, excipient, solvent or encapsulating material, involved in carrying or transporting the subject agents from one organ, or portion of the body, to another organ, or portion of the body. Each carrier must be “acceptable” in the sense of being compatible with the other ingredients of the formulation and not injurious to the tissue of the patient (e.g., physiologically compatible, sterile, physiologic pH, etc.). The term “carrier” denotes an organic or inorganic ingredient, natural or synthetic, with which the active ingredient is combined to facilitate the application. The components of the composition or vaccine composition described herein also are capable of being co-mingled with the molecules of the present disclosure, and with each other, in a manner such that there is no interaction which would substantially impair the desired pharmaceutical efficacy. Some examples of materials which can serve as pharmaceutically-acceptable carriers include: (1) sugars, such as lactose, glucose and sucrose; (2) starches, such as corn starch and potato starch; (3) cellulose, and its derivatives, such as sodium carboxymethyl cellulose, methylcellulose, ethyl cellulose, microcrystalline cellulose and cellulose acetate; (4) powdered tragacanth; (5) malt; (6) gelatin; (7) lubricating agents, such as magnesium stearate, sodium lauryl sulfate and talc; (8) excipients, such as cocoa butter and suppository waxes; (9) oils, such as peanut oil, cottonseed oil, safflower oil, sesame oil, olive oil, corn oil and soybean oil; (10) glycols, such as propylene glycol; (11) polyols, such as glycerin, sorbitol, mannitol and polyethylene glycol (PEG); (12) esters, such as ethyl oleate and ethyl laurate; (13) agar; (14) buffering agents, such as magnesium hydroxide and aluminum hydroxide; (15) alginic acid; (16) pyrogen-free water; (17) isotonic saline; (18) Ringer's solution; (19) ethyl alcohol; (20) pH buffered solutions; (21) polyesters, polycarbonates and / or polyanhydrides; (22) bulking agents, such as polypeptides and amino acids (23) serum component, such as serum albumin, HDL and LDL; (22) C2-C12 alcohols, such as ethanol; and (23) other non-toxic compatible substances employed in pharmaceutical formulations. Wetting agents, coloring agents, release agents, coating agents, sweetening agents, flavoring agents, perfuming agents, preservative and antioxidants can also be present in the formulation. The composition or vaccine composition described herein may conveniently be presented in unit dosage form and may be prepared by any of the methods well-known in the art of pharmacy. The term "unit dose" when used in reference to a composition or vaccine composition described herein of the present disclosure refers to physically discrete units suitable as unitary dosage for the subject, each unit containing a predetermined quantity of active material calculated to produce the desired therapeutic effect in association with the required diluent; i.e., carrier, or vehicle. Relative amounts of the active ingredient, the pharmaceutically acceptable excipient, and / or any additional ingredients in a pharmaceutical composition described herein will vary, depending upon the identity, size, and / or condition of the subject treated and further depending upon the route by which the composition is to be administered. The composition may comprise between 0.1% and 100% (w / w) active ingredient. Pharmaceutically acceptable excipients used in the manufacture of provided pharmaceutical compositions include inert diluents, dispersing and / or granulating agents, surface active agents and / or emulsifiers, disintegrating agents, binding agents, preservatives, buffering agents, lubricating agents, and / or oils. Excipients such as cocoa butter and suppository waxes, coloring agents, coating agents, sweetening, flavoring, and perfuming agents may also be present in the composition. Exemplary diluents include calcium carbonate, sodium carbonate, calcium phosphate, dicalcium phosphate, calcium sulfate, calcium hydrogen phosphate, sodium phosphate lactose, sucrose, cellulose, microcrystalline cellulose, kaolin, mannitol, sorbitol, inositol, sodium chloride, dry starch, cornstarch, powdered sugar, and mixtures thereof. Exemplary granulating and / or dispersing agents include potato starch, corn starch, tapioca starch, sodium starch glycolate, clays, alginic acid, guar gum, citrus pulp, agar, bentonite, cellulose, and wood products, natural sponge, cation-exchange resins, calcium carbonate, silicates, sodium carbonate, cross-linked poly(vinyl-pyrrolidone) (crospovidone), sodium carboxymethyl starch (sodium starch glycolate), carboxymethyl cellulose, cross-linked sodium carboxymethyl cellulose (croscarmellose), methylcellulose, pregelatinized starch (starch 1500), microcrystalline starch, water insoluble starch, calcium carboxymethyl cellulose, magnesium aluminum silicate (Veegum), sodium lauryl sulfate, quaternary ammonium compounds, and mixtures thereof. Exemplary surface active agents and / or emulsifiers include natural emulsifiers (e.g., acacia, agar, alginic acid, sodium alginate, tragacanth, chondrux, cholesterol, xanthan, pectin, gelatin, egg yolk, casein, wool fat, cholesterol, wax, and lecithin), colloidal clays (e.g., bentonite (aluminum silicate) and Veegum (magnesium aluminum silicate)), long chain amino acid derivatives, high molecular weight alcohols (e.g., stearyl alcohol, cetyl alcohol, oleyl alcohol, triacetin monostearate, ethylene glycol distearate, glyceryl monostearate, and propylene glycol monostearate, polyvinyl alcohol), carbomers (e.g., carboxy polymethylene, polyacrylic acid, acrylic acid polymer, and carboxyvinyl polymer), carrageenan, cellulosic derivatives (e.g., carboxymethylcellulose sodium, powdered cellulose, hydroxymethyl cellulose, hydroxypropyl cellulose, hydroxypropyl methylcellulose, methylcellulose), sorbitan fatty acid esters (e.g., polyoxyethylene sorbitan monolaurate (Tween®20), polyoxyethylene sorbitan (Tween®60), polyoxyethylene sorbitan monooleate (Tween®80), sorbitan monopalmitate (Span®40), sorbitan monostearate (Span®60), sorbitan tristearate (Span®65), glyceryl monooleate, sorbitan monooleate (Span®80), polyoxyethylene esters (e.g., polyoxyethylene monostearate (Myrj®45), polyoxyethylene hydrogenated castor oil, polyethoxylated castor oil, polyoxymethylene stearate, and Solutol®), sucrose fatty acid esters, polyethylene glycol fatty acid esters (e.g., Cremophor®), polyoxyethylene ethers, (e.g., polyoxyethylene lauryl ether (Brij®30)), poly(vinyl-pyrrolidone), diethylene glycol monolaurate, triethanolamine oleate, sodium oleate, potassium oleate, ethyl oleate, oleic acid, ethyl laurate, sodium lauryl sulfate, Pluronic®F-68, poloxamer P-188, cetrimonium bromide, cetylpyridinium chloride, benzalkonium chloride, docusate sodium, and / or mixtures thereof. Exemplary binding agents include starch (e.g., cornstarch and starch paste), gelatin, sugars (e.g., sucrose, glucose, dextrose, dextrin, molasses, lactose, lactitol, mannitol, etc.), natural and synthetic gums (e.g., acacia, sodium alginate, extract of Irish moss, panwar gum, ghatti gum, mucilage of isapol husks, carboxymethylcellulose, methylcellulose, ethylcellulose, hydroxyethylcellulose, hydroxypropyl cellulose, hydroxypropyl methylcellulose, microcrystalline cellulose, cellulose acetate, poly(vinyl-pyrrolidone), magnesium aluminum silicate (Veegum®), and larch arabogalactan), alginates, polyethylene oxide, polyethylene glycol, inorganic calcium salts, silicic acid, polymethacrylates, waxes, water, alcohol, and / or mixtures thereof. Exemplary preservatives include antioxidants, chelating agents, antimicrobial preservatives, antifungal preservatives, antiprotozoan preservatives, alcohol preservatives, acidic preservatives, and other preservatives. In certain embodiments, the preservative is an antioxidant. In other embodiments, the preservative is a chelating agent. Exemplary antioxidants include alpha tocopherol, ascorbic acid, acorbyl palmitate, butylated hydroxyanisole, butylated hydroxytoluene, monothioglycerol, potassium metabisulfite, propionic acid, propyl gallate, sodium ascorbate, sodium bisulfite, sodium metabisulfite, and sodium sulfite. Exemplary chelating agents include ethylenediaminetetraacetic acid (EDTA) and salts and hydrates thereof (e.g., sodium edetate, disodium edetate, trisodium edetate, calcium disodium edetate, dipotassium edetate, and the like), citric acid and salts and hydrates thereof (e.g., citric acid monohydrate), fumaric acid and salts and hydrates thereof, malic acid and salts and hydrates thereof, phosphoric acid and salts and hydrates thereof, and tartaric acid and salts and hydrates thereof. Exemplary antimicrobial preservatives include benzalkonium chloride, benzethonium chloride, benzyl alcohol, bronopol, cetrimide, cetylpyridinium chloride, chlorhexidine, chlorobutanol, chlorocresol, chloroxylenol, cresol, ethyl alcohol, glycerin, hexetidine, imidurea, phenol, phenoxyethanol, phenylethyl alcohol, phenylmercuric nitrate, propylene glycol, and thimerosal. Exemplary antifungal preservatives include butyl paraben, methyl paraben, ethyl paraben, propyl paraben, benzoic acid, hydroxybenzoic acid, potassium benzoate, potassium sorbate, sodium benzoate, sodium propionate, and sorbic acid. Exemplary alcohol preservatives include ethanol, polyethylene glycol, phenol, phenolic compounds, bisphenol, chlorobutanol, hydroxybenzoate, and phenylethyl alcohol. Exemplary acidic preservatives include vitamin A, vitamin C, vitamin E, beta-carotene, citric acid, acetic acid, dehydroacetic acid, ascorbic acid, sorbic acid, and phytic acid. Other preservatives include tocopherol, tocopherol acetate, deteroxime mesylate, cetrimide, butylated hydroxyanisol (BHA), butylated hydroxytoluened (BHT), ethylenediamine, sodium lauryl sulfate (SLS), sodium lauryl ether sulfate (SLES), sodium bisulfite, sodium metabisulfite, potassium sulfite, potassium metabisulfite, Glydant®Plus, Phenonip®, methylparaben, Germall®115, Germaben®II, Neolone®, Kathon®, and Euxyl®. Exemplary buffering agents include citrate buffer solutions, acetate buffer solutions, phosphate buffer solutions, ammonium chloride, calcium carbonate, calcium chloride, calcium citrate, calcium glubionate, calcium gluceptate, calcium gluconate, D-gluconic acid, calcium glycerophosphate, calcium lactate, propanoic acid, calcium levulinate, pentanoic acid, dibasic calcium phosphate, phosphoric acid, tribasic calcium phosphate, calcium hydroxide phosphate, potassium acetate, potassium chloride, potassium gluconate, potassium mixtures, dibasic potassium phosphate, monobasic potassium phosphate, potassium phosphate mixtures, sodium acetate, sodium bicarbonate, sodium chloride, sodium citrate, sodium lactate, dibasic sodium phosphate, monobasic sodium phosphate, sodium phosphate mixtures, tromethamine, magnesium hydroxide, aluminum hydroxide, alginic acid, pyrogen-free water, isotonic saline, Ringer’s solution, ethyl alcohol, and mixtures thereof. Exemplary lubricating agents include magnesium stearate, calcium stearate, stearic acid, silica, talc, malt, glyceryl behanate, hydrogenated vegetable oils, polyethylene glycol, sodium benzoate, sodium acetate, sodium chloride, leucine, magnesium lauryl sulfate, sodium lauryl sulfate, and mixtures thereof. Exemplary natural oils include almond, apricot kernel, avocado, babassu, bergamot, black current seed, borage, cade, camomile, canola, caraway, carnauba, castor, cinnamon, cocoa butter, coconut, cod liver, coffee, corn, cotton seed, emu, eucalyptus, evening primrose, fish, flaxseed, geraniol, gourd, grape seed, hazel nut, hyssop, isopropyl myristate, jojoba, kukui nut, lavandin, lavender, lemon, litsea cubeba, macadamia nut, mallow, mango seed, meadowfoam seed, mink, nutmeg, olive, orange, orange roughy, palm, palm kernel, peach kernel, peanut, poppy seed, pumpkin seed, rapeseed, rice bran, rosemary, safflower, sandalwood, sasquana, savoury, sea buckthorn, sesame, shea butter, silicone, soybean, sunflower, tea tree, thistle, tsubaki, vetiver, walnut, and wheat germ oils. Exemplary synthetic oils include, but are not limited to, butyl stearate, caprylic triglyceride, capric triglyceride, cyclomethicone, diethyl sebacate, dimethicone 360, isopropyl myristate, mineral oil, octyldodecanol, oleyl alcohol, silicone oil, and mixtures thereof. Liquid dosage forms for oral and parenteral administration include pharmaceutically acceptable emulsions, microemulsions, solutions, suspensions, syrups and elixirs. In addition to the active ingredients, the liquid dosage forms may comprise inert diluents commonly used in the art such as, for example, water or other solvents, solubilizing agents and emulsifiers such as ethyl alcohol, isopropyl alcohol, ethyl carbonate, ethyl acetate, benzyl alcohol, benzyl benzoate, propylene glycol, 1,3-butylene glycol, dimethylformamide, oils (e.g., cottonseed, groundnut, corn, germ, olive, castor, and sesame oils), glycerol, tetrahydrofurfuryl alcohol, polyethylene glycols and fatty acid esters of sorbitan, and mixtures thereof. Besides inert diluents, the oral compositions can include adjuvants such as wetting agents, emulsifying and suspending agents, sweetening, flavoring, and perfuming agents. In certain embodiments for parenteral administration, the conjugates described herein are mixed with solubilizing agents such as Cremophor®, alcohols, oils, modified oils, glycols, polysorbates, cyclodextrins, polymers, and mixtures thereof. The formulation of the composition or vaccine composition described herein may dependent upon the route of administration. Injectable preparations suitable for parenteral administration or intratumoral, peritumoral, intralesional or perilesional administration include, for example, sterile injectable aqueous or oleaginous suspensions and may be formulated according to the known art using suitable dispersing or wetting agents and suspending agents. The sterile injectable preparation may also be a sterile injectable solution, suspension or emulsion in a nontoxic parenterally acceptable diluent or solvent, for example, as a solution in 1,3 propanediol or 1,3 butanediol. Among the acceptable vehicles and solvents that may be employed are water, Ringer's solution, U.S.P. and isotonic sodium chloride solution. In addition, sterile, fixed oils are conventionally employed as a solvent or suspending medium. For this purpose any bland fixed oil may be employed including synthetic mono- or di-glycerides. In addition, fatty acids such as oleic acid find use in the preparation of injectables. The injectable formulations can be sterilized, for example, by filtration through a bacterial-retaining filter, or by incorporating sterilizing agents in the form of sterile solid compositions which can be dissolved or dispersed in sterile water or other sterile injectable medium prior to use. Solid dosage forms for oral administration include capsules, tablets, pills, powders, and granules. In such solid dosage forms, the active ingredient is mixed with at least one inert, pharmaceutically acceptable excipient or carrier such as sodium citrate or dicalcium phosphate and / or (a) fillers or extenders such as starches, lactose, sucrose, glucose, mannitol, and silicic acid, (b) binders such as, for example, carboxymethylcellulose, alginates, gelatin, polyvinylpyrrolidinone, sucrose, and acacia, (c) humectants such as glycerol, (d) disintegrating agents such as agar, calcium carbonate, potato or tapioca starch, alginic acid, certain silicates, and sodium carbonate, (e) solution retarding agents such as paraffin, (f) absorption accelerators such as quaternary ammonium compounds, (g) wetting agents such as, for example, cetyl alcohol and glycerol monostearate, (h) absorbents such as kaolin and bentonite clay, and (i) lubricants such as talc, calcium stearate, magnesium stearate, solid polyethylene glycols, sodium lauryl sulfate, and mixtures thereof. In the case of capsules, tablets, and pills, the dosage form may include a buffering agent. Solid compositions of a similar type can be employed as fillers in soft and hard-filled gelatin capsules using such excipients as lactose or milk sugar as well as high molecular weight polyethylene glycols and the like. The solid dosage forms of tablets, dragées, capsules, pills, and granules can be prepared with coatings and shells such as enteric coatings and other coatings well known in the art of pharmacology. They may optionally comprise opacifying agents and can be of a composition that they release the active ingredient(s) only, or preferentially, in a certain part of the intestinal tract, optionally, in a delayed manner. Examples of encapsulating compositions which can be used include polymeric substances and waxes. Solid compositions of a similar type can be employed as fillers in soft and hard-filled gelatin capsules using such excipients as lactose or milk sugar as well as high molecular weight polethylene glycols and the like. The active ingredient can be in a micro-encapsulated form with one or more excipients as noted above. The solid dosage forms of tablets, dragées, capsules, pills, and granules can be prepared with coatings and shells such as enteric coatings, release controlling coatings, and other coatings well known in the pharmaceutical formulating art. In such solid dosage forms the active ingredient can be admixed with at least one inert diluent such as sucrose, lactose, or starch. Such dosage forms may comprise, as is normal practice, additional substances other than inert diluents, e.g., tableting lubricants and other tableting aids such a magnesium stearate and microcrystalline cellulose. In the case of capsules, tablets and pills, the dosage forms may comprise buffering agents. They may optionally comprise opacifying agents and can be of a composition that they release the active ingredient(s) only, or preferentially, in a certain part of the intestinal tract, optionally, in a delayed manner. Examples of encapsulating agents which can be used include polymeric substances and waxes. Suitable devices for use in delivering intradermal pharmaceutical compositions described herein include short needle devices. Intradermal compositions can be administered by devices which limit the effective penetration length of a needle into the skin. Alternatively or additionally, conventional syringes can be used in the classical Mantoux method of intradermal administration. Jet injection devices which deliver liquid formulations to the dermis via a liquid jet injector and / or via a needle which pierces the stratum corneum and produces a jet which reaches the dermis are suitable. Ballistic powder / particle delivery devices which use compressed gas to accelerate the compound in powder form through the outer layers of the skin to the dermis are suitable. For topical administration, the composition or vaccine composition described herein can be formulated into ointments, salves, gels, or creams, as is generally known in the art. Topical administration can utilize transdermal delivery systems well known in the art. An example is a dermal patch. Compositions suitable for oral administration may be presented as discrete units, such as capsules, tablets, lozenges, each containing a predetermined amount of the anti-inflammatory agent. Other compositions include suspensions in aqueous liquids or non-aqueous liquids such as a syrup, elixir or an emulsion. Other delivery systems can include time-release, delayed release or sustained release delivery systems. Such systems can avoid repeated administrations of the anti-inflammatory agent, increasing convenience to the subject and the physician. Many types of release delivery systems are available and known to those of ordinary skill in the art. They include polymer base systems such as poly(lactide-glycolide), copolyoxalates, polycaprolactones, polyesteramides, polyorthoesters, polyhydroxybutyric acid, and polyanhydrides. Microcapsules of the foregoing polymers containing drugs are described in, for example, U.S. Patent 5,075,109. Delivery systems also include non-polymer systems that are: lipids including sterols such as cholesterol, cholesterol esters and fatty acids or neutral fats such as mono- di- and tri-glycerides; hydrogel release systems; sylastic systems; peptide based systems; wax coatings; compressed tablets using conventional binders and excipients; partially fused implants; and the like. Specific examples include, but are not limited to: (a) erosional systems in which the anti-inflammatory agent is contained in a form within a matrix such as those described in U.S. Patent Nos.4,452,775, 4,667,014, 4,748,034 and 5,239,660 and (b) diffusional systems in which an active component permeates at a controlled rate from a polymer such as described in U.S. Patent Nos.3,832,253, and 3,854,480. In addition, pump-based hardware delivery systems can be used, some of which are adapted for implantation. Use of a long-term sustained release implant may be particularly suitable for treatment of chronic conditions. Long-term release, are used herein, means that the implant is constructed and arranged to deliver therapeutic levels of the active ingredient for at least 30 days, and preferably 60 days. Long-term sustained release implants are well-known to those of ordinary skill in the art and include some of the release systems described above. In some embodiments, the composition or vaccine composition described herein used for therapeutic administration must be sterile. Sterility is readily accomplished by filtration through sterile filtration membranes (e.g., 0.2 micron membranes). Alternatively, preservatives can be used to prevent the growth or action of microorganisms. Various preservatives are well known and include, for example, phenol and ascorbic acid. In some embodiments, the present disclosure contemplates a vaccine composition comprising a pharmaceutically acceptable injectable vehicle. The vaccines of the present disclosure may be administered in conventional vehicles with or without other standard carriers, in the form of injectable solutions or suspensions. The added carriers might be selected from agents that elevate total immune response in the course of the immunization procedure. Liposomes have been suggested as suitable carriers. The insoluble salts of aluminum, that is aluminum phosphate or aluminum hydroxide, have been utilized as carriers in routine clinical applications in humans. Polynucleotides and polyelectrolytes and water-soluble carriers such as muramyl dipeptides have been used. Preparation of injectable vaccines of the present disclosure, includes mixing the antigen and / or the Gb3 or an analog thereof with muramyl dipeptides or other carriers. The resultant mixture may be emulsified in a mannide monooleate / squalene or squalane vehicle. Four parts by volume of squalene and / or squalane are used per part by volume of mannide monooleate. Methods of formulating vaccine compositions are well known to those of ordinary skill in the art. (Rola, Immunizing Agents and Diagnostic Skin Antigens. In: Remington's Pharmaceutical Sciences,18th Edition, Gennaro (ed.), (Mack Publishing Company 1990) pages 1389-1404). Additional pharmaceutical carriers may be employed to control the duration of action of a vaccine in a therapeutic application. Control release preparations can be prepared through the use of polymers to complex or adsorb chimeric construct. For example, biocompatible polymers include matrices of poly(ethylene-co-vinyl acetate) and matrices of a polyanhydride copolymer of a stearic acid dimer and sebacic acid. (Sherwood et al. (1992) Bio / Technology 10: 1446). The rate of release of the chimeric construct from such a matrix depends upon the molecular weight of the construct, the amount of the construct within the matrix, and the size of dispersed particles. (Saltzman et al. (1989) Biophys. J.55: 163; Sherwood et al, supra.; Ansel et al. Pharmaceutical Dosage Forms and Drug Delivery Systems, 5th Edition (Lea & Febiger 1990); and Gennaro (ed.), Remington's Pharmaceutical Sciences, 18th Edition (Mack Publishing Company 1990)). The chimeric construct can also be conjugated to polyethylene glycol (PEG) to improve stability and extend bioavailability times (e.g., Katre et al.; U.S. Pat. No.4,766,106). A subject in need thereof The present disclosure, in some aspects, provides methods and compositions of enhancing an immune response in a subject by administering Gb3 or an analog thereof. As described herein, the term “subject” to which administration is contemplated may refer to a human (i.e., male or female) of any age group, pediatric subject (e.g., neonate, infant, child, or adolescent) or adult subject (e.g., young adult, middle–aged adult, or senior adult) or non–human animal. In some embodiments, the human is a neonate, infant, adult, or an elderly human. In some embodiments, the non–human animal is a mammal, for example a primate (e.g., cynomolgus monkey or rhesus monkey), commercially relevant mammal (e.g., cattle, pig, horse, sheep, goat, cat, or dog), or bird (e.g., commercially relevant bird, such as chicken, duck, goose, or turkey). In some embodiments, the subject is a companion animal or a research animal. In some embodiments, the non-human animal is a fish, reptile, or amphibian. The non-human animal may be a male or female at any stage of development. The non-human animal may be a transgenic animal or genetically engineered animal. A “subject in need thereof” refers to a human subject in need of treatment of a disease or in need of reducing the risk of developing a disease. In some embodiments, the subject has any of the diseases described herein (e.g., infectious disease, cancer, or allergy). In some embodiments, the subject is at risk of developing any of the diseases described herein (e.g., infectious disease, cancer, or allergy). In some embodiments, administering Gb3 and an antigen as described herein to a subject having a disease treats the disease (therapeutic use). In some embodiments, administering Gb3 and an antigen as described herein to a subject at risk of developing a disease reduces the likelihood by 20% (e.g., by 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 99% or more) of the subject developing the disease (prophylactic use). In some embodiments, a subject has or is at risk for an infectious disease caused by a pathogen (e.g., an infectious bacterium, a virus, a parasite, or a fungus). In some embodiments, a subject has or is at risk for a disease cause by a virus. In some embodiments, the virus is an adenovirus, a coronavirus, an enterovirus such as polio virus, dengue virus, Ebola virus, a herpes virus such as herpes simplex virus, cytomegalovirus and varicella-zoster, measles, mumps, rubella, hepatitis A virus, hepatitis B virus, hepatitis C virus, human papilloma virus, influenza virus, rabies, Japanese encephalitis, rotavirus, human immunodeficiency virus (HIV), respiratory syncytial virus (RSV), smallpox, yellow fever, dengue virus, or Zika virus. In some embodiments, a subject has or is at risk for an infectious disease caused by a Beta Coronavirus, such as MERS- CoV, SARS-CoV-1, or SARS-CoV-2 or an influenza virus, such as human influenza A (e.g., H1N1 or H3N1) or a human influenza B virus. In some embodiments, the virus is from a group 1 or group 2 influenza A virus. In some embodiments, a subject has or is at risk for a cancer. In some embodiments, the cancer is a hematological cancer, lung cancer, breast cancer, brain cancer, gastrointestinal cancer, liver cancer, kidney cancer, bladder cancer, pancreatic cancer, ovarian cancer, testicular cancer, prostate cancer, endometrial cancer, muscle cancer, bone cancer, neuroendocrine cancer, connective tissue cancer, head and neck cancer, or skin cancer. Administration of immunostimulatory compositions The terms “treatment,” “treat,” and “treating” refer to reversing, alleviating, delaying the onset of, or inhibiting the progress of a disease described herein. In some embodiments, treatment may be administered after one or more signs or symptoms of the disease have developed or have been observed. In other embodiments, treatment may be administered in the absence of signs or symptoms of the disease. For example, treatment may be administered to a susceptible subject prior to the onset of symptoms (e.g., in light of a history of symptoms and / or in light of exposure to a pathogen). Treatment may also be continued after symptoms have resolved, for example, to delay or prevent recurrence. Prophylactic treatment refers to the treatment of a subject who is not and was not with a disease but is at risk of developing the disease or who was with a disease, is not with the disease, but is at risk of regression of the disease. In some embodiments, the subject is at a higher risk of developing the disease or at a higher risk of regression of the disease than an average healthy member of a population. An “effective amount” of a composition described herein refers to an amount sufficient to elicit the desired biological response. An effective amount of a composition described herein may vary depending on such factors as the desired biological endpoint, the pharmacokinetics of the compound, the condition being treated, the mode of administration, and the age and health of the subject. In some embodiments, an effective amount is a therapeutically effective amount. In some embodiments, an effective amount is a prophylactic treatment. In some embodiments, an effective amount is the amount of a compound described herein in a single dose. In some embodiments, an effective amount is the combined amounts of a compound described herein in multiple doses. When an effective amount of a composition is referred herein, it means the amount is prophylactically and / or therapeutically effective, depending on the subject and / or the disease to be treated. Determining the effective amount or dosage is within the abilities of one skilled in the art. The terms “administer,” “administering,” or “administration” refers to implanting, absorbing, ingesting, injecting, inhaling, or otherwise introducing a compound described herein, or a composition thereof, in or on a subject. The composition of the vaccine composition described herein may be administered systemically (e.g., via intravenous injection) or locally (e.g., via local injection). In some embodiments, the composition of the vaccine composition described herein is administered orally, intravenously, topically, intranasally, or sublingually. Parenteral administrating is also contemplated. The term “parenteral” as used herein includes subcutaneous, intracutaneous, intravenous, intramuscular, intraarticular, intraarterial, intrasynovial, intrasternal, intrathecal, intralesional, intradermally, and intracranial injection or infusion techniques. In some embodiments, the administering is done intramuscularly, intradermally, orally, intravenously, topically, intranasally, intravaginally, or sublingually. In some embodiments, the composition is administered prophylactically. In some embodiments, the composition or vaccine composition is administered once or administered repeatedly (e.g., 2, 3, 4, 5, or more times). In some embodiments, the administration occurs more than once (e.g., 2, 3, 4, 5, or more times). In some embodiments, the administration occurs more than once. For multiple administrations, the administrations may be done over a period of time (e.g., 6 months, a year, 2 years, 5 years, 10 years, or longer). In some embodiments, the composition or vaccine composition is administered twice (e.g., Day 0 and Day 7, Day 0 and Day 14, Day 0 and Day 21, Day 0 and Day 28, Day 0 and Day 60, Day 0 and Day 90, Day 0 and Day 120, Day 0 and Day 150, Day 0 and Day 180, Day 0 and 3 months later, Day 0 and 6 months later, Day 0 and 9 months later, Day 0 and 12 months later, Day 0 and 18 months later, Day 0 and 2 years later, Day 0 and 5 years later, or Day 0 and 10 years later). Antigens Some aspects of the present invention relate to compositions comprising an antigen and Gb3 or an analog thereof. An “antigen” refers to an entity that is bound by an antibody or receptor, or an entity that induces the production of an antibody. In some embodiments, an antigen increases the production of antibodies that specifically binds to the antigen at one or more epitopes. In some embodiments, an antigen comprises a protein or polypeptide. Such a protein or peptide is referred to herein as an “immunogenic polypeptide.” In some embodiments, the term “antigen” encompasses nucleic acids (e.g., DNA or RNA molecules) that are immunogenic or encode immunogenic polypeptides. In some embodiments, the antigen comprises a nucleic acid encoding a protein or a polypeptide. In some embodiments, the antigen is from a microbial pathogen. For example, the antigen may comprise parts (coats, capsules, cell walls, flagella, fimbriae, and toxins) of bacteria, parasite, viruses, fungi, and other microorganisms. In some embodiments, the microbial pathogen is a bacterium, virus, parasite or fungus. In some embodiments, the antigen is a cancer-specific antigen (i.e., from a cancer). In some embodiments, a protein or polypeptide antigen is a wild type protein or polypeptide. In some embodiments, a protein or polypeptide antigen is a polypeptide variant of a wild type protein or polypeptide. The term “polypeptide variant” refers to molecules which differ in their amino acid sequence from a wild type (native) or reference sequence. Amino acid sequence variants may possess substitutions, deletions, and / or insertions at certain positions within the amino acid sequence, as compared to a wild type (native) or reference sequence. One measure of the degree of similarity between a polypeptide variant and a wild type (native) or reference sequence is the overall percentage of amino acids in the polypeptide variant that are identical to (i.e., occurring in the same position and same amino acid type as) the corresponding amino acids of the wild type (native) or reference sequence (i.e., “% identity”). In some embodiments, polypeptide variants possess at least 50% identity to a native or reference sequence. In some embodiments, variants share at least 70%, at least 80%, at least 90%, at least 95%, or at least 99% identity with a native or reference sequence. In some embodiments, a polypeptide variant encompasses covalent variants and derivatives. The term “derivative” is used synonymously with the term “variant” but generally refers to a molecule that has been modified and / or changed in any way relative to a reference molecule or starting molecule. In some embodiments, sequence tags or amino acids, such as one or more lysines, can be added to peptide sequences (e.g., at the N-terminal or C-terminal ends). Sequence tags can be used for peptide detection, purification or localization. Lysines can be used to increase peptide solubility or to allow for biotinylation. Alternatively, amino acid residues located at the carboxy and amino terminal regions of the amino acid sequence of a peptide or protein may optionally be deleted providing for truncated sequences. Certain amino acids (e.g., C-terminal or N-terminal residues) may alternatively be deleted depending on the use of the polypeptide, as for example, expression of the polypeptide as part of a larger sequence which is soluble or linked to a solid support. In some embodiments, a polypeptide variant comprises at least one substituted amino acid residue, in which an amino acid within a wild type (native) or initial polypeptide sequence is removed, and a different amino acid is inserted in its place at the same position. Substitutions may be single, where only one amino acid in the molecule has been substituted, or they may be multiple, where two or more amino acids have been substituted in the same molecule. In some embodiments, the polypeptide that includes 2, 3, 4, 5, 6, 7, 8, 9, 10, or more substitutions compared to a reference protein. In some embodiments, a polypeptide comprising substituted amino acids is an antigen. In some embodiments, a substitution is a conservative amino acid substitution. The term “conservative amino acid substitution” refers to the substitution of an amino acid that is normally present in a sequence with a different amino acid of similar size, charge, and / or polarity. Examples of conservative substitutions include the substitution of a non-polar (hydrophobic) residue such as isoleucine, valine, and leucine for another non-polar residue. Likewise, examples of conservative substitutions include the substitution of one polar (hydrophilic) residue for another such as between arginine and lysine, between glutamine and asparagine, and between glycine and serine. Additionally, the substitution of a basic residue such as lysine, arginine, or histidine for another, or the substitution of one acidic residue such as aspartic acid or glutamic acid for another acidic residue are additional examples of conservative substitutions. Examples of non-conservative substitutions include the substitution of a non-polar (hydrophobic) amino acid residue such as isoleucine, valine, leucine, alanine, methionine for a polar (hydrophilic) residue such as cysteine, glutamine, glutamic acid or lysine and / or a polar residue for a non-polar residue. In some embodiments, protein fragments, functional protein domains, and homologous proteins are used as antigens in accordance with the present disclosure. For example, an antigen may comprise any protein fragment (meaning a polypeptide sequence which is at least one amino acid residue shorter than a reference polypeptide sequence but otherwise identical) of a reference protein that is, for example, 10, 20, 30, 40, 50, 60, 70, 80, 90, 100 or greater than 100 amino acids in length. In another example, a polypeptide variant that includes a stretch of 20, 30, 40, 50, or 100 amino acids which are 40%, 50%, 60%, 70%, 80%, 90%, 95%, or 100% identical to a reference protein (e.g., a protein from a microbial pathogen) herein can be utilized in accordance with the disclosure. In some embodiments, an antigen comprises more than one (e.g., 2, 3, 4, 5, 6, 7, 8, 9, 10, or more) immunogenic proteins or polypeptides. In some embodiments, the more than one immunogenic protein or polypeptides are derived from one protein (e.g., different fragments or polypeptide variants derived from one protein). In some embodiments, the more than one (e.g., from 2, 3, 4, 5, 6, 7, 8, 9, 10, or more proteins) immunogenic proteins or polypeptides are derived from multiple proteins. In some embodiments, an antigen comprises a nucleic acid encoding an immunogenic protein or polypeptide. In some embodiments, the antigen comprises an immunogenic protein or polypeptide and a nucleic acid encoding the immunogenic protein or polypeptide. The term “nucleic acid” or “polynucleotide,” in its broadest sense, includes any compound and / or substance that comprises a polymer of nucleotides. Nucleic acids encoding immunogenic proteins or polypeptides typically comprise an open reading frame (ORF), and one or more regulatory sequences. Nucleic acids (also referred to as polynucleotides) may be or may include, for example, ribonucleic acids (RNAs), deoxyribonucleic acids (DNAs), threose nucleic acids (TNAs), glycol nucleic acids (GNAs), peptide nucleic acids (PNAs), locked nucleic acids (LNAs, including LNA having a β- D-ribo configuration, α-LNA having an α-L-ribo configuration (a diastereomer of LNA), 2′-amino-LNA having a 2′-amino functionalization, and 2′-amino- α-LNA having a 2′-amino functionalization), ethylene nucleic acids (ENA), cyclohexenyl nucleic acids (CeNA), or chimeras or combinations thereof. In some embodiments, a nucleic acid encoding an immunogenic polypeptide is a DNA (e.g., a DNA expression vector for an immunogenic protein or polypeptide). In some embodiments, the nucleic acid encoding the immunogenic polypeptide is a RNA (e.g., a messenger RNA). A “messenger RNA” (mRNA) refers to any polynucleotide that encodes a (at least one) polypeptide (e.g., a naturally occurring, non-naturally occurring, or modified polymer of amino acids) and can be translated to produce the encoded polypeptide in vitro, in vivo, in situ, or ex vivo. The basic components of an mRNA molecule typically include at least one coding region, a 5′ untranslated region (UTR), a 3′ UTR, a 5′ cap, and a poly-A tail. In some embodiments, the coding region of a nucleic acid (e.g., DNA or RNA) encoding an immunogenic polypeptide is codon optimized. Codon optimization methods are known in the art and may be used as provided herein. Codon optimization, in some embodiments, may be used to match codon frequencies in target and host organisms to ensure proper folding; bias GC content to increase mRNA stability or reduce secondary structures; minimize tandem repeat codons or base runs that may impair gene construction or expression; customize transcriptional and translational control regions; insert or remove protein trafficking sequences; remove / add post translation modification sites in encoded protein (e.g. glycosylation sites); add, remove or shuffle protein domains; insert or delete restriction sites; modify ribosome binding sites and mRNA degradation sites; adjust translational rates to allow the various domains of the protein to fold properly; or to reduce or eliminate problem secondary structures within the polynucleotide. Codon optimization tools, algorithms and services are known in the art. Non-limiting examples include services from GeneArt (Life Technologies), DNA2.0 (Menlo Park CA) and / or proprietary methods. In some embodiments, the open reading frame (ORF) sequence is optimized using optimization algorithms. In some embodiments, a codon optimized sequence shares less than 95% sequence identity to a naturally occurring or wild-type sequence (e.g., a naturally occurring or wild-type mRNA sequence encoding an immunogenic protein or polypeptide). In some embodiments, a codon optimized sequence shares less than 90% sequence identity to a naturally occurring or wild-type sequence (e.g., a naturally occurring or wild-type mRNA sequence encoding an immunogenic protein or polypeptide). In some embodiments, a codon optimized sequence shares less than 85% sequence identity to a naturally occurring or wild-type sequence (e.g., a naturally occurring or wild-type mRNA sequence encoding an immunogenic protein or polypeptide). In some embodiments, a codon optimized sequence shares less than 80% sequence identity to a naturally occurring or wild-type sequence (e.g., a naturally occurring or wild-type mRNA sequence encoding an immunogenic protein or polypeptide). In some embodiments, a codon optimized sequence shares less than 75% sequence identity to a naturally occurring or wild-type sequence (e.g., a naturally occurring or wild-type mRNA sequence encoding an immunogenic protein or polypeptide). In some embodiments, a nucleic acid encoding an immunogenic protein or polypeptide comprises one or more chemical modifications. The terms “chemical modification” and “chemically modified” refer to modification with respect to adenosine (A), guanosine (G), uridine (U), thymidine (T) or cytidine (C) ribonucleosides or deoxyribnucleosides in at least one of their position, pattern, percent or population. In some embodiments, a nucleic acid (e.g., DNA or RNA) encoding an immunogenic polypeptide comprises various (more than one) different modifications. In some embodiments, a particular region of a nucleic acid (e.g., DNA or RNA) contains one, two, or more (optionally different) nucleoside or nucleotide modifications. In some embodiments, a modified nucleic acid (e.g., DNA or RNA), when introduced into a cell or organism, exhibits reduced degradation in the cell or organism, respectively, relative to an unmodified nucleic acid. In some embodiments, a modified nucleic acid (e.g., DNA or RNA), when introduced into a cell or organism, may exhibit reduced immunogenicity in the cell or organism, respectively (e.g., a reduced innate response). A modified nucleic acid (e.g., DNA or RNA) may comprise modifications that are naturally occurring or non-naturally occurring, or the polynucleotide may comprise a combination of naturally occurring and non-naturally occurring modifications. A nucleic acid encoding an immunogenic polypeptide described herein may include any useful modification, for example, of a sugar, a nucleobase, or an inter-nucleoside linkage (e.g., to a linking phosphate, to a phosphodiester linkage or to the phosphodiester backbone). Modified nucleic acid (e.g., DNA or RNA), in some embodiments, comprise non-natural modified nucleotides that are introduced during synthesis or post-synthesis of the polynucleotides to achieve desired functions or properties. The modifications may be present on inter-nucleotide linkages, purine or pyrimidine bases, or sugars. The modification may be introduced with chemical synthesis or with a polymerase enzyme at the terminal of a chain or anywhere else in the chain. Any of the regions of a nucleic acid may be chemically modified. In some embodiments, a chemically modified nucleic acid comprises one or more modified nucleosides. A “nucleoside” refers to a compound containing a sugar molecule (e.g., a pentose or ribose) or a derivative thereof in combination with an organic base (e.g., a purine or pyrimidine) or a derivative thereof (also referred to herein as “nucleobase”). A “nucleotide” refers to a nucleoside, including a phosphate group. Modified nucleotides may by synthesized by any useful method, such as, for example, chemically, enzymatically, or recombinantly, to include one or more modified or non-natural nucleosides. Polynucleotides may comprise a region or regions of linked nucleosides. Such regions may have variable backbone linkages. The linkages may be standard phosphodiester linkages, in which case the polynucleotides would comprise regions of nucleotides. In some embodiments, a modified nucleobase is a modified cytosine. Exemplary nucleobases and nucleosides having a modified cytosine include N4-acetyl-cytidine (ac4C), 5- methyl-cytidine (m5C), 5-halo-cytidine (e.g., 5-iodo-cytidine), 5-hydroxymethyl-cytidine (hm5C), 1-methyl-pseudoisocytidine, 2-thio-cytidine (s2C), and 2-thio-5-methyl-cytidine. In some embodiments, a modified nucleobase is a modified uridine. Exemplary nucleobases and nucleosides having a modified uridine include 5-cyano uridine, and 4’-thio uridine. In some embodiments, a modified nucleobase is a modified adenine. Exemplary nucleobases and nucleosides having a modified adenine include 7-deaza-adenine, 1-methyl- adenosine (m1A), 2-methyl-adenine (m2A), and N6-methyl-adenosine (m6A). In some embodiments, a modified nucleobase is a modified guanine. Exemplary nucleobases and nucleosides having a modified guanine include inosine (I), 1-methyl-inosine (m1I), wyosine (imG), methylwyosine (mimG), 7-deaza-guanosine, 7-cyano-7-deaza-guanosine (preQ0), 7-aminomethyl-7-deaza-guanosine (preQ1), 7-methyl-guanosine (m7G), 1-methyl- guanosine (m1G), 8-oxo-guanosine, 7-methyl-8-oxo-guanosine. In some embodiments, an antigen of the present disclosure is from a microbial pathogen, e.g., from a bacterium, a mycobacterium, a fungus, a virus, a parasite, or a prion. For example, the antigen may comprise a protein or polypeptide, a nucleic acid, or a nucleic acid encoding a protein or polypeptide from the microbial pathogen. In some embodiments, the antigen may comprise a microbial pathogen (e.g., a bacterial cell, a viral particle, or a fungus cell). In some embodiments, the microbial pathogen cell is live or killed. In some embodiments, the microbial pathogen is attenuated its pathogenicity. An attenuated microbial pathogen may elicit immune response but does not cause the disease that a wild-type microbial pathogen would cause. Exemplary, non-limiting bacterial taxa, species, and strains, suitable for use in some embodiments of this disclosure include: Enterobacter spp. (e.g., Enterobacter cloacae), Salmonella spp. (e.g., Salmonella enteritidis, Salmonella typhi), Pseudomonas spp. (e.g., Pseudomonas aeruginosa, Pseudomonas pachastrellae, Pseudomonas stutzeri), Moraxella spp. (e.g., Moraxella catarrhalis), Neisseria spp. (e.g., Neisseria gonorrhoeae, Neisseria meningitidis), Helicobacter spp. (e.g., Helicobacter pylori), Stenotrophomonas spp., Vibrio spp. (e.g., Vibrio cholerae), Legionella spp. (Legionella pneumophila), Hemophilus spp. (e.g., Hemophilus influenzae), Klebsiella spp. (e.g., Klebsiella pneumoniae), Proteus spp. (e.g., Proteus mirabilis), Serratia spp. (Serratia marcescens), Bacillus spp. (e.g., Bacillus anthracis), Bordetella spp. (e.g., Bordetella pertussis), Borrelia spp. (e.g., Borrelia burgdorferi), Brucella spp. (e.g., Brucella abortus, Brucella canis, Brucella melitensis, Brucella suis), Campylobacter spp. (e.g., Campylobacter jejuni), Chlamydia spp., Chlamydophila spp. (e.g., Chlamydia pneumoniae, Chlamydia trachomatis, Chlamydophila psittaci), Clostridium spp. (e.g., Clostridium botulinum, Clostridium difficile, Clostridium perfringens, Clostridium tetani), Corynebacterium spp. (e.g., Corynebacterium diphtheriae), Enterococcus spp. (e.g., Enterococcus faecalis, Enterococcus faecium), Escherichia spp. (e.g., Escherichia coli, Enterotoxic E. coli, enteropathogenic E. coli; E. coli O157:H7); Francisella spp. (e.g., Francisella tularensis), Leptospira spp. (e.g., Leptospira interrogans), Listeria spp. (e.g., Listeria monocytogenes), Mycobacterium spp. (e.g., Mycobacterium leprae, Mycobacterium tuberculosis, Mycobacterium ulcerans), Mycoplasma spp. (e.g., Mycoplasma pneumoniae), Rickettsia spp. (e.g., Rickettsia rickettsii), Shigella spp. (e.g., Shigella sonnei), Staphylococcus spp. (e.g., Staphylococcus aureus, Staphylococcus epidermidis, Staphylococcus saprophyticus), Streptococcus spp. (e.g., Streptococcus agalactiae, Streptococcus pneumoniae, Streptococcus pyogenes), Treponema spp. (e.g., Treponema pallidum), Pseudodiomarina spp.( e.g., P. maritima), Marinobacter spp. (e.g., Marinobacter hydrocarbonoclasticus, Marinobacter vinifirmus), Alcanivorax spp. (e.g., alcanivorax dieselolei), Acetinobacter spp. (e.g., A. venetianus), Halomonas spp. (e.g., H. shengliensis), Labrenzia spp., Microbulifer spp. (e.g., M. schleiferi), Shewanella spp. (e.g., S. algae), Vibrio spp. (e.g., Vibrio cholerae, Vibrio alginolyticus, Vibrio hepatarius), and Yersinia spp. (e.g., Yersinia pestis). In some embodiments, the bacterium is Bacillus anthracis (causing anthrax), Bordetella pertussis (causing whooping cough), Corynebacterium diphtheriae (causing diphtheria), Clostridium tetani (causing tetanus), Haemophilus influenzae type b, Pneumococcus spp., (causing pneumococcal infections), Streptococcus spp., Staphylococci spp. (including Group A or B streptococci), Mycobacterium spp. (e.g., Mycobacterium tuberculosis), Neiserria spp. (e.g., Neiserria meningitidis - causing meningococcal disease), Salmonella typhi (causing typhoid), Vibrio cholerae (causing Cholera), or Yersinia pestis (causing plague). In some embodiments, an antigen is derived from a Gram-negative bacterium. In some embodiments, the antigen comprises a lipopolysaccharide endotoxin (LPS) from a Gram-negative bacterium. A “lipopolysaccharide endotoxin (LPS)” refers to a large molecule consisting of a lipid and a polysaccharide composed of O-antigen, outer core and inner core joined by a covalent bond. LPS is found in the outer membrane of Gram-negative bacteria. Non-limiting examples of gram-negative bacterial species include: Neisseria species including Neisseria gonorrhoeae and Neisseria meningitidis, Branhamella species including Branhamella catarrhalis, Escherichia species including Escherichia coli, Enterobacter species, Proteus species including Proteus mirabilis, Pseudomonas species including Pseudomonas aeruginosa, Pseudomonas mallei, and Pseudomonas pseudomallei, Klebsiella species including Klebsiella pneumoniae, Salmonella species, Shigella species, Serratia species, Acinetobacter species; Haemophilus species including Haemophilus influenzae and Haemophilus ducreyi; Brucella species, Yersinia species including Yersinia pestis and Yersinia enterocolitica, Francisella species including Francisella tularensis, Pasturella species including Pasteurella multocida, Vibrio cholerae, Flavobacterium species, Meningosepticum, Campylobacter species including Campylobacter jejuni, Chlamydia species including Chlamydia trachomatis, Bacteroides species (oral, pharyngeal) including Bacteroides fragilis, Fusobacterium species including Fusobacterium nucleatum, Calymmatobacterium granulomatis, Streptobacillus species including Streptobacillus moniliformis, Legionella species including Legionella pneumophila. In some embodiments, an antigen is derived from a Gram-positive bacterium. Exemplary Gram-positive bacteria include, but are not limited to, Staphylococcus spp., Streptococcus spp., Micrococcus spp., Peptococcus spp., Peptostreptococcus spp., Enterococcus spp., Bacillus spp., Clostridium spp., Lactobacillus spp., Listeria spp., Erysipelothrix spp., Propionibacterium spp., Eubacterium spp., Corynebacterium spp., Capnocytophaga spp., Bifidobacterium spp., and Gardnerella spp.. In some embodiments, the Gram-positive bacterium is a bacterium of the phylum Firmicutes. In some embodiments, the Gram-positive bacterium is Streptococcus. Other types of bacteria include acid-fast bacilli, spirochetes, and actinomycetes. Examples of acid-fast bacilli include Mycobacterium species including Mycobacterium tuberculosis and Mycobacterium leprae. Examples of spirochetes include Treponema species including Treponema pallidum, Treponema pertenue, Borrelia species including Borrelia burgdorferi (Lyme disease), and Borrelia recurrentis, and Leptospira species. Examples of actinomycetes include: Actinomyces species including Actinomyces israelii, and Nocardia species including Nocardia asteroides. Examples of viruses include but are not limited to: Retroviruses, human immunodeficiency viruses including HIV-1, HDTV-III, LAVE, HTLV-III / LAV, HIV-III, HIV- LP, Cytomegaloviruses (CMV), Picornaviruses, polio viruses, hepatitis A virus, enteroviruses, human Coxsackie viruses, rhinoviruses, echoviruses, Calciviruses, Togaviruses, equine encephalitis viruses, rubella viruses, Flaviruses, dengue viruses, encephalitis viruses, yellow fever viruses, Coronaviruses, Rhabdoviruses, vesicular stomatitis viruses, rabies viruses, Filoviruses, Ebola virus, Paramyxoviruses, parainfluenza viruses, mumps virus, measles virus, respiratory syncytial virus (RSV), Orthomyxoviruses, influenza viruses, Bungaviruses, Hantaan viruses, phleboviruses and Nairo viruses, Arena viruses, hemorrhagic fever viruses, reoviruses, orbiviruses, rotaviruses, Birnaviruses, Hepadnaviruses, Hepatitis B virus, parvoviruses, Papovaviridae, papilloma viruses, polyoma viruses, Adenoviruses, Herpesviruses including herpes simplex virus 1 and 2, varicella zoster virus, Poxviruses, variola viruses, vaccinia viruses, Irido viruses, African swine fever virus, delta hepatitis virus, non-A, non-B hepatitis virus, Hepatitis C, Norwalk viruses, astroviruses, and unclassified viruses. In some embodiments, the virus is adenovirus, enterovirus such as poliomyelitis (polio), Ebola virus, herpes viruses such as herpes simplex virus, cytomegalovirus and varicella-zoster (chickenpox and shingles), measles, mumps, rubella, hepatitis-A, -B, or-C, human papilloma virus, Influenza virus, rabies, Japanese encephalitis, rotavirus, human immunodeficiency virus (HIV), respiratory syncytial virus (RSV), smallpox, yellow fever, or Zika Virus. In some embodiments, an antigen comprises a viral protein and / or a nucleic acid encoding a viral protein (e.g., a viral structural or non-structural protein). In some embodiments, the antigen is a viral antigen (e.g., a viral protein or fragment thereof). In some embodiments, the antigen comprises a nucleic acid encoding the viral genome. In some embodiments, the viral genome is modified to produce a modified virus that is attenuated. In some embodiments, the antigen comprises a live attenuated, inactivated, or killed virus. In some embodiments, an antigen comprises a viral antigen from an adenovirus, a coronavirus, an enterovirus such as polio virus, dengue virus, Ebola virus, a herpes viruses such as herpes simplex virus, cytomegalovirus and varicella-zoster, measles, mumps, rubella, hepatitis A virus, hepatitis B virus, hepatitis C virus, human papilloma virus, influenza virus, rabies, Japanese encephalitis, rotavirus, human immunodeficiency virus (HIV), respiratory syncytial virus (RSV), smallpox, yellow fever, dengue virus, or Zika virus. In some embodiments the antigen is from an influenza virus. In some embodiments, the antigen is an antigen from a human influenza A or a human influenza B virus. In some embodiments, the antigen is an antigen from a group 1 or group 2 influenza A virus. In some embodiments, the antigen is a group 1 or group 2 influenza A hemagglutinin (HA) protein, or an immunogenic fragment thereof. In some embodiments, the antigen from an influenza virus is selected from, but not limited to Hemagglutinin (HA), Neuraminidase (NA), Nucleoprotein (NP), M1 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. In some embodiments, an antigen comprises a protein and / or a nucleic acid encoding a viral protein from a Beta Coronavirus, such as MERS-CoV, SARS-CoV-1, or SARS-CoV-2. In some embodiments, the antigen comprises a spike protein, envelope protein, membrane protein, or nucleocapsid protein from a Beta Coronavirus, and / or a nucleic acid encoding a spike protein, envelope protein, membrane protein, or nucleocapsid protein from a Beta Coronavirus. In some embodiments, the antigen comprises an immunogenic fragment of a protein from a Beta Coronavirus, and / or a nucleic acid encoding an immunogenic fragment of a protein from a Beta Coronavirus (e.g., a receptor binding domain (RBD) of Beta coronavirus spike protein). In some embodiments, the antigen comprises a MERS-CoV, SARS-CoV-1, or SARS-CoV-2 spike protein, or an immunogenic fragment thereof. In some embodiments, an antigen comprises a live attenuated, inactivated, or killed MERS-CoV, SARS-CoV-1, or SARS-CoV-2 virus. In some embodiments the coronavirus antigen is selected from, but not limited to, spike proteins S, envelope proteins E, membrane proteins M, nucleocapsid proteins N. Examples of fungus include, but are not limited to: Cryptococcus species including Crytococcus neoformans, Histoplasma species including Histoplasma capsulatum, Coccidioides species including Coccidiodes immitis, Paracoccidioides species including Paracoccidioides brasiliensis, Blastomyces species including Blastomyces dermatitidis (causing sporotrichosis), Candida species including Candida albicans, Sporothrix species including Sporothrix schenckii, Aspergillus species, Cryptococcus species, Mucormycete, Blastomyces dermatitidis (causing blastomycosis), or endemic mycosis causing fungus such as Histoplasma capsulatum (causing histoplasmosis) and fungi of mucormycosis. Other infectious organisms include, without limitation: parasites. Parasites include Plasmodium species, such as Plasmodium species including Plasmodium falciparum, Plasmodium malariae, Plasmodium ovale, Plasmodium vivax, Toxoplasma gondii. Blood-borne and / or tissue-borne parasites include Plasmodium species, Babesia species including Babesia microti and Babesia divergens, Leishmania species including Leishmania tropica, Leishmania species, Leishmania braziliensis, Leishmania donovani, Trypanosoma species including Trypanosoma gambiense, Trypanosoma rhodesiense (African sleeping sickness), and Trypanosoma cruzi (Chagas' disease). In some embodiments, the parasite is a Plasmodium spp., Leishmania, or a helminth. Other medically relevant microorganisms have been described extensively in the literature, e.g., see C. G. A Thomas, Medical Microbiology, Bailliere Tindall, Great Britain 1983, incorporated herein by reference. In some embodiments, an antigen of the present disclosure comprises a cancer-specific antigen and / or a nucleic acid encoding such. A “cancer-specific antigen” refers to a protein that is specifically expressed or upregulated in a cancer cell, as compared to non-cancerous cells of the same origin. A cancer-specific antigen, or an epitope derived thereof, can be recognized by the immune system to induce an immune response against the cancer. Classes of proteins that may be cancer-specific antigen include, without limitation: enzymes, receptors, and transcription factors. A large number of proteins that are specifically expressed in cancer cells or are upregulated in cancer cells have been identified (Hassane et al., Holland-Frei Cancer Medicine. 6th Edition, incorporated herein by reference). Known cancer-specific antigens are classified into different classes: cancer / testis antigens (e.g., MAGE family members or NY-ESO-1), differentiation antigens (e.g., tyrosinase and Melan-A / MART-1 for melanoma, and PSA for prostate cancer), overexpressed cancer-specific antigens (e.g., Her-2 / neu, Survivin, Telomerase and WT1), cancer-specific antigens arising from mutations of normal genes (e.g., mutated β- catenin or CDK4), cancer-specific antigens arising from abnormal post-translational modifications (e.g., altered glycosylation patterns) that lead to novel epitopes in tumors (e.g., MUC1), and oncoviral proteins (e.g., human papilloma type 16 virus proteins, E6 and E7). In some embodiments, the tumor-specific antigen is expressed in a broad range of different types of cancers. In some embodiments, the tumor-specific antigen is expressed only in one or relatively few types of cancer. In some embodiments, an antigen comprises a fragment or an epitope derived from a cancer-specific antigen and / or a nucleic acid encoding such. For example, the fragment or an epitope derived from a cancer-specific antigen may be 5-40 amino acids long. In some embodiments, the fragment or an epitope derived from a cancer-specific antigen is 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, or 40 amino acids long. In some embodiments, a fragment or epitope derived from a cancer-specific antigen is a heteroclitic epitope. A “heteroclitic epitope” refers to an altered version of an endogenous peptide sequence (i.e., an analog) from a cancer-specific antigen engineered to elicit potent immune reactions. Heteroclitic epitopes have increased stimulatory capacity or potency for a specific T cell, as measured by an increased response to a given dose, or by requiring a lesser amount of the epitope to achieve the same response. Heteroclitic epitopes may therefore be beneficial as vaccine components since these epitopes induce T cell responses stronger than those induced by the native epitope. In some embodiments, a heteroclitic epitope comprises modifications, e.g., amino acid substitutions, as compared to the native sequence in the cancer-specific antigen. In some embodiments, the heteroclitic epitope comprises more than one amino acid substitution (e.g., 2, 3, 4, 5, or more substitutions) compared to the native sequence of the cancer-specific antigen it is derived from. In some embodiments, a heteroclitic epitope is at least 60%, at least 70%, at least 80%, at least 90%, at least 98%, or at least 99% identical to the native sequence that it is derived from. In some embodiments, a heteroclitic epitope is 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 98%, or 99% identical to the native sequence that it is derived from. In some embodiments, a heteroclitic epitope is more immunogenic than a peptide of its native sequence. For example, a heteroclitic epitope may be at least 30% more immunogenic (i.e., induces a stronger immune response) than its corresponding native peptide. In some embodiments, a heteroclitic epitope may be at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 100%, at least 2-fold, at least 3-fold, at least 4- fold, at least 5-fold, at least 6-fold, at least 7-fold, at least 8-fold, at least 9-fold, at least 10-fold, at least 20-fold, at least 30-fold, at least 40-fold, at least 50-fold, at least 60-fold, at least 70-fold, at least 80-fold, at least 90-fold, at least 100-fold, or more immunogenic than its corresponding native peptide. In some embodiments, the fragment or epitope derived from a cancer-specific antigen is a cryptic epitope. A “cryptic epitope” refers to an epitope derived from a cancer-specific antigen that does not necessarily undergo antigen processing / presentation and are therefore ‘hidden’ from immune recognition. Cryptic epitopes usually appear in very low concentration on antigen presenting cells (APC) and do not elicit the removal of auto-reactive T cells. Cryptic epitopes are not presented for recognition by T cells unless they are produced in unusually large concentrations or unless they are freed from the configuration of their native antigen. Cryptic epitopes derived from cancer-specific antigens may be used to break the tolerance of T cells to the tumor and induce potent immune response against the tumor. Such principles have been described in Pardoll, et al., PNAS, Vol.96, pp.5340–5342 (1999), the entire contents of which are incorporated herein by reference. In some embodiments, a cryptic epitope is generated from translation of a non-coding region of the cancer-specific antigen gene or translation of a different reading frame of a coding region of the cancer-specific antigen. A cryptic epitope may be more immunogenic (i.e., induces a stronger immune response) than any native peptide derived from the cancer-specific antigen. For example, a cryptic epitope may be at least 30% more immunogenic than any native peptide derived from the cancer-specific antigen. In some embodiments, a cryptic epitope is at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 100%, at least 2-fold, at least 3-fold, at least 4-fold, at least 5-fold, at least 6-fold, at least 7-fold, at least 8- fold, at least 9-fold, at least 10-fold, at least 20-fold, at least 30-fold, at least 40-fold, at least 50- fold, at least 60-fold, at least 70-fold, at least 80-fold, at least 90-fold, at least 100-fold, or more immunogenic than any native peptide derived from the cancer-specific antigen. One skilled in the art is familiar with how to assess the immune response induced by an antigen, e.g., measuring antibody titers. In some embodiments, a cancer-specific antigen is a neoantigen. A “neoantigen” refers to an antigen generated via random somatic mutations occurring in cancer cells and are thus specific to the lineage of the cancer cells it is derived from. Neoantigens are regarded in the art to be responsible for the immunogenicity of tumors (Srivastava et al., 1993, Duan et al., 2009; van der Bruggen et al., 2013, incorporated herein by reference), and mathematic modeling has predicted the existence of tens to hundreds of neoepitopes (epitopes derived from neoantigens) in individual human tumors (Srivastava 2009, incorporated herein by reference). The recent revolution in high- throughput DNA sequencing and accompanying bioinformatics approaches has finally made it possible to actually identify the individually specific neoepitopes in individual cancers. In some embodiments, an antigen described herein is an antigen designed to provide broad heterologous protection against a range of pathogens. Heterologous immunity refers to the phenomenon whereby a history of an immune response against a stimulus or pathogen can provide a level of immunity to a second unrelated stimulus or pathogen (e.g., as described in Chen et al., Virology 2015482: 89-97, incorporated herein by reference). For example, an antigen that induces cross-reactive memory CD8+ T cells against multiple unrelated viruses such as influenza A and Epstein-Barr Virus (EBV), as described in Watkin et al., J Allerg Clin Immunol 2017 Oct; 140(4) 1206-1210, incorporated herein by reference. In some embodiments, the compound of Formula (I) or Formula (II) induces and / or enhances antibody-mediated heterologous protection. Polypeptide or polynucleotide molecules of the present disclosure may share a certain degree of sequence similarity or identity with reference molecules (e.g., reference polypeptides or reference polynucleotides), for example, wild-type molecules. The term “identity” as known in the art, refers to a relationship between the sequences of two or more polypeptides or polynucleotides, as determined by comparing the sequences. In the art, identity also means the degree of sequence relatedness between them as determined by the number of matches between strings of two or more amino acid residues or nucleic acid residues. Identity measures the percent of identical matches between the smaller of two or more sequences with gap alignments (if any) addressed by a particular mathematical model or computer program (e.g., “algorithms”). Identity of related peptides can be readily calculated by known methods. “% identity” as it applies to polypeptide or polynucleotide sequences is defined as the percentage of residues (amino acid residues or nucleic acid residues) in the candidate amino acid or nucleic acid sequence that are identical with the residues in the amino acid sequence or nucleic acid sequence of a second sequence after aligning the sequences and introducing gaps, if necessary, to achieve the maximum percent identity. Methods and computer programs for the alignment are well known in the art. It is understood that identity depends on a calculation of percent identity but may differ in value due to gaps and penalties introduced in the calculation. Generally, variants of a particular polynucleotide or polypeptide have at least 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% but less than 100% sequence identity to that particular reference polynucleotide or polypeptide as determined by sequence alignment programs and parameters described herein and known to those skilled in the art. Such tools for alignment include those of the BLAST suite (Stephen F. Altschul, et al (1997), "Gapped BLAST and PSI-BLAST: a new generation of protein database search programs", Nucleic Acids Res.25:3389-3402). Another popular local alignment technique is based on the Smith-Waterman algorithm (Smith, T.F. & Waterman, M.S. (1981) “Identification of common molecular subsequences.” J. Mol. Biol.147:195-197.) A general global alignment technique based on dynamic programming is the Needleman–Wunsch algorithm (Needleman, S.B. & Wunsch, C.D. (1970) “A general method applicable to the search for similarities in the amino acid sequences of two proteins.” J. Mol. Biol.48:443-453.). More recently a Fast Optimal Global Sequence Alignment Algorithm (FOGSAA) has been developed that purportedly produces global alignment of nucleotide and protein sequences faster than other optimal global alignment methods, including the Needleman–Wunsch algorithm. Other tools are described herein, specifically in the definition of “identity” below. As used herein, the term “homology” refers to the overall relatedness between polymeric molecules, e.g., between nucleic acid molecules (e.g., DNA molecules and / or RNA molecules) and / or between polypeptide molecules. Polymeric molecules (e.g., nucleic acid molecules (e.g., DNA molecules and / or RNA molecules) and / or polypeptide molecules) that share a threshold level of similarity or identity determined by alignment of matching residues are termed homologous. Homology is a qualitative term that describes a relationship between molecules and can be based upon the quantitative similarity or identity. Similarity or identity is a quantitative term that defines the degree of sequence match between two compared sequences. In some embodiments, polymeric molecules are considered to be “homologous” to one another if their sequences are at least 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, or 99% identical or similar. The term “homologous” necessarily refers to a comparison between at least two sequences (polynucleotide or polypeptide sequences). Two polynucleotide sequences are considered homologous if the polypeptides they encode are at least 50%, 60%, 70%, 80%, 90%, 95%, or even 99% for at least one stretch of at least 20 amino acids. In some embodiments, homologous polynucleotide sequences are characterized by the ability to encode a stretch of at least 4–5 uniquely specified amino acids. For polynucleotide sequences less than 60 nucleotides in length, homology is determined by the ability to encode a stretch of at least 4–5 uniquely specified amino acids. Two protein sequences are considered homologous if the proteins are at least 50%, 60%, 70%, 80%, or 90% identical for at least one stretch of at least 20 amino acids. Homology implies that the compared sequences diverged in evolution from a common origin. The term “homolog” refers to a first amino acid sequence or nucleic acid sequence (e.g., gene (DNA or RNA) or protein sequence) that is related to a second amino acid sequence or nucleic acid sequence by descent from a common ancestral sequence. The term “homolog” may apply to the relationship between genes and / or proteins separated by the event of speciation or to the relationship between genes and / or proteins separated by the event of genetic duplication. “Orthologs” are genes (or proteins) in different species that evolved from a common ancestral gene (or protein) by speciation. Typically, orthologs retain the same function in the course of evolution. “Paralogs” are genes (or proteins) related by duplication within a genome. Orthologs retain the same function over the course of evolution, whereas paralogs can evolve new functions, even if these are related to the original one. The term “identity” refers to the overall relatedness between polymeric molecules, for example, between polynucleotide molecules (e.g., DNA molecules and / or RNA molecules) and / or between polypeptide molecules. Calculation of the percent identity of two polynucleic acid sequences, for example, can be performed by aligning the two sequences for optimal comparison purposes (e.g., gaps can be introduced in one or both of a first and a second nucleic acid sequences for optimal alignment and non-identical sequences can be disregarded for comparison purposes). In some embodiments, the length of a sequence aligned for comparison purposes is at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, or 100% of the length of the reference sequence. The nucleotides at corresponding nucleotide positions are then compared. When a position in the first sequence is occupied by the same nucleotide as the corresponding position in the second sequence, then the molecules are identical at that position. The percent identity between the two sequences is a function of the number of identical positions shared by the sequences, taking into account the number of gaps, and the length of each gap, which needs to be introduced for optimal alignment of the two sequences. The comparison of sequences and determination of percent identity between two sequences can be accomplished using a mathematical algorithm. For example, the percent identity between two nucleic acid sequences can be determined using methods such as those described in Computational Molecular Biology, Lesk, A. M., ed., Oxford University Press, New York, 1988; Biocomputing: Informatics and Genome Projects, Smith, D. W., ed., Academic Press, New York, 1993; Sequence Analysis in Molecular Biology, von Heinje, G., Academic Press, 1987; Computer Analysis of Sequence Data, Part I, Griffin, A. M., and Griffin, H. G., eds., Humana Press, New Jersey, 1994; and Sequence Analysis Primer, Gribskov, M. and Devereux, J., eds., M Stockton Press, New York, 1991; each of which is incorporated herein by reference. For example, the percent identity between two nucleic acid sequences can be determined using the algorithm of Meyers and Miller (CABIOS, 1989, 4:11-17), which has been incorporated into the ALIGN program (version 2.0) using a PAM120 weight residue table, a gap length penalty of 12 and a gap penalty of 4. The percent identity between two nucleic acid sequences can, alternatively, be determined using the GAP program in the GCG software package using an NWSgapdna.CMP matrix. Methods commonly employed to determine percent identity between sequences include, but are not limited to those disclosed in Carillo, H., and Lipman, D., SIAM J Applied Math., 48:1073 (1988); incorporated herein by reference. Techniques for determining identity are codified in publicly available computer programs. Exemplary computer software to determine homology between two sequences include, but are not limited to, GCG program package, Devereux, J., et al., Nucleic Acids Research, 12(1), 387 (1984)), BLASTP, BLASTN, and FASTA Altschul, S. F. et al., J. Molec. Biol., 215, 403 (1990)). EXAMPLES Example 1 – Gb3 abundance fosters the GC reaction To generate a system that allows for the modulation of Gb3 levels, mice that lacked the key enzymes involved in synthesis (α1,4-galactosyltransferase; A4Galt) or degradation (α- galactosidase A; αGalA) of Gb3 were used (FIG.5A). To calibrate this model for Gb3 abundance, C57BL / 6 (WT), A4galt-KO, and Gla-KO mice were immunized intraperitoneally with 4- hydroxyl-3-nitrophenylacetyl coupled to ovalbumin (NP-OVA) (FIG.1A) and the number of Gb3-positive naive B cells, GC B cells, and differentiated plasma cells was determined 10 days after immunization. Among the different B cell populations, Gb3 expression was restricted to GC B cells and lacking in naive B and plasma cells (FIGs.5B-5D). In addition to GC B cells, Gb3 was also detected in splenic CD11bposclassical dendritic cells (cDC2), albeit at lower levels (FIG. 5E). Whereas A4galt-KO mice expectedly failed to express Gb3, WT and Gla-KO animals showed ~20% and 50% Gb3posGC B cells (FIGs.5F-5G). Thus, A4galt-KO, WT, and Gla-KO mice represent Gb3-deficient, homeostatic, and Gb3-abundant conditions, respectively, and hence are a suitable model to test the functional impact of various Gb3 levels on GC responses. Following NP-OVA immunization, the magnitude of GC formation and plasma cell differentiation were quantified. Elevated Gb3 abundance in Gla-KO mice led to increased numbers of GCs as well as amplified GC B cell and plasma cell frequencies in the spleen when compared to WT animals (FIGs.1B and 1C). By contrast, Gb3-deficient A4galt-KO mice lacked proper GC organization and exhibited poor differentiation of GC B lymphocytes into plasma cells (FIGs.1B and 1C). In addition, a low frequency of NP-specific IgG-secreting plasma cells were observed in the absence of Gb3, while these were increased in Gla-KO animals compared to WT (FIG.1H). Moreover, Tfh cell numbers in the spleen correlated with Gb3 levels, with an increase in Gla-KO and reduction in A4galt-deficient animals (FIG.1I). Notably, mice abundant in Gb3 showed higher titers of total IgG as well as IgG2c compared to WT, while A4galt-KO animals lacked IgG2c class switch (FIG.1D). Since WT and A4galt-KO mice showed similar levels of total IgG, antibody maturation was measured by quantifying avidity and affinity of antigen-antibody complexes. Accordingly, antibodies from A4galt-KO mice had low avidity, as indicated by the quick denaturation of antigen-antibody complexes in the presence of 2M NaSCN (FIG.1E). Furthermore, antibodies from A4galt-KO serum showed weak binding to BSA substituted with a low number of NP residues, indicating poor affinity (FIG.1F). By contrast, antibodies from Gb3-abundant mice exhibited significantly increased antigen-binding avidity (FIG.1E), while there was no difference between WT and Gla- KO mice for NP-specific affinities (FIG.1F). To perform an in-depth analysis of the BCR repertoire in GC B cells, the Rep-SHM-Seq method was used to detect specific BCR usage and assess somatic hypermutation (SHM) patterns in enriched clonotypes after NP-OVA immunization, where ≥90% nucleic acid sequence similarity in the CDR3 region was used as cutoff to define a clonotype. To examine heavy chain variable gene segment (VH) enrichment, VHusage of GC B cells was compared with naive B lymphocytes. In line with previous studies, there was significant usage of NP-specific VH1-72 in GC B cells compared to naive B lymphocytes in all immunized mice of the different genotypes, while there was no significant difference in other VHsegments studied (FIG.6). VH1-72 rearrangement in GC B cells generated three dominant clonotypes in all animal groups (FIG.1G), where a clonotype is considered as enriched in one sample if it makes up more than 0.3% of all productive junctions. Since Rep-SHM-Seq detects both productive and non-productive V(D)J sequences, a database of intrinsic SHM patterns of non-productive VH1-72 sequences for each genotype was generated. These intrinsic mutations were then compared with the SHM frequencies of the dominant VH1-72 clonotypes in order to identify their level of affinity maturation as described. The mutation analysis of clonotypes showed that dominant VH1-72 B cell clones from all mice showed a G-to-T point mutation at residue 98 of CDR1, which corresponded to the mutation W33L that affords high affinity for NP- antigen in mice on C57BL / 6 background. While there was no difference in the frequencies of W33L mutations in WT and Gla-KO mice, A4galt-deficient GC B cells showed lower frequencies of the high-affinity W33L mutation in all dominant VH1-72 clonotypes (FIG.1H and 1I). To determine if low VH1-72 SHM frequencies in B cells that lack Gb3 were due to an overall lower mutational burden based on differential activation-induced cytidine deaminase (AID) activity, the total number of mutations in all clonotypes that appeared in GCs was quantified. Interestingly, the total number of mutations in A4galt-KO were higher than in WT and Gla-KO GC B cells. However, when mutation frequencies in enriched clones were compared, it was determined that less dominant clones had more mutations in Gb3-deficient animals, while expanded clones had higher mutation rates in WT and Gb3-abundant mice (FIG.1J). Altogether, this suggests Gb3 abundance expands GC B cells, plasma and Tfh cells, and mice lacking Gb3 show poor antibody affinity maturation and reduced mutation frequencies in dominant BCR clonotypes. Since an increased number of GC B cells in Gla-KO mice was observed, it was assessed whether Gb3 provided a competitive advantage for B cell expansion during the GC reaction. For this purpose, mixed bone marrow chimera was generated using irradiation of recipient C57BL / 6.SJL mice followed by reconstitution with donor bone marrow from either WT, Gla-KO, or A4galt-KO mice (CD45.2+). In parallel, twofold the number of bone marrow cells from CD45.1-congenic animals was used as competitive WT control (FIG.7A). Using this model, it was determined that Gb3-abundant GC B cells outcompeted cells from WT origin, while B cells lacking Gb3 showed poor expansion during the GC response (FIG.7B). Performing cell surface staining for antibody isotypes, GC B cells derived from Gla-KO bone marrow exhibited an increased proportion of IgG2c-expressing cells when compared to the respective WT controls (FIG.7C). To further investigate the intrinsic effect of Gb3 during GC reactions, naïve B cells were transferred from WT, Gla-KO, or A4galt-KO mice to muMT-KO animals, which lacked mature B cells, and the GC response was quantified 14 days after immunization with NP-OVA (FIG.7D). It was determined that the transfer of Gb3-abundant B cells resulted in higher GC B cell numbers as well as higher IgG and IgG2c titers in the serum when compared to WT, while the GC B cells derived from Gb3-deficient mice led to weak IgG2c induction (FIGs.7E and 7F). Overall, these findings suggest that the expansion of GC B cells and IgG2c induction are a B cell intrinsic function of Gb3. Example 2 – Gb3 binds to CD19 to boost BCR signaling Within germinal centers, centroblasts in the dark zone undergo extensive proliferation as well as somatic hypermutation. Subsequently, centroblasts transition into the light zone to become centrocytes, which recognize antigen presented on follicular dendritic cells (FDCs) and receive stimulation from Tfh cells. These interactions determine the fate of GC B cell selection, leading either to plasma and memory B cell differentiation or, alternatively, to re-entry into the dark zone for further affinity maturation. Since the transition between dark and light zone is critical for effective humoral responses, the impact of Gb3 on the composition of centroblasts and centrocytes was examined. Analyzing GC B cells for the centroblast marker CXCR4 and the centrocyte molecule CD83, it was determined that centroblast / centrocyte transition was severely hampered in the absence of Gb3 (FIGs.2A and 2B). This suggests that the lipid Gb3 is crucial for proper positioning of GC B cells in the light zone to allow for productive selection processes to occur. GC B cell proliferation in the dark zone in response to BCR activation is mainly regulated by the transcription factor Foxo1. CD19 positively regulates BCR signaling, and cross-linking of BCR with CD19 reduces the activation threshold of the BCR by sustaining it in lipid rafts and reducing its internalization. Furthermore, mice either deficient in CD19 or containing loss-of- function mutations at two signaling tyrosine residues (Y482F and Y513F) lack selection of antigen-specific antibodies. Phosphorylation of Y482 / Y513 residues mediates the association of CD19 with PI3K, and the activation of the PI3K-Akt pathway leads to Foxo1 phosphorylation and triggers its proteasomal degradation, thus terminating the Foxo1-dependent gene signature that includes CXCR4 expression. An accumulation of CXCR4-expressing centroblasts in Gb3 deficiency was observed, therefore, the impact of Gb3 on BCR signaling and downstream activation of the PI3K / Akt / Foxo1 pathway was explored. GC B cells were isolated from the different mouse models and subjected them to BCR ligation with anti-F(ab)2 antibodies, prior to analyzing the phosphorylation of signaling molecules using immunoblot. Modulation of Gb3 abundance had no differential effect on phosphorylation in the proximal signal cascade, involving CD79b and Syk (FIG.2C). However, Gb3-abundant GC B cells showed strong CD19 downstream signaling, markedly higher phosphorylation of Akt and consequently low expression of total Foxo1 (FIG.2C). In contrast, CD19 downstream signaling was compromised in Gb3- deficient GC B cells, as they exhibited diminished phosphorylation of CD19, PI3K, and Akt. The low level of p-Akt in Gb3-deficient GC B cells resulted in impaired phosphorylation and concomitant accumulation of total Foxo1 (FIG.2C). Taken together, these data suggest Gb3 activates the CD19-PI3K-Akt axis, leading to Foxo1 degradation, which corresponds to CXCR4 downregulation and centroblast / centrocyte transition. GC B cells exhibit pronounced phosphatase activity and transient activation of kinases after BCR cross-linking, which makes the phosphorylation of signaling molecules a delicate process. In this context, was possible that the lipid Gb3 might facilitate the physical proximity of the BCR to its co-receptor CD19 to allow for its efficient activation. To this end, the interaction between BCR and CD19 was explored using proximity ligation assays (PLA). GC B cells from A4galt-KO mice showed a lower PLA signal than those from WT animals, demonstrating a decreased BCR-CD19 proximity in the absence of Gb3 (FIG.2D). By contrast, the PLA signal was significantly augmented in Gla-KO GC B cells, indicating that Gb3 abundance amplifies the spatial relationship between CD19 and the BCR (FIG.2D). In the BCR downstream signaling cascade, PI3K is physically recruited to the cytoplasmic tail of CD19. Performing PLA, GC B cells abundant in Gb3 showed increased interaction between CD19 and PI3K after BCR cross-linking (FIG.2D). Most notably, the PLA signal in A4galt-deficient GC B cells was virtually abolished (FIG.2D), suggesting that the lipid Gb3 is critically required for PI3K recruitment to CD19. Furthermore, PLA between Gb3 and CD19 revealed a direct interaction between the lipid and the co-receptor (FIG.2E), which indicated that direct interaction with Gb3 promotes the clustering of CD19 with the BCR complex and consequently amplifies CD19 downstream signaling after BCR stimulation. It was assessed whether the lipid Gb3 could exert a direct effect on GC B cell stimulation and whether the carbohydrate headgroup and / or the lipid tail are required for its activation- promoting properties. For this purpose, we isolated Gb3-deficient GC B cells from immunized A4galt-KO mice and cultured them in the presence of galabiaosylceramide (GA2), Gb3, globotriaosylsphingosine (Lyso-Gb3), isoglobotriaosylceramide (iGb3), globotetraosylceramide (Gb4), or a Gb3-sugar analog for two hours. GA2, iGb3, and Gb4 share a similar ceramide backbone like Gb3 and only differ in their carbohydrate headgroups. By contrast, Lyso-Gb3 and the Gb3 analog contain the same sugar headgroup as Gb3, whereas Lyso-Gb3 consists of a sphingosine base instead of the full ceramide lipid tail, and the sugar of the Gb3 analog is connected to a short alkyl chain (FIG.2F). Phosphorylation of Akt after BCR cross-linking was measured using phospho-flow (FIG.2G). Exogenous addition of Gb3, Lyso-Gb3, or the Gb3- sugar analog restored Akt activation in A4galt-deficient GC B cells, albeit at different levels (FIG. 2G). By contrast, GA2, iGb3, and Gb4 had no effect on B cell activation. These results suggest the impact of Gb3 on B cell stimulation based on its ability to reconstitute Gb3-deficient GC B cells. Furthermore, Gb3-mediated activation of BCR downstream signaling might rely on the lipid’s trisaccharide structure and not the ceramide lipid tail. The direct interaction between CD19 and different lipids was analyzed using a protein lipid overlay (PLO) assay. PVDF membranes were loaded with different concentrations of lipids, and in accordance with the phospho-flow data, Gb3 strongly bound to CD19, followed by Lyso- Gb3 and Gb3 analog (FIG.2H). No CD19 binding with GA2, iGb3, or Gb4 was observed. Next, to quantify binding affinity of Gb3 and CD19, isothermal titration calorimetry (ITC) was used, in which the lipid was injected into a reaction chamber containing recombinant CD19 in solution. Since the titration of lipid into aqueous phase is challenging in ITC and the CD19-Gb3 interaction depends on the carbohydrate headgroup, the Gb3 analog with a short alkyl chain was used for the ITC assay. Binding data revealed a specific interaction between Gb3 and CD19 with a stoichiometry of 1:1 and a dissociation constant of 4.8 µM (FIG.2I). As a further test for the direct binding of Gb3 to CD19, the competition between the known Gb3-ligand Shiga toxin subunit B (STxB) and recombinant CD19 was examined, using Gb3-coated hydrophobic ELISA. The binding data demonstrated that the interaction of Gb3 with STxB was stronger than with CD19, as preincubating the plates with STxB was sufficient to reduce Gb3-CD19 engagement (FIG.8A). The crystal structure, which resolved binding of STxB to Gb3, as well as site-directed mutagenesis studies identified the amino acid residues in STxB that are critically required for interacting with Gb3. Interestingly, STxB and the CD19 ectodomain exhibit sequence homology, suggesting that CD19 might use similar binding sites for its interaction with Gb3 (FIG.8B). Site- directed mutagenesis of CD19 was performed and mutations in three amino acid residues that correspond to established Gb3-binding sites in StxB (M1: F122A, M2: W124A, M3: G198T) were introduced. Subsequently, the binding-site mutants of CD19 were used for transfection of CD19-deficient A20 B lymphocytes, a murine B cell line that also expressed Gb3 (FIGs.2J, 8C, and 8D). Because WT and mutant CD19-transfected A20 B cells produced different levels of CD19, transfected B cells with similar CD19 expression (FIG.8D) were sorted and PLA was performed to assess the impact of CD19 mutations on Gb3 binding. Whereas the F122A and W124A substitutions did not affect the interaction of Gb3 with CD19, the G198T mutant revealed a drastically reduced PLA signal (FIG.2J), suggesting that this residue represented a crucial binding site for Gb3 interaction. This suggests Gb3 binds to CD19 and regulates its capacity for downstream signaling (FIG.2K). Example 3- Gb3-mediated IgG2c isotype switch is dependent on type I interferon signaling In addition to CD19, STxB also shows sequence similarity with the ectodomain of type I interferon receptor. Since type I interferon is important for IgG2c class switching, and as Gla-KO mice had elevated titers of IgG2c, it was assessed whether Gb3-dependent IgG2c induction was regulated via signaling through interferon α receptor (IFNAR1). Because type I interferon signaling is important for GCs to form, the impact of IFNAR1 specifically on IgG2c class switching following the initial phase of GC development was tested. To this end, anti-IFNAR1 blocking antibodies were injected into mice with ongoing GC reactions at day 6 and 8 post immunization (FIG.9A). Indeed, the amplified GC B cell response in Gb3-abundant animals was not affected by anti-IFNAR1 treatment (FIG.9B). By contrast, IFNAR1 blocking reduced the total IgG titers in Gla-deficient mice to WT levels, and IgG2c production was virtually abrogated (FIG.9C). To further validate the impact of IFNAR signaling on Gb3-mediated IgG2c class switch, Gla-deficient and Gla- / - / Ifnar- / -(double knock-out, DKO) mice were used, and IgG1- as well as IgG2c-positive GC B cells were quantified after NP-OVA immunization. Gla-deficient and DKO mice showed comparable frequencies of IgG1-expressing cells, whereas IgG2c-positive GC B cells were virtually lacking in the absence of functional IFNAR signaling in DKO mice (FIGS.9D and 9E). The titers of IgG1 and IgG2c antibodies were analyzed in serum and it was determined that IgG2c induction was specifically dependent on IFNAR signaling as a significantly reduced ratio of serum IgG2c to IgG1 was observed in DKO animals (FIG.9F). Furthermore, the effect of Gb3 on type I interferon signaling was explored and examined as a possible molecular interaction between Gb3 and IFNAR1 on GC B cells, using proximity ligation assays (PLA). Analysis based on confocal microscopy revealed elevated PLA signal for Gb3 and IFNAR1 on GC B cells isolated from Gla-KO mice compared to WT, while GC B cells from A4galt-deficient mice lacking Gb3 failed to produce any PLA signal (FIG.9G). In order to functionally investigate Gb3-mediated IFNAR1 signaling, FACS-sorted GC B cells were stimulated with IFNαand the activation of downstream kinases was assessed. Immunoblot analysis showed augmented phosphorylation of Tyk2, JAK1, STAT1, and STAT2 in GC B cells from Gb3-abundant mice when compared to WT (FIG.9H). In sharp contrast, GC B cells from Gb3-deficient animals displayed diminished activation of the respective kinases (FIG.9H). This suggests that Gb3 interaction with IFNAR1 modulates the type I interferon signaling cascade and facilitates the selection of the IgG2c class of antibodies. Example 4 –Gb3 drives B cell repertoire diversity A central key to effective immunity is the generation of broad antibody responses, which are not limited to the most prominent antigenic determinants, but also recognize subdominant epitopes. Interclonal competition and repetitive mutation and selection processes increase affinity and impair clonal diversity. Since Gb3-abundant mice exhibited higher numbers of centrocytes, a cell population that undergoes selection in the light zone of GCs, it was assessed whether high levels of Gb3 help with the selection of B cell clones reactive against diverse epitopes. A rarefaction analysis of GC B cells isolated after NP-OVA immunization based on the Rep-SHM- Seq libraries was performed, using the R package iNEXT (FIGs.3A and 3B). Rarefaction analysis allows estimation of species richness, where each clonotype is defined as a unique species. Analysis was carried out for each sample with a number of reads from 100 to 5000, while diversity was tested statistically at 1000, 3000, and 5000 number of reads (FIG.3B). The While there was no significant difference between WT and A4galt-KO, it was determined that B cell clones from Gla-deficient animals showed higher diversity (FIG.3B ). It was assessed whether higher clonal diversity in Gb3-abundant mice facilitates the selection of GC B cells reactive with subdominant epitopes. Using the NP-OVA system for immunization, NP serves as the dominant antigenic determinant and OVA as subdominant epitope. Detecting GC B cell reactivities using fluorochrome-coupled NP or OVA, analysis by flow cytometry showed that Gla-KO mice displayed a sizable population of OVA-reactive B cells, while WT and Gb3-deficient animals only selected for NP-binding BCRs (FIG.3C). Moreover, compared to WT and A4galt-KO, Gb3-abundant mice showed strikingly increased IgG titers specific for OVA (FIGs.10A and 10B). Further, OVA-specific plasma cells were detected in the bone marrow of Gla-deficient mice at day 60 post immunization, highlighting the lasting humoral response to subdominant epitopes that was mediated by Gb3 abundance (FIG.10C). The effect of Gb3was assessed on the selection of subdominant epitopes is B cell-intrinsic. The B cell transfer set-up was used to muMT-KO mice that lack mature B lymphocytes (FIG.10D). In comparison to the other experimental groups, a higher frequency of OVAposGC B cells was observed, as well as elevated anti-OVA IgG titers in mice who received Gla-KO B cells (FIGs. 10E and 10F), corroborating the B cell-intrinsic function of Gb3-mediated selection of B cell reactivity toward subdominant epitopes. The expansion of Tfh cells and selection of diverse B cell clones depends on antigen presentation by GC B lymphocytes. Thus, taking into account that GC B cells show a wide expression range of MHC-II, it was assessed whether Gb3 affects MHC-II levels as well as antigen presentation to Tfh cells. In line with previous studies, lower MHC-II expression was found on WT centroblasts than on centrocytes and naive B cells. However, mice rich in Gb3 maintained high amounts of MHC-II on centroblasts as well as centrocytes (FIG.3D). In sharp contrast, Gb3-deficient GC B cell subsets displayed a strikingly lower surface level of MHC-II (FIG.3D). CD45.1-congenic OVA-specific CD4 T cells (OT-II) were injected into NP-OVA immunized mice and quantified the generation of Tfh cells (FIG.3E). Compared to WT, the increased expansion of OVA-specific Tfh cells in Gb3-abundant mice was virtually abrogated in the absence of Gb3 (FIG.3E). The density of MHC-II / peptide complexes on antigen-presenting GC B cells during their interaction with Tfh cells has been described to regulate B cell selection or entry into the GC reaction. Since extraordinary number of OVA-reactive GC B cells were observed following hapten-based immunization in Gb3-abundant mice, it was assessed whether the selection of GC B cells reactive with subdominant epitopes is dependent on Gb3-regulated MHC-II expression levels. To this end, the GC response was compared in the mouse models expressing MHC-II from a homozygous or haplosufficient gene locus (FIG.3F). Consistent with prior work, MHC-II haplosufficiency halved MHC-II surface expression on GC B cells in WT and Gb3-abundant mice, whereas the effect was negligible in Gb3 deficiency which is characterized by overall low amounts of MHC-II (FIG.3G). Following NP-OVA immunization, the amplified frequencies of GC B and Tfh cells in Gla-deficient animals were reduced upon lowered MHC-II expression in heterozygous MHC-II / Gla-KO mice (FIGs.10G, 10H, and 10I.). The elevated response to subdominant OVA antigen in Gb3-abundant mice was virtually abolished when MHC-II expression was cut in half (FIG.3H). These findings were reflected in serum antibody titers, with anti-OVA IgG in Gla-KO / MHC-II-Het animals brought to WT levels, whereas MHC-II haplosufficiency did not affect the antibody response to the dominant hapten NP (FIGs.3I and 3J). Thus, the GC response to subdominant epitopes was strictly dependent on Gb3-modulated MHC-II expression. This suggests Gb3 regulates MHC-II-restricted antigen presentation to select Tfh and GC B cells of great diversity. Example 5- High Gb3 level cross-protects against influenza infection In viral infection and vaccination, the generation of broadly neutralizing antibodies reactive with subdominant antigens is vital to ensure continued protection in the face of emerging mutant viruses. It was assessed whether Gb3 abundance in GC B cells allows for the selection of diverse antibodies during respiratory flu infection. For this purpose, the mouse models were infected with influenza A virus (H1N1, strain PR8) and monitored the cellular and humoral immune responses. In contrast to A4galt-deficient mice, intranasal infection with 102plaque forming units (PFU) of H1N1 triggered a strong GC response in mediastinal lymph nodes in Gla- KO animals (FIGs.11A and 11B), followed by increased titers of total IgG and IgG2c antibodies when Gb3 was abundant (FIG.11C). The viral antigen hemagglutinin (HA) consists of a globular head, which largely contains the dominant antigenic sites, and a head-supporting stalk domain that harbors subdominant epitopes. The Gb3-abundant mice exhibited increased titers of serum antibodies that reacted with the HA stalk region (FIG.11D), suggesting an amplified response to subdominant antigenic determinants mediated by Gb3. Moreover, Gla-deficient animals showed increased antibody titers recognizing recombinant H3, the most distantly related HA molecule compared to H1 (FIG.11E). Live virus was used to examine the neutralization capacity of serum antibodies derived from the different mouse models. Compared to WT and A4galt-KO animals, neutralization of H1N1 in vitro was augmented using serum from Gb3-abundant mice (FIG.11F). Antibodies from Gla-deficient animals also allowed for neutralization of a distantly related heterologous influenza virus (H3N2, strain HK68 X-31), demonstrating Gb3-mediated induction of cross-reactive antibodies (FIG.11G). In vivo challenge experiments were performed, using H1N1 for priming followed by secondary infection with either H1N1 or H3N2 (FIG.11H). Compared to WT, Gla-KO mice showed protection against both influenza strains, as reflected by reduced weight loss and low viral burden in the lung (FIGs.11I-11L). In contrast, A4galt-deficient mice suffered from weight loss and failed to control pulmonary viral load (FIGs.11I-11L). Mice with high Gb3 levels were able to virtually eradicate H3N2 viral burden in the lungs (FIG.111L), demonstrating Gb3-mediated cross-protection. This suggests that Gb3 in GC B cells drives the recognition of the HA stalk region, development of cross-reactive antibodies, and heterologous protection against influenza infection. Example 6- Use of Gb3 as adjuvant against influenza Based on the results describing the immunological functions of Gb3 in GC B cells, an exogenous Gb3was developed as a potential adjuvant for B cell responses upon vaccination. Administration of synthetic Gb3 was assessed to determine if it was able to reach GC B cells. For this purpose, A4galt-KO mice, which are devoid of endogenous Gb3, were subcutaneously immunized with emulsified Gb3 in combination with NP-OVA (FIG.12A). Ten days after immunization, ~20% Gb3posGC B cells were detected in the draining lymph node (FIG.12B). In addition, Gb3-treated mice showed increased total IgG, IgG2c, as well as Akt-phosphorylation in activated GC B cells (FIGs.12 C and 12D). These results demonstrate that injected Gb3 is physically acquired by GC B cells and deploys its functional impact on B cell activation, CD19 downstream signaling, and elevated antibody responses. Thus, to assess the adjuvant effect of Gb3 in anti-viral vaccination, WT mice were immunized with recombinant hemagglutinin (rHA) alone, or in combination with either Gb3 or the well-established adjuvant alum (FIG.4A). Compared to rHA alone and alum, the Gb3- formulated rHA group mounted a better GC response, marked by an increased percentage of GC B cells in draining lymph nodes (FIGs.13A and 13B). In a prime-boost model, both Gb3- and alum-formulated rHA induced robust antibody responses (FIGs.4B-4D). However, mice immunized with Gb3-formulated rHA showed the strongest production of the IgG2c class of antibodies (FIG.4D), higher avidity of antigen-antibody complexes (FIG.4E), and dramatically elevated titers of antibodies reactive with the HA stalk as an indicator of subdominant epitope recognition (FIG.4F). While both alum- and Gb3-adjuvanted animals had robust memory B cell responses as identified by ELISPOT, plasma cells secreting IgG2c were present in the Gb3- adjuvanted group at day 60 post immunization (FIG.4G). Moreover, the antibodies isolated from the Gb3-adjuvant group bound more effectively to rHA molecules from group 1 (H1 and H5) as well as group 2 (H3 and H7) of influenza viruses (FIG.4H). Whereas Gb3- and alum-adjuvanted groups had similar H1N1 (PR8) neutralization titers, only Gb3 treatment facilitated efficient neutralization of the group 2 virus H3N2 (X-31) (FIGs.4I and 4J). This suggests exogeneous Gb3 acts as a powerful adjuvant and promotes the production of cross-reactive antibodies. It was assessed if Gb3-immunized mice were broadly protected against influenza infections with distantly related viral strains. To this end, vaccinated animals were infected with either H1N1 or H3N2 and monitored weight loss and virus multiplication in the lung (FIG.4K). Gb3-adjuvanted rHA provided protection from both viral strains as characterized by reduced weight loss (FIGs.4L and 4M) and improved clearance of viruses in the lung at day 5 post infection (FIGs.4N and 4O). By contrast, alum-immunized mice were protected only against group-1 influenza infections. Furthermore, a single-shot vaccination was used to test the potency of Gb3 as an adjuvant (FIG.13A) and observed elevated titers of H1N1 hemagglutination inhibition (HI) (FIG.13C). In comparison to rHA only and alum, the Gb3-vaccinated animals exhibited less viral burden in the lung and greater protection from disease (FIGs.13D and 13E). To assess whether protection against viral infection was critically dependent on antibodies, serum from vaccinated mice was transferred to naive WT recipients. Animals that received serum from the Gb3-adjuvant group were better protected than mice from the other study groups, as reflected in the respective weight loss curves (FIG.9F). It was considered whether Gb3 was an adjuvant to the human system. First, it was assessed whether Gb3 is able to interact with CD19 to drive BCR downstream signaling in human GC B cells. For this assay, CD77posand CD77negGC B cells were sorted from human tonsils and in parallel reconstituted CD77negcells with exogeneous Gb3 (FIG.14A). Performing PLA, a strong signal was found in confocal microscopy, indicative of proximity between Gb3 and CD19 in human GC B cells (FIG.14B). Functionally, after BCR cross-linking, CD77posB cells displayed higher phosphorylation of Akt and degradation of Foxo1 than CD77negcells. Furthermore, treatment with Gb3 was able to reconstitute effective BCR downstream signaling in CD77negGC B cells (FIG.14C). The adjuvant effect of Gb3 was compared with the clinically used adjuvant alum, using human tonsil organoids as previously described. Briefly, dissociated tonsil cells were cultured in vitro to form organoids, prior to stimulation with antigens and adjuvants, an experimental system that efficiently mimics the human GC response (FIG.14D). Compared to stimulation with rHA alone, Gb3 improved GC responses as well as plasma cell differentiation (FIG.14E). In addition, Gb3 triggered a total anti-rHA IgG1 titer higher than rHA and alum, reminiscent of the findings in the murine model regarding IgG2c production (FIG.14F). This suggests that the lipid Gb3 can activate CD19 downstream signaling in human B cells and has great potential as an adjuvant in the human system, involving IgG1-based adjuvanticity. Example 7- Use of Gb3 as adjuvant against SARS-CoV-2 It was previously demonstrated that Gb3-driven humoral responses were protective against a broad range of viruses. Therefore, Gb3 was then tested as an adjuvant for a SARS-CoV- 2 subunit vaccine using a prime boost model (FIG.15O). For this assay, recombinant spike protein (S-protein) was used as an antigen and antibody responses were monitored until 72 days after immunization. An increase in total IgGs was observed (FIGs.15P-15R), as well as increased persistence of receptor binding domain (RBD) specific memory (FIG.15S) and plasma cells (FIG.15T) in the bone marrow of mice that received Gb3 or alum. Only mice immunized with Gb3 and S-protein demonstrated an induction and persistence of IgG2c class antibodies. To test the function of these antibodies, an ACE2 and S-protein binding inhibition assay was used, where the percentage of inhibition is proportionate the neutralization capacity of assayed IgGs. Serum from mice immunized with Gb3 and S-protein had greater binding inhibition than the other immunized groups (FIG.15U) which suggests that although the antibody titers between Gb3 and alum immunized mice are similar, IgGs from Gb3 immunized mice have higher affinity. Taken together, these findings highlight Gb3 as a potent adjuvant for anti-viral vaccination. Example 8- High Gb3 level protects against cancer It was previously demonstrated that Gb3-driven humoral responses were protective against a broad range of diseases. Therefore, the role of Gb3 was also tested in cancer immunity. To test this, mice were treated with 1x106live MCA101-OVA tumor cells in the right flank. Subsequently, from day 2 to day 16, tumor growth was monitored in wild-type, Gla KO (elevated Gb3), and A4galt KO (Gb3-deficient) mice. Tumor volume (mm3) was increased in A4galt KO (Gb3-deficient) mice compared to Gla KO (elevated Gb3) and wild-type animals. Notably, Gla KO (elevated Gb3) mice strikingly controlled tumor growth. Therefore, there is an inverse correlation between Gb3 abundance and tumor growth, demonstrating that Gb3 protects against cancer. EQUIVALENTS AND SCOPE Those skilled in the art will recognize, or be able to ascertain using no more than routine experimentation, many equivalents of the embodiments described herein. The scope of the present disclosure is not intended to be limited to the above description, but rather is as set forth in the appended claims. Articles such as “a,” “an,” and “the” may mean one or more than one unless indicated to the contrary or otherwise evident from the context. Claims or descriptions that include “or” between two or more members of a group are considered satisfied if one, more than one, or all of the group members are present, unless indicated to the contrary or otherwise evident from the context. The disclosure of a group that includes “or” between two or more group members provides embodiments in which exactly one member of the group is present, embodiments in which more than one members of the group are present, and embodiments in which all of the group members are present. For purposes of brevity those embodiments have not been individually spelled out herein, but it will be understood that each of these embodiments is provided herein and may be specifically claimed or disclaimed. It is to be understood that the disclosure encompasses all variations, combinations, and permutations in which one or more limitation, element, clause, or descriptive term, from one or more of the claims or from one or more relevant portion of the description, is introduced into another claim. For example, a claim that is dependent on another claim can be modified to include one or more of the limitations found in any other claim that is dependent on the same base claim. Furthermore, where the claims recite a composition, it is to be understood that methods of making or using the composition according to any of the methods of making or using disclosed herein or according to methods known in the art, if any, are included, unless otherwise indicated or unless it would be evident to one of ordinary skill in the art that a contradiction or inconsistency would arise. Where elements are presented as lists, e.g., in Markush group format, it is to be understood that every possible subgroup of the elements is also disclosed, and that any element or subgroup of elements can be removed from the group. It is also noted that the term “comprising” is intended to be open and permits the inclusion of additional elements or steps. It should be understood that, in general, where an embodiment, product, or method is referred to as comprising particular elements, features, or steps, embodiments, products, or methods that consist, or consist essentially of, such elements, features, or steps, are provided as well. For purposes of brevity those embodiments have not been individually spelled out herein, but it will be understood that each of these embodiments is provided herein and may be specifically claimed or disclaimed. Where ranges are given, endpoints are included. Furthermore, it is to be understood that unless otherwise indicated or otherwise evident from the context and / or the understanding of one of ordinary skill in the art, values that are expressed as ranges can assume any specific value within the stated ranges in some embodiments, to the tenth of the unit of the lower limit of the range, unless the context clearly dictates otherwise. For purposes of brevity, the values in each range have not been individually spelled out herein, but it will be understood that each of these values is provided herein and may be specifically claimed or disclaimed. It is also to be understood that unless otherwise indicated or otherwise evident from the context and / or the understanding of one of ordinary skill in the art, values expressed as ranges can assume any subrange within the given range, wherein the endpoints of the subrange are expressed to the same degree of accuracy as the tenth of the unit of the lower limit of the range. Where websites are provided, URL addresses are provided as non-browser-executable codes, with periods of the respective web address in parentheses. The actual web addresses do not contain the parentheses. In addition, it is to be understood that any particular embodiment of the present disclosure may be explicitly excluded from any one or more of the claims. Where ranges are given, any value within the range may explicitly be excluded from any one or more of the claims. Any embodiment, element, feature, application, or aspect of the compositions and / or methods of the disclosure, can be excluded from any one or more claims. For purposes of brevity, all of the embodiments in which one or more elements, features, purposes, or aspects is excluded are not set forth explicitly herein.

Claims

CLAIMS What is claimed is:

1. A method of enhancing an immune response in a subject, the method comprising administering to the subject an effective amount of globotriaosylceramide (Gb3) or an analog thereof.

2. The method of claim 1, wherein the subject has or is at risk of developing a disease.

3. The method of claim 2, wherein the disease is caused by a bacterium, a virus, a parasite, or a fungus.

4. The method of claim 3, wherein the disease is a disease caused by a virus.

5. The method of claim 4, wherein the virus is an adenovirus, a coronavirus, an enterovirus such as polio virus, dengue virus, Ebola virus, a herpes viruses such as herpes simplex virus, cytomegalovirus and varicella-zoster, measles, mumps, rubella, hepatitis A virus, hepatitis B virus, hepatitis C virus, human papilloma virus, influenza virus, rabies, Japanese encephalitis, rotavirus, human immunodeficiency virus (HIV), respiratory syncytial virus (RSV), smallpox, yellow fever, dengue virus, or Zika virus.

6. The method of claim 5, wherein the virus is an influenza virus.

7. The method of claim 6, wherein the virus is a human influenza A or a human influenza B virus.

8. The method of claim 7, wherein the virus is from a group 1 or group 2 influenza A virus.

9. The method of claim 4, wherein the virus is a beta coronavirus.

10. The method of claim 9, wherein the virus is MERS-CoV, SARS-CoV-1, or SARS-CoV-2.

11. The method of claim 2, wherein the disease is a cancer.

12. The method of claim 11, wherein the cancer is a hematological cancer, lung cancer, breast cancer, brain cancer, gastrointestinal cancer, liver cancer, kidney cancer, bladder cancer, pancreatic cancer, ovarian cancer, testicular cancer, prostate cancer, endometrial cancer, muscle cancer, bone cancer, neuroendocrine cancer, connective tissue cancer, head and neck cancer, or skin cancer.

13. The method of any one of claims 1-12, wherein the subject is a human.

14. The method of claim 13, wherein the subject is a human neonate, infant, adult, or an elderly human.

15. The method of any one of claims 1-12, wherein the subject is a companion animal or a research animal.

16. The method of any one of claims 1-15, wherein the immune response comprises a humoral response.

17. The method of any one of claims 1-16, wherein the immune response comprises binding of Gb3 or an analog thereof to Cluster of Differentiation 19 (CD19).

18. The method of any one of claims 1-17, wherein the immune response comprises activation of the PI3K-Akt-mTOR pathway.

19. The method of any one of claims 1-18, wherein the immune response comprises a reduction of transcription mediated by Forkhead box protein O1 (FOXO-1).

20. The method of any one of claims 1-19, wherein the immune response comprises enhanced B cell receptor (BCR) signaling.

21. The method of any one of claims 1-20, wherein the administration induces the expansion of germinal center B cells in the subject.

22. The method of any one of claims 1-21, wherein the administration induces the production of an antibody in the subject.

23. The method of claim 22, wherein the antibody is an immunoglobulin G (IgG).

24. The method of claim 23, wherein the IgG is a subclass 1 IgG (IgG1) or a subclass 2 IgG (IgG2).

25. The method of claim 24, wherein the IgG is a subclass 2c IgG (IgG2c).

26. The method of any one of claims 1-25, further comprising administering to the subject an antigen.

27. The method of claim 26, wherein the antigen is administered before, after, or concurrently with Gb3 or an analog thereof.

28. The method of claim 26 or claim 27, wherein the administration induces the production of an antibody in the subject that is specific for the antigen.

29. The method of claim 28, wherein the antigen is an antigen from a bacterium, a virus, a parasite, or a fungus.

30. The method of claim 29, wherein the antibody is an antibody that neutralizes the bacterium, virus, parasite, or fungus.

31. The method of claim 29 or claim 30, wherein the administration confers heterotypic protection in the subject.

32. The method of claim 28, wherein the antigen is an antigen from a cancer.

33. The method of claim 32, wherein the antibody is an antibody that promotes immunity against the cancer.

34. The method of any one of claims 1-33, wherein the administration occurs intramuscularly, intradermally, orally, intravenously, topically, intranasally, or sublingually.

35. The method of any one of claims 1-34, wherein the administration occurs more than once.

36. The method of any one of claims 1-35, wherein the administration treats a disease in the subject.

37. The method of any one of claims 1-35, wherein the administration prevents a disease in the subject.

38. The method of claim 36 or 37, wherein the disease is caused by a bacterium, a virus, a parasite, or a fungi.

39. The method of claim 36 or 37, wherein the disease is a cancer.

40. A composition comprising an antigen and Gb3 or an analog thereof.

41. The composition of claim 40, wherein the antigen comprises a protein or polypeptide.

42. The composition of claim 40 or 41, wherein the antigen comprises a nucleic acid encoding a protein or a polypeptide.

43. The composition of claim 42, wherein the nucleic acid is DNA or RNA.

44. The composition of any one of claims 40-43, wherein the antigen is a viral antigen.

45. The composition of claim 44, wherein the virus is an adenovirus, a coronavirus, an enterovirus such as polio virus, dengue virus, Ebola virus, a herpes viruses such as herpes simplex virus, cytomegalovirus and varicella-zoster, measles, mumps, rubella, hepatitis A virus, hepatitis B virus, hepatitis C virus, human papilloma virus, influenza virus, rabies, Japanese encephalitis, rotavirus, human immunodeficiency virus (HIV), respiratory syncytial virus (RSV), smallpox, yellow fever, dengue virus, or Zika virus.

46. The composition of claim 45, wherein the antigen is an antigen from an influenza virus.

47. The composition of claim 46, wherein the antigen is an antigen from a human influenza A or a human influenza B virus.

48. The composition of claim 47, wherein the antigen is an antigen from a group 1 or group 2 influenza A virus.

49. The composition of claim 48, wherein the antigen comprises a group 1 or group 2 influenza A hemagglutinin (HA) protein, or an immunogenic fragment thereof.

50. The composition of claim 45, wherein the antigen is from a beta coronavirus.

51. The composition of claim 50, wherein the antigen is an antigen from MERS-CoV, SARS- CoV-1, or SARS-CoV-2.

52. The composition of claim 51 wherein the antigen comprises a MERS-CoV, SARS-CoV-1, or SARS-CoV-2 spike protein, or an immunogenic fragment thereof.

53. The composition of claim 45, wherein the antigen comprises a viral particle, a killed or inactivated virus, or a live attenuated virus.

54. The composition of claim 53, wherein the virus is an influenza virus.

55. The composition of claim 54, wherein the virus is a human influenza A or a human influenza B virus.

56. The composition of claim 55, wherein the virus is a group 1 or group 2 influenza A virus.

57. The composition of claim 53, wherein the virus is a beta coronavirus.

58. The composition of claim 57, wherein the virus is MERS-CoV, SARS-CoV-1, or SARS- CoV-2.

59. The composition of any one of claims 40-58, further comprising a pharmaceutically acceptable carrier.

60. The composition of any one of claims 40-59, wherein the composition is a vaccine composition.

61. The composition of claims 60, wherein the Gb3 or an analog thereof acts as an adjuvant.

62. The composition of 60 or 61, wherein the vaccine composition further comprises a second adjuvant.

63. The composition of claim 62, wherein the second adjuvant is alum or an emulsion.

64. The composition of any one of claim 60-63, wherein the vaccine composition is a subunit vaccine, an attenuated vaccine, or a conjugate vaccine.

65. A method of enhancing an immune response to an antigen in a subject in need thereof, the method comprising administering to the subject an effective amount of the composition of any one of claims 40-64.

66. The method of claim 65, wherein the antigen is a viral antigen.

67. The method of claim 65 or 66, wherein the subject is infected with a virus.

68. The method of claim 65 or 66, wherein the subject is at risk for infection by a virus.

69. The method of any one of claims 65-67, wherein the virus is an adenovirus, a coronavirus, an enterovirus such as polio virus, dengue virus, Ebola virus, a herpes viruses such as herpes simplex virus, cytomegalovirus and varicella-zoster, measles, mumps, rubella, hepatitis A virus, hepatitis B virus, hepatitis C virus, human papilloma virus, influenza virus, rabies, Japanese encephalitis, rotavirus, human immunodeficiency virus (HIV), respiratory syncytial virus (RSV), smallpox, yellow fever, dengue virus, or Zika virus.

70. The method of claim 69, wherein the virus is an influenza virus.

71. The method of claim70, wherein the virus is a human influenza A or a human influenza B virus.

72. The method of claim 71, wherein the virus is a group 1 or group 2 influenza A virus.

73. The method of claim 69, wherein the virus is a beta coronavirus.

74. The method of claim 73, wherein the virus is MERS-CoV, SARS-CoV-1, or SARS-CoV- 2.

75. The method of any one of claims 65-74, wherein the subject is a human.

76. The method of claim 75, wherein the subject is a human adult or an elderly human.

77. The method of any one of claims 65-74, wherein the subject is a companion animal or a research animal.

78. The method of any one of claims 65-77, wherein the immune response comprises a humoral response.

79. The method of any one of claims 65-78, wherein the immune response comprises binding of Gb3 or an analog thereof to Cluster of Differentiation 19 (CD19).

80. The method of any one of claims 65-79, wherein the immune response comprises activation of the PI3K-Akt-mTOR pathway.

81. The method of any one of claims 65-80, wherein the immune response comprises a reduction of transcription mediated by Forkhead box protein O1 (FOXO-1).

82. The method of any one of claims 65-81, wherein the immune response comprises enhanced B cell receptor (BCR) signaling.

83. The method of any one of claims 65-82, wherein administration of the composition induces the expansion of germinal center B cells in the subject.

84. The method of any one of claims 65-83, wherein administration of the composition induces the production of an antibody in the subject.

85. The method of claim 84, wherein the antibody is specific for the antigen.

86. The method of claim 85, wherein the antibody is an immunoglobulin G (IgG).

87. The method of claim 86, wherein the IgG is a subclass 1 IgG (IgG1) or a subclass 2 IgG (IgG2).

88. The method of claim 87, wherein the IgG is a subclass 2c IgG (IgG2c).

89. The method of any one of claims 84-88, wherein the antibody is a neutralizing antibody.

90. The method of any one of claims 84-89, wherein the antibody inhibits binding between the antigen and an antigen-binding receptor of the subject.

91. The method of claim 90, wherein the antigen is a group 1 or group 2 influenza A hemagglutinin (HA) protein and the antigen-binding receptor is a glycoprotein or glycolipid of the subject that is modified by sialic acid.

92. The method of claim 90, wherein the antigen is a MERS-CoV, SARS-CoV-1, or a SARS- CoV-2 spike protein and the antigen-binding receptor is an angiotensin converting enzyme 2 (ACE2) protein of the subject.

93. The method of any one of claims 65-92, wherein administration of the composition confers heterotypic protection in the subject.

94. The method of claim 93, wherein administration of the composition enhances heterotypic protection in the subject, compared with administration of the antigen alone.

95. The method of any one of claims 65-94, wherein administration of the composition occurs intramuscularly, intradermally, orally, intravenously, topically, intranasally, or sublingually.

96. The method of any one of claims 65-95, wherein administration of the composition treats a disease in the subject.

97. The method of any one of claims 65-96, wherein administration of the composition prevents a disease in the subject.

98. The method of claim 96 or 97, wherein the disease is a disease caused by a virus.

99. The method of claim 98, wherein the disease is influenza, Middle East respiratory syndrome (MERS), sudden acute respiratory syndrome (SARS), or coronavirus disease 2019 (COVID-19).

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