Epstein-BARR virus antigen-encoding messenger ribonucleic acid and antigen protein vaccines

Abstract

Provided are a pharmaceutical composition comprising a delivery vehicle and at least two Epstein-Barr virus (EBV) antigen-encoding messenger ribonucleic acid (mRNA) constructs. Methods of treatment, methods of making, uses of the pharmaceutical composition, and pharmaceutical compositions comprising at least two or more EBV antigens are provided. All contemplate treating and preventing (i.e. reducing the likelihood of a symptom or a severity of a symptom of) EBV infections and EBV-associated diseases, such as infectious mononucleosis, multiple sclerosis, rheumatoid arthritis and systemic lupus erythematosus.

Description

[0001] Attorney Docket No: 70488WO01 EPSTEIN-BARR VIRUS ANTIGEN-ENCODING MESSENGER RIBONUCLEIC ACID AND ANTIGEN PROTEIN VACCINES SEQUENCE LISTING The instant application contains a Sequence Listing, which has been submitted electronically in computer readable form in XML file format and is hereby incorporated by reference in its entirety. Said XML file, created on April 30, 2025, is named “70488WO01” and is 438,914 bytes in size. FIELD OF THE INVENTION This invention is in the field of treating and preventing viral infections. In particular, the invention relates to nucleic acids encoding Epstein Barr virus (EBV) antigens (Epstein Barr Virus constructs). It includes the use of Epstein-Barr virus antigen constructs for treating and preventing Epstein-Barr virus infections and Epstein-Barr virus-associated diseases. BACKGROUND Epstein-Barr virus (EBV), also known as human gammaherpesvirus 4 and human herpesvirus 4 (HHV-4), is one of the most common viruses in humans, infecting at least 90% of adults. EBV establishes asymptomatic latent infection in most infected individuals but is also known as the primary causative agent of diseases including infectious mononucleosis and multiple sclerosis (MS). Additionally, EBV infection is associated with certain types of malignancies, such as gastric carcinoma, nasopharyngeal carcinoma, Hodgkin’s lymphoma, non-Hodgkin’s lymphoma, Burkitt’s lymphoma, and post-transplant lymphoproliferative disorder, as well as an increased risk of systemic lupus erythematosus, rheumatoid arthritis, and Sjögren's syndrome. EBV virions contain a double-stranded DNA genome of about 192 kilobases encoding about 85 genes. The EBV genome is encased in a protein nucleocapsid surrounded by a viral tegument. An outer envelope layer comprises lipids and surface glycoproteins, which target the virus to its primary host cells, B lymphocytes and epithelial cells. These glycoproteins in the envelope are EBV glycoprotein-H (gH), glycoprotein-L (gL), glycoprotein-42 (gp42), glycoprotein-B (gB), glycoprotein- 220 (gp220), and glycoprotein-350 (gp350). EBV gH, gL, gp42, gB and then either gp220 or gp350 bind to cluster of differentiation 21 (CD21), cluster of differentiation 35 (CD35), and major histocompatibility complex II (MHC-II) proteins on the B cell, gaining the virion access to the cell, whereas gH, gL, and gp42 bind to integrins, gaining the virion access to epithelial cells. A gp220-CD21 or a gp350-CD21 interaction also occur in some CD21-expressing epithelial cells. Gp220 and gp350 share homology except that gp350 comprises additional amino acids that together have higher homology to endogenous proteins from Homo sapiens. After initial infection of host cells, EBV enters a stage of active production of infectious virions, termed the lytic replication stage (or lytic stage). During the lytic stage, one or more lytic gene Attorney Docket No: 70488WO01 products, including ZEBRA, BRLF1, BNLF2, BCRF1, and viral capsid antigens (VCAs) are expressed; as well as envelope glycoproteins such as gp350 and gp220. Following a period of lytic replication, EBV enters a state of persistent viral infection without active virion production, termed “latency” or the “latent phase.” Latent EBV infection is accompanied by characteristic gene expression programs, including expression of one or more latent gene products such as EBV nuclear antigen-1 (EBNA1), EBNA2, EBNA3A, EBNA3B, EBNA3C, EBNA leader protein (EBNA-LP), EBV latent membrane protein-1 (LMP1), and EBV LMP2. Latently infected cells can be reactivated to lytic viral production by triggers, which are not yet understood. After primary infection, EBV persists lifelong in the memory B lymphocytes of the infected host, with episodic reactivations and production EBV virions, and accordingly antigens, both of which are detectable in saliva. This results in a balance between viral replication and host immune responses. However, EBV persistence combined with genetic and other factors can lead to the development of cancers or trigger immune-mediated inflammatory diseases such as infectious mononucleosis and MS. Lupo J. et al., Viruses, 2023; 15: 656-678. A number of EBV vaccine candidates have been evaluated in animal models and human trials. Most prophylactic vaccine candidates have focused on the major EBV envelope gp350 as the immunogen. Gu et al. reported that a recombinant live vaccinia virus expressing EBV gp350 elicited EBV neutralizing antibodies and modest protection in children, but not in adults. Gu et al., Dev. Biol. Stand.1995; 84: 171–177. A recombinant EBV gp350 vaccine, when administered, was found not to protect against EBV infection, but its administration reduced the occurrence of infectious mononucleosis. Sokal et al., J. Infect. Dis.2007;196(12):1749–1753. Therapeutic EBV vaccine candidates have largely focused on delivery by modified vaccinia virus Ankara (MVA) vector and primarily targeted T cell epitopes of EBNA1 and EBV LMP2. For example, Taylor et al. have described a modified vaccinia virus Ankara (MVA) vector expressing a peptide fragment of EBNA1 fused to the full-length EBV LMP2 protein. The so-called MVA-EL vaccine was reported to induce antigen-specific CD4+ and CD8+ T cell responses in early clinical trials, but these trials died out. Taylor et al., J. Virol. Jan.2004, p.768–778. Similarly, a recombinant human adenoviral vector expressing full length EBV LMP2 protein was reported to induce antigen-specific T cell responses in vitro and in in mice. Pan et al., Biochem Biophys Res Commun.2006 Sep 1;347(3):551-7. There remains a need for an EBV vaccine for use in preventing EBV infection as well as in treating EBV-associated malignancies and EBV-associated diseases, such as infectious mononucleosis, post-transplant lymphoproliferative disorder, and MS. SUMMARY OF THE INVENTION In one aspect, a pharmaceutical composition is provided, the pharmaceutical composition comprising a delivery vehicle and at least two Epstein-Barr virus (EBV) antigen-encoding messenger ribonucleic acid (mRNA) constructs; each of the at least two EBV antigen-encoding mRNA Attorney Docket No: 70488WO01 constructs comprising a segment that encodes an EBV antigen; the EBV antigens comprising an EBV B cell module antigen and an EBV T cell module antigen; the EBV B cell module antigen comprising an EBV glycoprotein-220 (gp220) antigen; and the EBV T cell module antigen comprising at least two, at least three, or at least four of: (a) an EBV latent membrane protein-1 (LMP1) antigen; (b) an EBV latent membrane protein-2 (LMP2) antigen; (c) an EBV nuclear antigen-1 (EBNA1) antigen; (d) an EBV nuclear antigen-3A (EBNA3A) antigen; and (e) a BamHI Z EBV replication activator (ZEBRA) antigen. In another aspect, a pharmaceutical composition is provided, the pharmaceutical composition comprising a delivery vehicle and an EBV antigen-encoding mRNA construct; each EBV antigen-encoding mRNA construct comprising a segment that encodes an EBV antigen; the EBV antigens comprising an EBV T cell module antigen; and the EBV T cell module antigen comprising at least two, at least three, or at least four of: (a) an EBV LMP1 antigen; (b) an EBV LMP2 antigen; (c) an EBNA1 antigen; (d) an EBNA3A antigen; and (e) a ZEBRA antigen. In another aspect, a pharmaceutical composition is provided, the pharmaceutical composition comprising lipids and at least two EBV antigen-encoding mRNA constructs; the lipids encapsulating the at least two EBV antigen-encoding mRNA constructs, thereby forming LNPs; each of the at least two EBV antigen- encoding mRNA constructs comprising a segment that encodes an EBV antigen; the EBV antigens comprising an EBV B cell module antigen and an EBV T cell module antigen; the EBV B cell module antigen comprising an EBV gp220 antigen; and the EBV T cell module antigen comprising at least two, at least three, or at least four of: (a) an EBV LMP1 antigen; (b) an EBV LMP2 antigen; (c) an EBNA1 antigen; (d) EBNA3A antigen; and (e) a ZEBRA antigen. In another aspect, a pharmaceutical composition is provided, the pharmaceutical composition comprising lipids and an EBV antigen-encoding mRNA construct; the lipids encapsulating the EBV antigen-encoding mRNA construct, thereby forming LNPs; each EBV antigen-encoding mRNA construct comprising a segment that encodes an EBV antigen; the EBV antigens comprising an EBV T cell module antigen; and the EBV T cell module antigen comprising at least two, at least three, or at least four of: (a) an EBV LMP1 antigen; (b) an EBV LMP2 antigen; (c) an EBNA1 antigen; (d) an EBNA3A antigen; and (e) a ZEBRA antigen. In another aspect, a pharmaceutical composition is provided, the pharmaceutical composition comprising a delivery vehicle and at least two EBV antigen-encoding mRNA constructs; each of the at least two EBV antigen-encoding mRNA constructs comprising a segment that encodes an EBV antigen; the EBV antigens comprising an EBV B cell module antigen; the EBV B cell module antigen comprising an EBV gp220 antigen, an EBV gH antigen, an EBV gL antigen, and an EBV gp42 antigen. In another aspect, a pharmaceutical composition is provided, the pharmaceutical composition comprising a delivery vehicle and at least two EBV antigen-encoding mRNA constructs; each of the at least two EBV antigen-encoding mRNA constructs comprising a segment that encodes an EBV Attorney Docket No: 70488WO01 antigen; the EBV antigens comprising an EBV B cell module antigen; the EBV B cell module antigen comprising an EBV gp220 antigen, an EBV gH antigen, an EBV gL antigen, and an EBV gp42 antigen; each of the at least two EBV antigen-encoding mRNA constructs lacking a RNA-dependent RNA polymerase and a replicase; the pharmaceutical composition lacking a RNA-dependent RNA polymerase-encoding mRNA construct; and each of the at least two antigen-encoding mRNA constructs being non-replicating mRNA constructs. In another aspect, a pharmaceutical composition is provided, the pharmaceutical composition comprising a delivery vehicle and at least two EBV antigen-encoding mRNA constructs; each of the at least two EBV antigen-encoding mRNA constructs comprising a segment that encodes an EBV antigen; the EBV antigens comprising an EBV B cell module antigen; the EBV B cell module antigen comprising an EBV gp220 antigen, an EBV gH antigen, an EBV gL antigen, and an EBV gp42 antigen; each of the EBV antigen-encoding mRNA constructs comprising a segment that encodes an RNA-dependent RNA polymerase and each of the at least two EBV antigen-encoding mRNA constructs being a self-replicating mRNA construct. In another aspect, a pharmaceutical composition is provided, the pharmaceutical composition comprising a delivery vehicle, at least two EBV antigen-encoding mRNA constructs, and an RNA-dependent RNA polymerase-encoding mRNA construct; each of the at least two EBV antigen-encoding mRNA constructs comprising a segment that encodes an EBV antigen; the EBV antigens comprising an EBV B cell module antigen; the EBV B cell module antigen comprising an EBV gp220 antigen, an EBV gH antigen, an EBV gL antigen, and an EBV gp42 antigen; the RNA- dependent RNA polymerase-encoding mRNA construct comprising a segment that encodes the RNA-dependent RNA polymerase; and the at least two EBV antigen-encoding mRNA constructs and the RNA-dependent RNA polymerase-encoding mRNA constructs being collectively trans-amplifying mRNA. In another aspect, a pharmaceutical composition is provided, the pharmaceutical composition comprising lipids and at least two EBV antigen-encoding mRNA constructs; the lipids encapsulating the at least two EBV antigen-encoding mRNA constructs, thereby forming LNPs; each of the at least two EBV antigen-encoding mRNA constructs comprising a segment that encodes an EBV antigen; the EBV antigens comprising an EBV B cell module antigen; the EBV B cell module antigen comprising an EBV gp220 antigen, an EBV gH antigen, an EBV gL antigen, and an EBV gp42 antigen. In another aspect, a pharmaceutical composition is provided, the pharmaceutical composition comprising lipids and at least two EBV antigen-encoding mRNA constructs; the lipids encapsulating the at least two EBV antigen-encoding mRNA constructs, thereby forming LNPs; each of the at least two EBV antigen-encoding mRNA constructs comprising a segment that encodes an EBV antigen; the EBV antigens comprising an EBV B cell module antigen; the EBV B cell module antigen comprising an EBV gp220 antigen, an EBV gH antigen, an EBV gL antigen, and an EBV gp42 Attorney Docket No: 70488WO01 antigen; each of the at least two EBV antigen-encoding mRNA constructs lacking a RNA-dependent RNA polymerase and a replicase; the pharmaceutical composition lacking a RNA-dependent RNA polymerase-encoding mRNA construct; and each of the at least two antigen-encoding mRNA constructs being non-replicating mRNA constructs. In another aspect, a pharmaceutical composition is provided, the pharmaceutical composition comprising lipids and at least two EBV antigen-encoding mRNA constructs; the lipids encapsulating the at least two EBV antigen-encoding mRNA constructs, thereby forming LNPs; each of the at least two EBV antigen-encoding mRNA constructs comprising a segment that encodes an EBV antigen; the EBV antigens comprising an EBV B cell module antigen; the EBV B cell module antigen comprising an EBV gp220 antigen, an EBV gH antigen, an EBV gL antigen, and an EBV gp42 antigen; each of the EBV antigen-encoding mRNA constructs comprising a segment that encodes an RNA-dependent RNA polymerase and each of the at least two EBV antigen-encoding mRNA constructs being a self-replicating mRNA construct. In another aspect, a pharmaceutical composition is provided, the pharmaceutical composition comprising lipids, at least two EBV antigen-encoding mRNA constructs, and an RNA-dependent RNA polymerase-encoding mRNA construct; the lipids encapsulating the at least two EBV antigen- encoding mRNA constructs and the RNA-dependent RNA polymerase-encoding mRNA construct, thereby forming LNPs; each of the at least two EBV antigen-encoding mRNA constructs comprising a segment that encodes an EBV antigen; the EBV antigens comprising an EBV B cell module antigen; the EBV B cell module antigen comprising an EBV gp220 antigen, an EBV gH antigen, an EBV gL antigen, and an EBV gp42 antigen; the RNA-dependent RNA polymerase-encoding mRNA construct comprising a segment that encodes the RNA-dependent RNA polymerase; and the at least two EBV antigen-encoding mRNA constructs and the RNA-dependent RNA polymerase-encoding mRNA constructs being collectively trans-amplifying mRNA. A pharmaceutical composition is provided, the pharmaceutical composition comprising at least two EBV recombinant T cell module antigens; the at least two recombinant T cell module antigens comprising: (a) at least four EBV LMP1 protein fragments, (b) at least four EBV LMP2 protein fragments, (c) at least three EBNA1 protein fragments, and (d) at least seven EBNA3A protein fragments; the first of the EBV LMP1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 2; the second of the EBV LMP1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 3; the third of the EBV LMP1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 4; the fourth of the EBV LMP1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 5; the first of the EBV LMP2 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 8; the second of the EBV LMP2 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 9; the third of the EBV LMP2 protein fragments having at least Attorney Docket No: 70488WO01 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 10; the fourth of the EBV LMP2 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 11; the first of the EBNA1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 13; the second of the EBNA1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 14; the third of the EBNA1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 15; the first of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 17; the second of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 18; the third of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 19; the fourth of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 20; the fifth of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 21; the sixth of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 22; the seventh of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 23; at least two of, or at least three of, the first, second, third, and fourth of the EBV LMP1 protein fragments not being adjacent to each other on the at least two recombinant T cell module antigens; at least two of, or at least three of, the first, second, third, and fourth of the EBV LMP2 protein fragments not being adjacent to each other on the at least two recombinant T cell module antigens; at least two of the first, second, and third of the EBNA1 protein fragments not being adjacent to each other on the at least two recombinant T cell module antigens; and at least two of, at least three of, at least four of, at least five of, or at least six of the first, second, third, fourth, fifth, sixth, and seventh of the EBNA3A protein fragments not being adjacent to each other on the at least two recombinant T cell module antigens. A unit dose comprising a syringe and the pharmaceutical composition of any of the above aspects; the syringe having an interior; and the pharmaceutical composition being in the interior. A method of treating multiple sclerosis, gastric carcinoma, nasopharyngeal carcinoma, post- transplant lymphoproliferative disorder, rheumatoid arthritis, and / or systemic lupus erythematosus in a subject, the method comprising administering an effective amount of the pharmaceutical composition of any of the above aspects to the subject. A method of eliciting an immune response to EBV in a subject, the method comprising administering an effective amount of the pharmaceutical composition of any of above aspects to the subject. A method of reducing the likelihood of multiple sclerosis relapse, reducing the number of relapses of multiple sclerosis, and / or increasing the time between relapses of multiple sclerosis in a first subject, the method comprising administering an effective amount of the pharmaceutical Attorney Docket No: 70488WO01 composition of any of the above aspects to the first subject, the reducing the likelihood of multiple sclerosis relapse in the first subject being relative to the likelihood of multiple sclerosis relapse in a second subject, who has not been administered the pharmaceutical composition, the reducing the number of relapses of multiple sclerosis in the first subject being relative to the number of relapses of multiple sclerosis in the second subject, and the increasing the time between relapses of multiple sclerosis in the first subject being relative to the time between relapses of multiple sclerosis in the second subject. The pharmaceutical composition of any of the above aspects for use as a medicament. The pharmaceutical composition of any of the above aspects for use in the treatment of a disease caused by EBV infection. The pharmaceutical composition of any of the above aspects for use in the treatment of multiple sclerosis. The pharmaceutical composition of any of the above aspects for use in the treatment of post- transplant lymphoproliferative disorder. The pharmaceutical composition of any of the above aspects for use in the treatment of cancers, such as gastric carcinoma, nasopharyngeal carcinoma, and lymphoma. A method of manufacturing the pharmaceutical composition of the above aspects, the method comprising: a. admixing the at least two EBV antigen-encoding mRNA constructs with an aqueous buffer, thereby obtaining an aqueous EBV antigen-encoding mRNA construct solution; b. admixing the lipids in an organic solvent, thereby obtaining a lipid solution; c. admixing the lipid solution and the aqueous EBV antigen-encoding mRNA construct solution with at least a T-mixer, a microfluidics mixer, or an impinging jet mixer, thereby obtaining a first admixture, wherein the first admixture comprises the LNPs, wherein at least some of at least two EBV antigen-encoding mRNA constructs are encapsulated in the LNPs; and d. purifying the LNPs to obtain the encapsulation by the lipids of the at least 50 mass %, at least 75 mass% of, at least 80 mass%, at least 85 mass%, at least 90 mass%, or at least 95 mass% of the at least two EBV antigen-encoding mRNA constructs. A method of manufacturing the pharmaceutical composition of the above aspects, the method comprising: a. admixing at least a first of the at least two EBV antigen-encoding mRNA constructs with an aqueous buffer, thereby obtaining a first aqueous EBV antigen-encoding mRNA construct solution; b. admixing the lipids in an organic solvent, thereby obtaining a first lipid solution; c. admixing the first lipid solution and the first aqueous EBV antigen-encoding mRNA construct solution with at least a T-mixer, a microfluidics mixer, or an impinging jet mixer, thereby obtaining a first admixture, wherein the first admixture comprises a first LNPs of the Attorney Docket No: 70488WO01 LNPs, wherein the at least the first of the at least two EBV antigen-encoding mRNA constructs are encapsulated in the first LNPs of the LNPs; d. admixing at least a second of the at least two EBV antigen-encoding mRNA constructs with the aqueous buffer, thereby obtaining a second aqueous EBV antigen-encoding mRNA construct solution; e. admixing the lipids in the organic solvent, thereby obtaining a second lipid solution; f. admixing the second lipid solution and the second aqueous EBV antigen-encoding mRNA construct solution with at least a T-mixer, a microfluidics mixer, or an impinging jet mixer, thereby obtaining a second admixture, wherein the second admixture comprises a second LNPs of the LNPs, wherein the at least the second of the at least two EBV antigen- encoding mRNA constructs are encapsulated in the second LNPs of the LNPs; g. admixing the first admixture and the second admixture and purifying the first LNPs and second LNPs to obtain the encapsulation by the lipids of the at least 50 mass %, at least 75 mass% of, at least 80 mass%, at least 85 mass%, at least 90 mass%, or at least 95 mass% of the at least two EBV antigen-encoding mRNA constructs. DESCRIPTION OF THE DRAWINGS FIG.1A shows a schematic representation of some of the recombinant proteins, which comprise LMP1, LMP2, EBNA1, EBNA3A, and ZEBRA protein fragments and which are expressed from EBV antigen T cell module constructs. FIG.1B shows a schematic representation of the EBV surface glycoproteins: gH, gL, gp42, and gp220. FIG.2 shows the expression of EBV gp220 constructs in HEK-293 cells. HEK-293 cells were electroporated with 1µg of self-amplifying messenger ribonucleic acid (SAM RNA or SAM or SAM controls) or 5µg of conventional (i.e. non-replicating mRNA, i.e. mRNA that is not SAM RNA nor trans-amplifying mRNA) (“mRNA”).24 hours post-electroporation, cells were fixed, stained, and antigen expression was detected by flow cytometry. The percent antigen-positive subset is shown. FIG.3 shows the expression of EBV gH, gL, and gp42 constructs in HEK-293 cells. HEK-293 cells were electroporated with 1µg of SAM RNA (“SAM controls”) or 5µg of conventional mRNA (“mRNA”). For co-electroporations with either two or three mRNAs 2.5µg or 2µg of each mRNA were used, respectively.24 hours post-electroporation, cells were fixed, stained, and antigen expression was detected by flow cytometry. The percent antigen positive subset is shown. FIG.4 shows a comparison of gH, gL, and gp42 mRNAs at equal moles versus equal mass on antigen expression. HEK-293 cells were electroporated with 1µg of SAM RNA or 6µg of conventional mRNA. For equal mass co-electroporations, 2µg or 1µg of each mRNA were used. For equal molar co-electroporations, 4.5 pmol or 2.2 pmol of each mRNA were used.24 hours post-electroporation, Attorney Docket No: 70488WO01 cells were fixed, stained, and antigen expression was detected by flow cytometry. The percent antigen positive subset is shown. FIG.5 shows a comparison of gH and gL mRNA ratios on antigen expression. HEK-293 cells were electroporated with different molar ratios of conventional mRNA. gH and gL were co- electroporated at a 1:1, 1:0.5, 1:2, 0.5:1, or 2:1 molar ratio where 1 = 3.4 pmol, 0.5 = 1.7 pmol, and 2 = 6.8 pmol of each mRNA used.24 hours post-electroporation, cells were fixed, stained, and antigen expression was detected by flow cytometry. The percent antigen positive subset is shown. FIG.6 shows that gp42 is co-immunoprecipitated from gH / gL in vitro. HEK-293 cells were transfected with 6µg of mRNA. For co-transfections with either two or three mRNAs 3µg or 2µg of each mRNA were used, respectively.24 hours post-transfection, cells were collected and proteins were immunoprecipitated using the AMMO1 antibody. Proteins were fractionated by SDS-PAGE and co-precipitated proteins were analyzed by immunoblotting using the BZLF2 (anti-gp42) antibody. FIG.7 shows a comparison of gp220 mRNA ratios in combination with gH / gL / gp42 mRNA on antigen expression. HEK-293 cells were electroporated with different molar ratios of conventional mRNA. gp220 mRNA was tested at different molar ratios while gH, gL, and gp42 mRNAs were kept constant at the molar ratio of 1:1:1 and will be represented as gp220 to gH / gL / gp42 ratios. gp220 and gH / gL / gp42 were co-electroporated at a 1:1, 0.5:1, and 2:1 molar ratio where 1 = 2.82 pmol, 0.5 = 1.41 pmol, and 2 = 5.64 pmol of each mRNA used.24 hours post-electroporation, cells were fixed, stained, and antigen expression was detected by flow cytometry. The percent antigen positive subset is shown. FIGS.8A-8D shows the percentage of human embryonic kidney-293 (HEK-293) cells expressing gp220 (FIG.8A), gH (FIG.8B), gL (FIG.8C), gp42 (FIG.8D) in vitro after administration of LNP RV39-formulated mRNA. Cells were transduced with (1) LNP RV39-formulated mRNA using stabilization B optimization and encoding for gp220- (gp220-SB), (2) LNP RV39-formulated mRNA encoding for gH, gL, and gp42, (3) a mix of both (1) and (2) at a 1:1 ratio ( B cell module antigens LNP gp220 + LNP (gH / gL / gp42)), (4) or LNP RV39 in which gp220-encoding, gL-encoding, gH- encoding, and gp42 encoding mRNAs were co-formulated ( B cell module antigens LNP co- formulated). Each sample was added in a serial dilution, 8 points. The LNP-RNA dose corresponds to the mRNA expressing the antigen analyzed to allow comparison of different formulations.24 post- transfection, cells were fixed, permeabilized and specifically stained for antigen expression as stated and analyzed by flow cytometry (iQue3). Data are presented by percentage of cells positive for each antigen expression (n=3). FIGS.9A and 9B show a comparison of T cell FL1 antigen expression in SAM vs conventional mRNA backbone. BHK cells were transfected with 5µg of mRNA. In FIG.9A, 18 hours post electroporation, cells were collected, proteins were fractionated by SDS-PAGE and analyzed by immunoblotting using the LMP1 (Abcam) antibody. In FIG.9B, 18 hours post electroporation, cells Attorney Docket No: 70488WO01 were fixed, stained, and antigen expression of LMP1 (Diagnostic BioSystems) was detected by flow cytometry. The percent antigen positive subset is shown. FIG.10 shows the time course to determine optimal protein expression of HA-tagged hli FL1. HEK-293 cells were mock transfected (“Mock”) or transfected with 5µg of HA-tagged hli FL1 mRNA (SEQ ID NO: 115, “hli FL1-HA”). Cells were treated with DMSO or MG1324 hours post electroporation. Cells were collected at 6, 24, or 48 hours post electroporation and proteins were concentrated 8X. Proteins were fractionated by SDS-PAGE and analyzed by immunoblotting using the ubiquitin or HA-tag antibodies. FIG.11 shows the detection of HA-tagged hli FL1 mRNA constructs. HEK-293 cells were transfected or mock transfected with 5µg of each mRNA (hli FL1-HA, hli FL1.1A-HA, hli FL1.1B-HA, hli FL1.2A-HA, hli FL1.2B-HA, and hli FL1.2C-HA). Cells were collected 24 hours post- electroporation, and protein were concentrated 10X. Proteins were fractionated by SDS-PAGE and analyzed by immunoblotting using the HA-tag or LMP1 antibodies. Actin was used as a loading control. FIG.12 shows the expression of T mosaic antigens by mass spectroscopy in HEK 293 cells following electroporation. Representative chromatograms for each peptide measured for the assay are shown. Selection of retention time windows (x-axes) and target b and y fragment ions (shown in chart legends) was aided by matching elution profiles and fragment ion patterns of isotope-labeled synthetic peptide standards (not shown). The abundance of each peptide was determined by summing the area under the curve for each fragment ion and normalizing it to the synthetic internal standard. Extracted ion chromatograms of EBV antigen peptide targets show high signal-to-noise ratio for at least 3 fragment ions from each peptide. FIG.13 shows that the 3-split construct reproducibly expresses most highly throughout the length of the sequence. The left graph shows normalized peptide abundance (normalized by peak area integration) from a triplicate analysis experiment, and the both the right and left graphs illustrate that highest abundance in the 3-split construct samples throughout the length of the constructs, with a mean intensity of ~12% of the 10 fmol / uL internal standard. FIG.14 shows a comparison of addition of T cell mRNAs to B cell mRNAs on antigen expression. LNPs containing mRNAs were transfected into HEK-293 cells. LNPs contained B cell mRNAs gH, gL, and gp42, T cell mRNA FL1 full length (FL1), or T cell mRNAs FL1.2A, FL1.2B, and FL1.2C (FL13-split). B cell LNPs were tested at 5 ng, 2.5 ng, and 1.25 ng as positive controls where 1 = 5n g, 0.5 = 2.5 ng, and 0.25 = 1.25 ng of LNPs used. B cell LNPs combined with T cell LNPs were tested at different ratios of 1:1, 1:0.5, and 1: 0.25, where the B cell LNPs were kept constant. B cell LNPs combined with T cell LNPs were tested at different ratios of 0.5:1 and 0.25:1, where the T cell LNPs were kept constant.24 hours post-transfection, cells were fixed, stained, and antigen Attorney Docket No: 70488WO01 expression was detected by flow cytometry. The percent antigen positive subset (%488+) times geomean (intensity) is shown. FIG.15 shows in vitro expression of gp220 when both LNP-formulated modules are co- transduced in HEK-293 cells. Cells were transduced with RV39-formulated mRNA encoding for B cell module antigens or a mix of Ab / T ell module at the indicated ratio. Each sample was added in a serial dilution, 8 points. The LNP-RNA dose corresponds to the mRNA expressing gp220 antigen to allow comparison of different combo mix.24 post-transduction, cells were fixed, permeabilized and specifically stained for gp220 antigen expression and analyzed by flow cytometry (iQue3). Data are presented by percentage of cells positive for each antigen expression (n=3). FIG.16 shows the immunogenicity of EBV-T module mRNA in DC-T cell co-culture. Induction of robust T Cell responses by DCs electroporated with EBV-T module mRNA was observed. Immature DCs underwent electroporation with full-length, 2-split, and 3-split-mosaic T module mRNAs, in the presence or absence of hli integration, and were then cocultured with autologous T cells isolated from EBV-positive human donors (IMXP00647, IMXP00361 and IMXXP01057). For positive controls, mosaic EBV peptide pulsing was utilized, while negative controls were established via mock electroporation or GFP mRNA electroporation. After 24-hour incubation, the co-cultures of T cells and mRNA-electroporated / peptide-loaded mature DCs were assessed using the IFN-γ FluoroSpot assay. Spot-forming cells (SFCs) were quantified as a measure of IFN-γ response. FIGS.17A-17F show EBV antigen-specific CD8+ T cell responses to mRNA-vaccine candidates in vitro. Memory CD8+T cell responses to mRNA-LNP formulations in vitro in ten different EBV-positive donors are shown. % CD8+T IFNγ+TNFα+DP cells were detected after nine days PBMC culture followed by 4-hour peptide stimulation. Responses to EBNA1 (FIG.17A), EBNA3A (FIG.17B), LMP1 (FIG.17C), LMP2 (FIG.17D), ZEBRA (a.k.a. BZFL1) (FIG.17E), and EBV-negative donor (FIG.17F) are shown. Controls include cells stimulated with empty LNPs, EBV mosaic peptide pool mix, and MILTENYI BIOTECH®PEPTIVATOR®EBV Consensus or unstimulated. LOD: limit of detection. FL1: full-length T cell module mosaic; 1A+1B: 2-split T cell module mosaic; 2A+2B+2C: 3-split T cell module mosaic. FIG.18 shows an overview of CD8+T cell responses to proteins in the Mosaic construct. Heatmap of memory CD8+T cell responses to mRNA-LNP formulations (1, 0.5, 0.25 mg / ml) were detected in vitro in ten different donors. % CD8+T IFNγ+TNFα+DP cell responses against EBV peptide pools are shown. FL1: full-length T cell module mosaic; 1A+1B: 2-split T cell module mosaic; 2A+2B+2C: 2-split T cell module mosaic. FIG.19 shows that EBV gp220-specific binding antibodies were detected after immunizing mice with gp220-FL (mRNA construct encoding full-length EBV gp220), gp220-TM (mRNA construct encoding EBV gp220 with transmembrane domain and intracellular domain), gp220-NP (mRNA construct encoding EBV gp220 with ferritin domain that forms nanoparticles), and SAM gp220-FL (self-amplifying mRNA construct encoding full-length EBV gp220; positive control). EBV gp220- Attorney Docket No: 70488WO01 specific binding antibodies were analyzed by ELISA after mice were immunized with gp220-FL, gp220-TM gp220-NP, and SAM gp220-FL. Conventional graph (GMT ± 95% CI) showing the gp220 binding antibodies is shown. A geometric mean titer (GMT) is the average antibody titer for a group of subjects calculated by multiplying all values and taking the nth root of the number, where n is the number of subjects with available data. * indicates statistical significance. FIGS. 20A-20F showgeometric mean ratio (GMR) graphs of EBV gp220 / gp350-specific bindingantibodies after immunization with gp220 constructs at 21-days (FIGS.20A, 20C, and 20E) and 35- days (FIGS.20B, 20D, and 20F) after initial administration. GMR graphs for EBV gp220 / gp350- specific binding antibodies after immunization with gp220-FL, gp220-TM gp220-NP, and SAM gp220- FL are shown. Arrow indicates statistical significance. FIG.21 shows EBV B cell neutralizing antibodies analyzed using Raji cell after immunization with gp220-FL, gp220-TM gp220-NP, and SAM gp220-FL. Conventional graph (GMT ± 95% CI) showing the EBV neutralizing antibodies analyzed with Raji cell is shown. * indicates statistical significance. FIGS.22A, 22B, and 22C show GMR graphs of EBV B cell neutralizing antibodies analyzed using Raji cells after immunization with gp220 constructs, gp220-FL, gp220-TM gp220-NP, and SAM gp220-FL. FIG.22A shows the neutralizing antibody titers, and FIGS.22B and 22C illustrates the fold-changes across selected groups (see FIG.22A for group labels). FIGS.23A, 23B, and 23C show GMR graphs of EBV neutralizing antibodies analyzed using HEK-293 cells after immunization with gp220 constructs, gp220-FL, gp220-TM gp220-NP, and SAM gp220-FL, are shown. FIGS.24A, 24 B, and 24C show that EBV gH / gL-specific binding antibodies were detected after immunization with gH / gL / gp42, gH / gL and gp42 mRNA constructs. EBV gH / gL-specific binding antibodies were analyzed with ELISA after immunization with gH / gL / gp42, gH / gL and gp42 mRNA constructs. FIG.24A is a conventional graph (GMT ± 95% CI) showing the gH / gL binding antibodies, * indicates statistical significance. FIGS.24B and 24C shows the same data as FIG.24A, with the GMT values additionally indicated on the x-axis, and with day 21 results on FIG.24B and day 35 results on FIG.24C. FIGS.25A-25F show GMR graphs of EBV gH / gL binding antibodies on day 21 (FIGS.25A, 25C, and 25E) and day 35 (FIGS.25B, 25D, and 25F) after immunization with gH / gL / gp42, gH / gL and gp42 mRNA constructs. EBV gH / gL-specific binding antibodies were detected after immunization with gH / gL / gp42, gH / gL and gp42 mRNA constructs. Arrow indicates statistical significance. FIGS.26A, 26B, and 26C show EBV gp42-specific binding antibodies on day 21 (FIGS.26A and 26B) and day 36 (FIGS.26A and 26C) after immunization with gH / gL / gp42, gH / gL and gp42 mRNA constructs. EBV gp42-specific binding antibodies were analyzed with ELISA after immunization with gH / gL / gp42, gH / gL and gp42 mRNA constructs. FIG.26A: conventional graph (GMT ± 95% CI) Attorney Docket No: 70488WO01 showing the gp42 binding antibodies, * indicates statistical significance. FIG.26B: shows the same data as FIG.26A, with the GMT values additionally indicated on the x-axis. FIGS.27A-27F show GMR graphs of EBV gp42-specific binding antibodies on day 21 (FIGS. 27A, 27C, and 27E) and day 35 (FIGS.27B, 27D, and 27F) after immunization with gH / gL / gp42, gH / gL and gp42 mRNA constructs. EBV gp42-specific binding antibodies were analyzed with ELISA after immunization with gH / gL / gp42, gH / gL and gp42 mRNA constructs. Arrow indicates statistical significance. FIGS.28A and 28B show EBV B cell neutralizing antibodies (Raji cell assay) after immunization with gH / gL / gp42, gH / gL, gp42 mRNA constructs and SAM gH / gL / gp42. FIG.28A: conventional graph (GMT ± 95% CI) showing the EBV neutralizing antibodies analyzed with Raji cell, * indicates statistical significance. FIG.28B: shows the same data as FIG.28A, with the GMT values additionally indicated on the x-axis. FIGS.29A, 29B, and 29C show GMR graphs of EBV neutralizing antibodies analyzed using Raji cell assay after immunization with gH / gL / gp42, gH / gL, gp42 mRNA constructs and SAM gH / gL / gp42. FIGS.30A and 30B show EBV epithelial cell neutralizing antibodies analyzed using HEK-293 cells after immunization with gH / gL / gp42, gH / gL and gp42 conventional mRNA constructs and SAM gH / gL / gp42 constructs. FIG.30A: conventional graph (GMT ± 95% CI) showing the EBV neutralizing antibodies analyzed with HEK-293 cells, * indicates statistical significance. FIG.30B: shows the same data as FIG.30A, with the GMT values additionally indicated on the x-axis. FIGS.31A-31H show GMR graphs of EBV neutralizing antibodies analyzed using HEK-293 cells on day 21 (FIGS.31A, 31C, 31E, and 31G) and day 35 (FIGS.31B, 31D, 31F, and 31H) after immunization with gH / gL / gp42, gH / gL and gp42 conventional mRNA constructs and SAM gH / gL / gp42 constructs. FIG.32 shows EBV neutralizing antibody titers in Raji B cells after 35 days of immunization with gp220-FL, gH / gL / gp42 and gH / gL, stabilization B- (SB-) optimized gp220-FL, gH / gL / gp42 and gH / gL, as well as the combination of gp220-FL + gH / gL / gp42, stabilization B-optimized gp220-FL + gH / gL / gp42 and stabilization B-optimized gp220-FL+ gH / gL constructs. FIG.32 depicts a conventional graph (GMT ± 95% CI) showing the EBV neutralizing antibodies analyzed with Raji cells. FIG.33 shows EBV neutralizing antibody titers in HEK-293 epithelial cells after 35 days of immunization with gp220-FL, gH / gL / gp42 and gH / gL, stabilization B-optimized gp220-FL, gH / gL / gp42 and gH / gL, as well as the combination of gp220-FL + gH / gL / gp42, stabilization B- optimized gp220-FL + gH / gL / gp42 and stabilization B-optimized gp220-FL+ gH / gL constructs. FIG. 33 depicts a conventional graph (GMT ± 95% CI) showing the EBV neutralizing antibodies analyzed with HEK-293 epithelial cells. Attorney Docket No: 70488WO01 FIGS.34A and 34B depict conventional graphs (GMT ± 95% CI) showing the EBV neutralizing antibodies analyzed with Raji cells (FIG.34A) and HEK-293 epithelial cells (FIG.34B). FIG.34A shows EBV neutralizing antibody titers in Raji B cells after 21 days of immunization with gp220-FL, gH / gL / gp42 and gH / gL, stabilization B-optimized gp220-FL, gH / gL / gp42 and gH / gL, as well as the combination of gp220-FL + gH / gL / gp42, stabilization B-optimized gp220-FL + gH / gL / gp42 and SB- optimized gp220-FL+ gH / gL constructs. FIG.34B shows EBV neutralizing antibody titers in HEK-293 epithelial cells after 21 days of immunization with gp220-FL, gH / gL / gp42 and gH / gL, stabilization B- optimized gp220-FL, gH / gL / gp42 and gH / gL, as well as the combination of gp220-FL + gH / gL / gp42, stabilization B-optimized gp220-FL + gH / gL / gp42 and stabilization B-optimized gp220-FL+ gH / gL constructs. FIG.35 shows the Boolean sum of total EBV antigen-specific CD4+ and CD8+ T cell responses. EBV antigen-specific CD8+ (top panel) and CD4+ (bottom panel) T cell responses were measured using multi-parameter flow cytometry with intracellular cytokine staining after stimulation of mouse splenocytes with peptide libraries specific for EBNA1, EBNA3A, LMP1, LMP2, and ZEBRA (a.k.a. BZFL1). The bars represent each of the five EBV antigens tested. Data shown are arithmetic means ± SEM. Statistically significant differences in the total EBV antigen-specific T cell response between vaccine groups are highlighted by an asterisk. FIG.36 shows phenotypic Tc / Th Subsets for immunodominant CD8+ / CD4+ EBV antigen. Antigen-specific CD8+ and CD4+ T cell responses were measured by multi-parameter flow cytometry with intracellular cytokine staining after stimulation of mouse splenocytes with peptide libraries specific for EBNA1, EBNA3A, LMP1, LMP2, and ZEBRA (a.k.a. BZFL1). The data represent the antigen-specific response to the immunodominant CD8 LMP2 antigen (top panel) and the immunodominant CD4 EBNA1 antigen (bottom panel). The data are displayed as the sum total of the antigen-specific response categorized into T cytotoxic (Tc) phenotypic (top panel) subsets or T helper (Th) phenotypic (bottom panel) subsets. Each bar represents a different phenotypic subset. Data are displayed as arithmetic Mean ±SEM. Statistically significant differences between vaccine groups are highlighted by an asterisk. FIG.37 shows CD8 / CD4+ T cell response to Individual EBV Mosaic Fragments. EBV antigen- specific CD8+ (top panel) and CD4+ (bottom panel) T cell responses were measured using multi- parameter flow cytometry with intracellular cytokine staining after stimulation of mouse splenocytes with peptide libraries specific for the individual mosaic fragment regions for EBNA1, EBNA3A, LMP1, LMP2, and ZEBRA analyzing across the FL1 protein from N-terminus (“FIG.37”) to C-terminus (“FIG.37 (cont-2)”). The data represent the Boolean sum-total of the EBV antigen-specific CD8+ or CD4+ T cell response. FIG.38 shows the Boolean sum of total EBV antigen-specific CD4+ and CD8+ T cell responses. EBV antigen-specific CD8+ (top panel) and CD4+ (bottom panel) T cell responses were measured Attorney Docket No: 70488WO01 using multi-parameter flow cytometry with intracellular cytokine staining after stimulation of mouse splenocytes with peptide libraries specific for EBNA1, EBNA3A, LMP1, LMP2, and ZEBRA (a.k.a. BZFL1). The data represent the Boolean sum-total of the EBV antigen-specific CD8+ or CD4+ T cell response. The bars represent each of the five EBV antigens tested. Data shown are arithmetic means ± SEM. Statistically significant differences in the total EBV antigen-specific T cell response between vaccine groups are highlighted by an asterisk. FIG.39 shows EBV antigen-specific CD8+ and CD4+ T cell responses for the mosaic junction regions. EBV antigen-specific CD8+ and CD4+ T cell responses were measured using multi- parameter flow cytometry with intracellular cytokine staining after stimulation of mouse splenocytes with peptide libraries specific for the mosaic junction regions spanning 12 amino acids (6 / 6) or 14 amino acids (7 / 7) in either direction at the mosaic junction. Peptides were designed to cover all junctions across the full length of the mosaic. Data shown represent the antigen-specific response for the individual mice within each group displayed as arithmetic Mean ±SEM. FIG.40 shows total EBV antigen-specific CD8+ T cell response elicited by EBV full-length T cell module mosaic mRNA and SAM FL1 constructs. Antigen-specific CD8+ T cell responses were measured by multi-parameter flow cytometry with intracellular cytokine staining after stimulation of mouse splenocytes with pooled peptides specific for EBNA1, EBNA3A, LMP1, LMP2, and ZEBRA (a.k.a. BZFL1). The data are displayed as the sum total of the antigen-specific response and each bar represents the CD8+ T cell response to a different antigen. Data shown represent the antigen- specific CD8+ T cell response displayed as arithmetic Mean ± SEM. Statistically significant differences between vaccine groups as computed geometric means with 95% CI are indicated by an asterisk. FIGS.41A and 41B show LMP2-specific CD8+ T cell response elicited by SAM FL1 vs mRNA FL1 ± hli. Antigen-specific CD8+ T cell responses were measured by multi-parameter flow cytometry with intracellular cytokine staining after stimulation of mouse splenocytes with pooled peptides specific for EBNA1, EBNA3A, LMP1, LMP2, and ZEBRA (a.k.a. BZFL1). The data represent the antigen-specific response for the immunodominant LMP2 antigen. Data shown represent the LMP2- specific response for the individual mice within each group displayed as arithmetic Mean ± SEM. Statistically significant differences between vaccine groups as computed geometric means with 95% CI are indicated by an asterisk. SAM-FL1 construct (0.15 µg) induced significantly higher IL-2 (FIG. 41B), TNFα, IFN-γ and CD107a (FIG.41A) production as compared to mRNA FL1 and / or hli mRNA FL1 (5 µg). FIGS.42A-42D show LMP2-specific CD8+ T cell response elicited by mRNA FL1 v Fragments and their counterparts with hli. Antigen-specific CD8+ T cell responses were measured by multi- parameter flow cytometry with intracellular cytokine staining after stimulation of mouse splenocytes with pooled peptides specific for EBV LMP2. Data shown represent the LMP2-specific response for Attorney Docket No: 70488WO01 the individual mice within each group displayed as arithmetic Mean ± SEM, and statistically significant differences between vaccine groups as computed geometric means with 95% CI are indicated by an asterisk. mRNA-FL construct in 3 fragments induced significantly higher IL-2 and IFN-γ compared to its counterpart with hli. FIG.42A: IFN-g; FIG.42B: CD107a; FIG.42C: TNF-a; FIG.42D: IL-2. FIG.43 shows distribution of phenotypic subsets of LMP2-specific CD8+ T cells in mouse spleens 2wp2 (SD35). Antigen-specific CD8+ T cell responses were measured by multi-parameter flow cytometry with intracellular cytokine staining after stimulation of mouse splenocytes with pooled peptides specific EBV LMP2. The data are displayed as the sum total of the LMP2-specific response categorized into T cytotoxic (Tc) phenotypic subsets. Each bar represents a different Tc subset. Data shown represent the LMP2-specific CD8+ T cell response displayed as arithmetic Mean ± SEM. Statistically significant differences between vaccine groups as computed geometric means with 95% CI are indicated by an asterisk. SAM-FL1 (0.15 µg) elicited significantly higher LMP2-specific Tc1 response compared to mRNA-FL1 ± hli (5 µg). FIG.44 shows total EBV antigen-specific CD8+ T cell response elicited by EBV full-length T cell module mosaic conventional mRNA and SAM FL1 constructs. Antigen-specific CD8+ T cell responses were measured by multi-parameter flow cytometry with intracellular cytokine staining after stimulation of mouse splenocytes with pooled peptides specific for EBNA1, EBNA3A, LMP1, LMP2, and ZEBRA (a.k.a. BZFL1). The data are displayed as the sum total of the antigen-specific response and each bar represents the CD8+ T cell response to a different antigen. Data shown represent the antigen- specific CD8+ T cell response displayed as arithmetic Mean ± SEM. Statistically significant differences between vaccine groups as computed geometric means with 95% CI are indicated by an asterisk. FIG.45A-45D show LMP1-specific CD4+ T cell response elicited by SAM-FL1 constructs and conventional mRNA FL1 constructs with and without further encoding of hli. Antigen-specific CD4+ T cell responses were measured by multi-parameter flow cytometry with intracellular cytokine staining (IFN-γ: FIG.45A; IL-5 / IL-13: FIG.45B; IL-2: FIG.45C; TNF-α: FIG.45D) after stimulation of mouse splenocytes with pooled peptides specific for EBV LMP1. Data shown represent the LMP1-specific response for the individual mice within each group displayed as arithmetic Mean ± SEM, and statistical analysis with geometric means with 95% CI showed no significant difference. FIG.46 shows distribution of phenotypic subsets of LMP1-specific CD4+ T cell in mouse spleens 2wp2 (SD35). Antigen-specific CD4+ T cell responses were measured by multi-parameter flow cytometry with intracellular cytokine staining after stimulation of mouse splenocytes with pooled peptides specific for EBV LMP1. The data are displayed as the sum total of the LMP1-specific response categorized into Helper T (Th) phenotypic subsets. Each bar represents a different Th subset. Data shown represent the LMP1-specific CD4+ T cell response displayed as arithmetic Mean Attorney Docket No: 70488WO01 ± SEM. Statistically significant differences between vaccine groups as computed geometric means with 95% CI are indicated by an asterisk. LMP1 induced a Th0 dominant CD4+ T cell response with a high Th2 background. FIGS.47A-47D show LMP2-specific CD4+ T cell response elicited by SAM-FL1 constructs and conventional mRNA FL1 constructs with and without further encoding of hli antigen-specific CD4+ T cell responses were measured by multi-parameter flow cytometry with intracellular cytokine staining (IFN-γ: FIG.45A; IL-5 / IL-13: FIG.45B; IL-2: FIG.45C; TNF-α: FIG.45D) after stimulation of mouse splenocytes with pooled peptides specific for EBV LMP2. Data shown represent the LMP2-specific response for the individual mice within each group displayed as arithmetic Mean ± SEM. Statistically significant differences between vaccine groups as computed geometric means with 95% CI are indicated by an asterisk. FIG.48 shows distribution of phenotypic subsets of LMP2-specific CD4+ T cells in mouse spleens 2wp2 (SD35). Antigen-specific CD4+ T cell responses were measured by multi-parameter flow cytometry with intracellular cytokine staining after stimulation of mouse splenocytes with pooled peptides specific for EBV LMP2. The data are displayed as the sum total of the LMP2-specific response categorized into Helper T (Th) phenotypic subsets. Each bar represents a different Th subset. Data shown represent the LMP2-specific CD4+ T cell response displayed as arithmetic Mean ± SEM. Statistically significant differences between vaccine groups as computed geometric means with 95% CI are indicated by an asterisk. Similar to LMP1, LMP2 induced a Th0 dominant CD4+ T cell response with a high Th2 background. FIG.49 shows an embodiment of a schematic representation of full length EBNA1 protein (SEQ ID NO: 12) and EBNA1 protein fragments. EBNA1 fragment 1: amino acids 1-22 and 66-86 of SEQ ID NO: 12 (i.e., SEQ ID NO: 13); EBNA1 fragment 2: amino acids 454-503 of SEQ ID NO: 12 (i.e., SEQ ID NO: 14); EBNA1 fragment 3: amino acids 504-619 of SEQ ID NO: 12 (i.e., SEQ ID NO: 15). FIG.50 shows the methods for making the formulations used in Example 17, which include co- formulating the EBV antigen-encoding mRNA constructs encoding the T cell module antigens and encoding the B cell module antigens versus separately formulating within the LNPs the EBV antigen- encoding mRNA constructs encoding the T cell module antigens and the EBV antigen-encoding mRNA constructs encoding the B cell module antigens and then combining the separately formulated LNPs (called “co-filling”). FIG.51 shows the percent of activated EBV antigen-specific CD44+ cells in a population of CD4+ T cells and demonstrates that co-formulation and co-filling of EBV antigen-encoding mRNA constructs encoding T cell module proteins and encoding B cell module proteins initiates T cell responses to each of EBNA1, EBNA3A, LMP1, LMP2, and ZEBRA (a.k.a. BZLF1). FIG.52 shows the percent of activated EBV antigen-specific CD44+ cells in a population of CD8+ T cells and demonstrates that co-formulation and co-filling of EBV antigen-encoding mRNA Attorney Docket No: 70488WO01 constructs encoding T cell module proteins and encoding B cell module proteins initiates T cell responses to each of EBNA1, EBNA3A, LMP1, LMP2, and ZEBRA (a.k.a. BZLF1). FIGS.53A-53H show that neutralizing antibody titers against EBV virions were robust both on day 21 and on day 35 after the first administration of mRNA constructs encoding the T cell module antigens combined with the mRNA constructs encoding the B cell module in groups designed to evaluate varying degrees of co-formulating or co-filling the mRNA constructs prior to the administration. Co-formulation and co-filling, and thereby co-administration, of the mRNA constructs encoding the T cell module antigens with the mRNA constructs encoding the B cell module antigens does not prevent a robust neutralizing antibody response to the B cell module antigens—gH, gL, gp42, and gp220—that are responsible for EBV virion infection of B cells and epithelial cells. FIG.54 shows the conditions for Example 18. FIGS.55A, 55B, and 55C show IgG antibody titers against gp350 / gp220, gH and gL, and gp42, respectively, from the sera obtained at day 21 and day 35 from the CB6F1 mice for groups 2, 3, 6, 10, and 11 as shown in FIG.54. FIGS.56A, 56B, and 56C show IgG antibody titers against gp350 / gp220, gH and gL, and gp42, respectively, from the sera obtained at day 21 and day 35 from the CD1 mice for groups 2, 3, 6, 10, and 11 as shown in FIG.54. FIGS.57A, 57B, and 57C show IgG antibody titers against gp350 / gp220, gH and gL, and gp42, respectively, from the sera obtained at day 21 and day 35 from the CB6F1 mice for groups 6, 7, 8, 9, and 10 as shown in FIG.54. FIGS.58A, 58B, and 58C show IgG antibody titers against gp350 / gp220, gH and gL, and gp42, respectively, from the sera obtained at day 21 and day 35 from the CD1 mice for groups 6, 7, 8, 9, and 10 as shown in FIG.54. FIGS.59A, 59B, and 59C show IgG antibody titers against gp350 / gp220, gH and gL, and gp42, respectively, from the sera obtained at day 21 and day 35 from the CB6F1 mice for groups 3, 10, and 13 as shown in FIG.54. FIGS.60A, 60B, and 60C show IgG antibody titers against gp350 / gp220, gH and gL, and gp42, respectively, from the sera obtained at day 21 and day 35 from the CD1 mice for groups 3, 10, and 13 as shown in FIG.54. FIG.61 provides an overview of the methods used in Example 19 on human peripheral blood monocyte cells. FIGS.62A, 62B, and 62C provide the pre-existing immune responses to EBNA1, EBNA3A, LMP1, LMP2, and ZEBRA (BZLF1) for donor 2 (FIG.62A), donor 7 (FIG.62B), and donor 15 (FIG. Attorney Docket No: 70488WO01 62C) without stimulation or with stimulation of a peptide mix from FL1 or the EBV peptide mix described in the methods of the examples. FIGS.63A, 63B, and 63C show that each of mRNA transfected mDCs from donor 2 could stimulate the CD8+ T cells regardless of whether the cells were expanded with the peptide mix described above (PEPMIX) or EBNA1, or LMP2. When expanded with the PEPMIX there was a preference for mRNA encoding LMP2b with alternative UTRs, mRNA encoding LMP2a, and mRNA encoding LMP2b, and finally with a preference for mRNA encoding EBNA1 (FIG.63A). FIGS.64A, 64B, and 64C show that the combined transfection with mRNA encoding FL1.2A, mRNA encoding FL1.2B, or mRNA encoding FL1.2C of mDCs from donor 2 could stimulate the CD8+ T cells regardless of whether the cells were expanded with the peptide mix described above (PEPMIX) or EBNA1, or LMP2. FIGS.65A, 65B, 65C, and 65D show that each of mRNA transfected mDCs from donor 7 could stimulate the CD8+ T cells regardless of whether the cells were expanded with PEPMIX or EBNA1, EBNA3A, or ZEBRA (BZLF1). When expanded with the PEPMIX there was a preference for mRNA encoding EBNA3A with alternative UTRs and mRNA encoding BZLF1, and then mRNA encoding EBNA1 (FIG.65A). FIGS.66A, 66B, 66C, and 66D demonstrate that the combined transfection with mRNA encoding FL1.2A, mRNA encoding FL1.2B, or mRNA encoding FL1.2C of mDCs from donor 7 could stimulate the CD8+ T cells regardless of whether the cells were expanded with PEPMIX or EBNA1, EBNA3A, or ZEBRA (BZLF1). FIG.67A demonstrates that mRNA-transfected mDCs from donor 15 could stimulate the CD8+ T cells when the cells were expanded with LMP1. FIG.67B shows that combined transfection with mRNA encoding FL1.2A, mRNA encoding FL1.2B, or mRNA encoding FL1.2C of mDCs from donor 15 could stimulate the CD8+ T cells expanded with LMP1. DESCRIPTION OF THE SEQUENCES SEQ ID NO: 1 EBV LMP1 protein (Genbank No. P03230) SEQ ID NO: 2 immunogenic fragment 1 of EBV LMP1 protein SEQ ID NO: 3 immunogenic fragment 2 of EBV LMP1 protein SEQ ID NO: 4 immunogenic fragment 3 of EBV LMP1 protein SEQ ID NO: 5 immunogenic fragment 4 of EBV LMP1 protein SEQ ID NO: 6 EBV LMP2A protein (Genbank No. P13285) SEQ ID NO: 7 EBV LMP2B protein (Genbank No. P13285) SEQ ID NO: 8 immunogenic fragment 1 of EBV LMP2A and LMP2B proteins Attorney Docket No: 70488WO01 SEQ ID NO: 9 immunogenic fragment 2 of EBV LMP2A and LMP2B proteins SEQ ID NO: 10 immunogenic fragment 3 of EBV LMP2A and LMP2B proteins SEQ ID NO: 11 immunogenic fragment 4 of EBV LMP2A and LMP2B proteins SEQ ID NO: 12 EBNA1 protein (Genbank No. P03211) SEQ ID NO: 13 immunogenic fragment 1 of EBNA1 protein SEQ ID NO: 14 immunogenic fragment 2 of EBNA1 protein SEQ ID NO: 15 immunogenic fragment 3 of EBNA1 protein SEQ ID NO: 16 EBNA3A protein (Genbank No. YP401669) SEQ ID NO: 17 immunogenic fragment 1 of EBNA3A protein SEQ ID NO: 18 immunogenic fragment 2 of EBNA3A protein SEQ ID NO: 19 immunogenic fragment 3 of EBNA3A protein SEQ ID NO: 20 immunogenic fragment 4 of EBNA3A protein SEQ ID NO: 21 immunogenic fragment 5 of EBNA3A protein SEQ ID NO: 22 immunogenic fragment 6 of EBNA3A protein SEQ ID NO: 23 immunogenic fragment 7 of EBNA3A protein SEQ ID NO: 24 EBV ZEBRA (BZLF1) protein (Genbank No. P03206) SEQ ID NO: 25 immunogenic fragment 1 of ZEBRA (BZLF1) protein SEQ ID NO: 26 immunogenic fragment 2 of ZEBRA (BZLF1) protein SEQ ID NO: 27 FL1 protein SEQ ID NO: 28 FL1 mRNA stabilization A (no split) open reading frame (ORF) SEQ ID NO: 29 FL1.1A protein (2-split) SEQ ID NO: 30 FL1.1A mRNA stabilization A ORF SEQ ID NO: 31 FL1.1B protein (2-split) SEQ ID NO: 32 FL1.1B mRNA stabilization A ORF SEQ ID NO: 33 FL1.2A protein (3-split) SEQ ID NO: 34 FL1.2A mRNA stabilization A ORF SEQ ID NO: 35 FL1.2B protein (3-split) SEQ ID NO: 36 FL1.2B mRNA stabilization A ORF SEQ ID NO: 37 FL1.2C protein (3-split) SEQ ID NO: 38 FL1.2C mRNA stabilization A ORF SEQ ID NO: 39 gH protein SEQ ID NO: 40 gH mRNA stabilization A ORF SEQ ID NO: 41 gL protein SEQ ID NO: 42 gL mRNA stabilization A ORF SEQ ID NO: 43 gp42 protein SEQ ID NO: 44 gp42 mRNA stabilization A ORF SEQ ID NO: 45 gp220 protein SEQ ID NO: 46 gp220 mRNA stabilization B ORF Attorney Docket No: 70488WO01 SEQ ID NO: 47 Tissue plasminogen activator (tPA) signal peptide SEQ ID NO: 48 5’ untranslated region (UTR) 4 SEQ ID NO: 49 3’ UTR4 SEQ ID NO: 50 5’ UTR3 SEQ ID NO: 51 3’ UTR3 SEQ ID NO: 52 5’ UTR7 SEQ ID NO: 53 3’ UTR7 SEQ ID NO: 54 poly(A)-1 Tail (A80) SEQ ID NO: 55 poly(A)-2 Tail (A30-GCATATGACT-A35) SEQ ID NO: 56 poly(A)-3 Tail (A24-GCATATGACT-A50) SEQ ID NO: 57 poly(A)-4 Tail (A27-GCATATGACT-A35) SEQ ID NO: 58 Full length gH mRNA stabilization A, no poly(A), no cap SEQ ID NO: 59 Full length gH mRNA stabilization A, cap, no poly(A) SEQ ID NO: 60 Full length gH mRNA stabilization A, poly(A), and cap SEQ ID NO: 61 Full length gH Plasmid stabilization A SEQ ID NO: 62 Full length gL mRNA stabilization A, no poly(A), no cap SEQ ID NO: 63 Full length gL mRNA stabilization A, cap, no poly(A) SEQ ID NO: 64 Full length gL mRNA stabilization A, poly(A), and cap SEQ ID NO: 65 Full length gL Plasmid stabilization A SEQ ID NO: 66 Full length gp42 mRNA stabilization A, no poly(A), no cap SEQ ID NO: 67 Full length gp42 mRNA stabilization A, cap, no poly(A) SEQ ID NO: 68 Full length gp42 mRNA stabilization A, poly(A), and cap SEQ ID NO: 69 Full length gp42 Plasmid stabilization A SEQ ID NO: 70 Full length gp220 mRNA stabilization B, no poly(A), no cap SEQ ID NO: 71 Full length gp220 mRNA stabilization B, cap, no poly(A) SEQ ID NO: 72 Full length gp220 mRNA stabilization B, poly(A), and cap SEQ ID NO: 73 Full length gp220 Plasmid stabilization B SEQ ID NO: 74 FL1.2A (3-split) mRNA stabilization A, no poly(A), no cap SEQ ID NO: 75 FL1.2A (3-split) mRNA stabilization A, cap, no poly(A) SEQ ID NO: 76 FL1.2A (3-split) mRNA stabilization A, poly(A), and cap SEQ ID NO: 77 FL1.2A (3-split) Plasmid stabilization A SEQ ID NO: 78 FL1.2B (3-split) mRNA stabilization A, no poly(A), no cap SEQ ID NO: 79 FL1.2B (3-split) mRNA stabilization A, cap, no poly(A) SEQ ID NO: 80 FL1.2B (3-split) mRNA stabilization A, poly(A), and cap SEQ ID NO: 81 FL1.2B (3-split) plasmid stabilization A SEQ ID NO: 82 FL1.2C (3-split) mRNA stabilization A, no poly(A), no cap SEQ ID NO: 83 FL1.2C (3-split) mRNA stabilization A, cap, no poly(A) SEQ ID NO: 84 FL1.2C (3-split) mRNA stabilization A, poly(A), and cap Attorney Docket No: 70488WO01 SEQ ID NO: 85 FL1.2C (3-split) Plasmid stabilization A SEQ ID NO: 86 FL1 mRNA stabilization A, no poly(A), no cap SEQ ID NO: 87 FL1 mRNA stabilization A, cap, no poly(A) SEQ ID NO: 88 FL1 mRNA stabilization A, poly(A), and cap SEQ ID NO: 89 FL1.1A (2-split) mRNA stabilization A, no poly(A), no cap SEQ ID NO: 90 FL1.1A (2-split) mRNA stabilization A, cap, no poly(A) SEQ ID NO: 91 FL1.1A (2-split) mRNA stabilization A, poly(A), and cap SEQ ID NO: 92 FL1.1B (2-split) mRNA stabilization A, no poly(A), no cap SEQ ID NO: 93 FL1.1B (2-split) mRNA stabilization A, cap, no poly(A) SEQ ID NO: 94 FL1.1B (2-split) mRNA stabilization A, poly(A), and cap SEQ ID NO: 95 gp220-D123 NP SEQ ID NO: 96 gp220-D123 TM SEQ ID NO: 97 gH-P2A-gL-P2A-gp42 SEQ ID NO: 98 gH-P2A-gL SEQ ID NO: 99 gp220 FL2 SEQ ID NO: 100 gp350-D123 NP2 SEQ ID NO: 101 gp220 FL3 SEQ ID NO: 102 gH / gL / gp42 FL2 SEQ ID NO: 103 hli-FL1 protein SEQ ID NO: 104 hli-FL1.1A protein SEQ ID NO: 105 hli-FL1.1B protein SEQ ID NO: 106 hli-FL1.2A protein SEQ ID NO: 107 hli-FL1.2B protein SEQ ID NO: 108 hli-FL1.2C protein SEQ ID NO: 109 hli-FL1.1A SEQ ID NO: 110 hli-FL1.1B SEQ ID NO: 111 hli-FL1.2A SEQ ID NO: 112 hli-FL1.2B SEQ ID NO: 113 hli-FL1.2C SEQ ID NO: 114 gH-P2A-gL-P2A-gp42 mRNA stabilization A SEQ ID NO: 115 HA-tagged hli FL1 mRNA stabilization A SEQ ID NO: 116 HA-tagged hli FL1 Plasmid stabilization A SEQ ID NO: 117 HA-tagged hli FL1 protein SEQ ID NO: 118 HA-tag protein SEQ ID NO: 119 FL1 mRNA stabilization B ORF SEQ ID NO: 120 FL1.1A mRNA stabilization B ORF SEQ ID NO: 121 FL1.1B mRNA Stabilization B ORF SEQ ID NO: 122 FL1.2A mRNA Stabilization B ORF Attorney Docket No: 70488WO01 SEQ ID NO: 123 FL1.2B mRNA Stabilization B ORF SEQ ID NO: 124 FL1.2C mRNA Stabilization B ORF SEQ ID NO: 125 Full length gH mRNA stabilization B ORF SEQ ID NO: 126 Full length gL mRNA stabilization B ORF SEQ ID NO: 127 Full length gp42 mRNA stabilization B ORF SEQ ID NO: 128 Full length gp220 mRNA stabilization A ORF SEQ ID NO: 129 FL1 mRNA stabilization B, no cap, no poly A SEQ ID NO: 130 FL1 mRNA stabilization B, cap, no poly A SEQ ID NO: 131 FL1 mRNA stabilization B, cap, poly A SEQ ID NO: 132 FL1.1A mRNA stabilization B, no cap, no poly A SEQ ID NO: 133 FL1.1A mRNA stabilization B, cap, no poly A SEQ ID NO: 134 FL1.1A mRNA stabilization B, cap, poly A SEQ ID NO: 135 FL1.1B mRNA stabilization B, no cap, no poly A SEQ ID NO: 136 FL1.1B mRNA stabilization B, cap, no poly A SEQ ID NO: 137 FL1.1B mRNA stabilization B, cap, poly A SEQ ID NO: 138 FL1.2A mRNA stabilization B, no cap, no poly A SEQ ID NO: 139 FL1.2A mRNA stabilization B, cap, no poly A SEQ ID NO: 140 FL1.2A mRNA stabilization B, cap, poly A SEQ ID NO: 141 FL1.2B mRNA stabilization B, no cap, no poly A SEQ ID NO: 142 FL1.2B mRNA stabilization B, cap, no poly A SEQ ID NO: 143 FL1.2B mRNA stabilization B, cap, poly A SEQ ID NO: 144 FL1.2C mRNA stabilization B, no cap, no poly A SEQ ID NO: 145 FL1.2C mRNA stabilization B, cap, no poly A SEQ ID NO: 146 FL1.2C mRNA stabilization B, cap, poly A SEQ ID NO: 147 Full length gH mRNA stabilization B, no cap, no poly A SEQ ID NO: 148 Full length gH mRNA stabilization B, cap, no poly A SEQ ID NO: 149 Full length gH mRNA stabilization B, cap, poly A SEQ ID NO: 150 Full length gL mRNA stabilization B, no cap, no poly A SEQ ID NO: 151 Full length gL mRNA stabilization B, cap, no poly A SEQ ID NO: 152 Full length gL mRNA stabilization B, cap, poly A SEQ ID NO: 153 Full length gp42 mRNA stabilization B, no cap, no poly A SEQ ID NO: 154 Full length gp42 mRNA stabilization B, cap, no poly A SEQ ID NO: 155 Full length gp42 mRNA stabilization B, cap, poly A SEQ ID NO: 156 Full length gp220 mRNA stabilization A, no cap, no poly A SEQ ID NO: 157 Full length gp220 mRNA stabilization A, cap, no poly A SEQ ID NO: 158 Full length gp220 mRNA stabilization A, cap, poly A SEQ ID NO: 159 Full length LMP2b mRNA, cap, poly A SEQ ID NO: 160 Full length LMP2a, 5’ & 3’ UTR4 mRNA, cap, poly A Attorney Docket No: 70488WO01 SEQ ID NO: 161 Full length LMP2b, 5’ & 3’ UTR4 mRNA, cap, poly A SEQ ID NO: 162 Full length EBNA1, 5’ & 3’ UTR4 mRNA, cap, poly A SEQ ID NO: 163 Full length EBNA3a w / gsgs-NLS mRNA, cap, poly A SEQ ID NO: 164 Full length EBNA3a, 5’ & 3’ UTR4 mRNA, cap, poly A SEQ ID NO: 165 Full length ZEBRA, 5’ & 3’ UTR4 mRNA, cap, poly A SEQ ID NO: 166 Full length LMP1, 5’ & 3’ UTR4 mRNA, cap, poly A DETAILED DESCRIPTION OF THE INVENTION The preferred materials and methods are described herein. Any methods and materials similar or equivalent to those described below can be used in the practice of or testing of the invention, with the exception for tests for pKa of the ionizable cationic lipid, pKa of the lipid nanoparticle, percent of encapsulation of nucleic acids within lipid nanoparticles, and the percent identities of nucleic sequences (e.g. EBV antigen-encoding mRNA construct sequences and non-EBV antigen-encoding mRNA construct sequences). Please use the tests for pKa of the ionizable cationic lipid, pKa of the lipid nanoparticle, percent of encapsulation of nucleic acids within lipid nanoparticles, and the percent identities of nucleic sequences (e.g. EBV antigen-encoding mRNA construct sequences and non- EBV antigen-encoding mRNA construct sequences). DEFINITIONS Unless defined otherwise, all technical and scientific terms herein have the same meaning as commonly understood by one of ordinary skill in the art. The following terminology will be used. It is also to be understood that the terminology used herein is for the purpose of describing particular embodiments only and is not intended to be limiting. The articles “a” and “an” are used herein to refer to one or to more than one (i.e., to at least one) of the grammatical object of the article. By way of example, “an element” means one element and more than one element. “Or” supports, contemplates, and when recited in the claims, claims “one or a combination of” as in “one or a combination of A, B, or C.” To illustrate, “A, B, or C” means A alone, B alone, C alone, the combination of A and B, the combination of A and C, the combination of B and C, and the combination of A, B, and C, unless otherwise illustrated. That is, “or” supports and contemplates “and” as in “and / or” wherein “and / or” includes any combinations within the list of alternatives without being limited solely to the combination of all alternatives in a list (i.e. “A, B, or C” includes “A and B” and is not limited to “A, B, and C”). Furthermore, the recitation of a list of alternatives, which may be conjoined by “and” and from which at least one alternative is selected (e.g. Markush language), further contemplates and supports all combinations within the list of alternatives. For example, “X is selected from the group of: A, B, and C” contemplates and supports “X is selected from the group of: A, B, C, and combinations thereof,” “X is selected from at least one of the group of: A, B, and C,” and “X is selected from one or Attorney Docket No: 70488WO01 more of the group of: A, B, and C.” For further example, “X is selected from the group consisting of A, B, and C” contemplates and supports “X is selected from the group consisting of A, B, C, and combinations thereof,” “X is selected from at least one of the group consisting of A, B, and C,” or “X is selected from one of more of the group consisting of A, B, and C.” Each of the following contemplates and supports any of the others: “comprises,” “consists of,” “consists essentially of,” “is / are / being,” “is selected from,” “is at least selected from,” “is selected from the group of,” “is selected from the group consisting of,” “is at least selected from the group consisting of,” “is from at least one of the group consisting of,” and “is from one or more of the group consisting of.” Please note that each of the above-listed terms have their ordinary meaning (i.e. “comprising” is open language and “consisting of” is closed language). However to avoid reciting for example, “X comprises, consists of, or is…A, B, or C,” in each and every instance, , recitation of “X comprises an A, a B, or a C” in the specification, for example, contemplates and supports embodiments wherein “X consists of an A, a B, or a C,” “X consists of an A, a B, a C, or combinations thereof,” “X consists of one or more of an A, a B, or a C,” “X is one or more of an A, a B, or a C,” “X is an A, a B, a C, or combinations thereof,” “X is selected from an A, a B, or a C,” “X is selected from an A, a B, a C, or combinations thereof,” “X is selected from the group consisting of an A, a B, a C, and combinations thereof,” “X is selected from at least one of the group consisting of an A, a B, and a C,” or “X is selected from one or more of the group consisting of an A, a B, and a C.” When a specific component of an embodiment is listed—e.g. “X comprises A, B, or C”—then also supported and contemplated are any embodiments which specifically exclude any individual or combinations of components—e.g. “X comprises A, but not B or C” or “X comprises A but does not comprise B or C.” A list of alternatives after “comprises,” “consists of,” “consists essentially of,” “is / are / being,” “is selected from,” “is at least selected from,” “is selected from the group of,” “is selected from the group consisting of,” “is at least selected from the group consisting of,” “is from at least one of the group consisting of,” or “is from one or more of the group consisting of” is meant to convey discrete items within the category without necessarily implying that a chemical bond (e.g. covalent bond, hydrogen bond, etc.) exists between them. For example, “a zwitterionic lipid comprising 1,2-diheptadecanoyl- sn-glycero-3-phosphocholine (17:0 PC), 1,2-distearoyl-sn-glycero-3-phosphocholine (DSPC), 1,2- distearoyl-sn-glycero-3-phosphocholine (19:0 PC), or 1,2-diarachidoyl-sn-glycero-3-phosphocholine (20:0 PC)” is meant to convey that the category (i.e. genus) of zwitterionic lipids can include within that category discrete lipids (i.e. species) such as DSPC, 17:0 PC, 19:0 PC, and 20:0 PC without being limited to the interpretation, for example, that the zwitterionic lipid has covalently bound to it one or more of DSPC, 17:0 PC, 19:0 PC, and 20:0 PC. In this regard, “comprises” is inclusive of “includes” (i.e. a word leaving open the list of discrete item within the category) and should not necessarily imply the category is a generic chemical formula to which discrete moieties must necessarily be covalently bound. E.g. the noble gas comprising a helium atom, a neon atom, an argon atom, or a krypton atom. As noted above, “a” or “an” includes “more than one” discrete items Attorney Docket No: 70488WO01 within the category; therefore each of the terms after the “comprising” or other supported term can include a sub-genus, and each need not necessarily be a species (e.g. the noble gas comprising a helium atom (a helium-4, a helium-3, or a helium-6), a neon atom (a neon-20, a neon-22, or a neon- 23), an argon atom (an argon-40, an argon-38, or an argon-42), or a krypton atom (a krypton-85, a krypton-95, or a krypton-92)). “Antigens” refers to a molecule that provokes an adaptive immune response and that can be bound to a protein comprising complementary-determining regions such as an antibody or a T cell receptor (e.g., causing an immune system to produce antibodies against the antigens). Herein, use of the term “antigen” encompasses immunogenic / antigenic proteins and immunogenic / antigenic fragments (e.g., an immunogenic / antigenic fragment that induces (or is capable of inducing) an immune response to human EBV). By “EBV antigen” is meant an antigen that causes an adaptive immune response (i.e. an antigen- based immune response, c.f. an innate immune response) to the Epstein-Barr virus. The EBV antigen need not necessarily be an EBV protein or an EBV protein fragment, and instead can also include a synthetic or naturally occurring protein with enough homology to an EBV protein or an EBV protein fragment for the adaptive immune response to the Epstein-Barr virus. In certain embodiments, such recombinant proteins include, without limitation, FL1, FL1.1A, FL1.2A, FL1.2A, FL1.2B, and FL1.2C (FIG.1A). The terms “protein”, “polypeptide” and “peptide” are used interchangeably herein and refer to any peptide-linked chain of amino acids, regardless of length or post-translational modification (e.g. phosphorylation or addition of sugars, lipids, or combinations thereof). It should also be understood that the term “antigen” encompasses full length proteins, truncated proteins, modified proteins, and peptides. Since EBV antigens are contemplated herein, since EBV antigens encompasses EBV proteins and EBV protein fragments, and since EBV proteins and EBV protein fragments often have post- translational modifications, “EBV antigens,” “EBV proteins,” and “EBV protein fragments” include a glycoprotein, a lipo-protein, a lipo-glyco-protein, and other terms for the protein that is the result of the post-translational modification of the protein as translated from the messenger RNA that encodes it. In this regard, the heterologous polypeptide may be translated from the segment that encodes the heterologous polypeptide once the recombinant RNA is in a cell. The translated protein, as encoded by the segment that encodes the protein, may have moieties to which post-translational modification adds the sugars, lipids, lipids and sugars, and other post-translational modifications. Accordingly, “the segment that encodes an EBV antigen” means and refers to, and segments that encode species of EBV antigens conveys, a segment that encodes an EBV protein or EBV protein fragment, and post-translational products thereof, including glycoproteins thereof, lipoproteins thereof, lipo- glycoproteins thereof, and post-translational products thereof. Gp220, gL, gH, and / or gp42 are for example glycoproteins as encoded in the at least two Epstein-Barr virus (EBV) antigen-encoding nucleic acid constructs (e.g. at least two EBV antigen-encoding mRNA constructs). The term “an Attorney Docket No: 70488WO01 EBV antigen” includes a pre-form and / or a pro-form of a biologically active molecule of the antigen and combinations thereof with the aforementioned post-translationally modified antigen, including glycoprotein of the antigen, a heterologous lipo-protein of the antigen, a heterologous lipo-glyco- protein of the antigen (e.g. pre-pro-insulin and respiratory syncytial virus pre-fusion glycoprotein). It is understood that such post-translational modifications may contribute to the antigenicity of the EBV antigen. Regarding any terms before “comprises,” “consists of,” “consists essentially of,” “is / are / being,” “is selected from,” “is at least selected from,” “is selected from the group of,” “is selected from the group consisting of,” “is at least selected from the group consisting of,” “is from at least one of the group consisting of,” “is from one or more of the group consisting of,” etc., specifically contemplated herein are categories of EBV antigens which, when encoded in at least two “EBV antigen-encoding” nucleic acid constructs (e.g. EBV antigen-encoding mRNA constructs), are distributed in their encoding across the two or more nucleic acid constructs (e.g. two or more EBV antigen-encoding mRNA constructs), such that all immunogens need not be encoded in each of the two or more nucleic acid constructs (e.g. two or more EBV antigen-encoding mRNA constructs) and / or that there is not necessarily any duplication of the encoding of a single antigen across the two or more nucleic acid constructs (e.g. two or more EBV antigen-encoding mRNA constructs) at all. Accordingly, for example, “at least two (alternatives including “at least three, at least four,…,at least seven”) EBV antigen-encoding nucleic acid constructs (e.g. EBV antigen-encoding mRNA constructs) comprising” (or any of the above-noted combination of terms) means that the “at least two EBV antigen-encoding nucleic acid constructs (e.g. EBV antigen-encoding mRNA constructs) collectively, or together, comprise” and does not mean “at least two EBV antigen-encoding nucleic acid constructs, each comprising” unless “each” or some other equivalent modifier is otherwise stated. Also for example, “the EBV antigens comprising…,” “the EBV B cell module antigen comprising,” and “the EBV T cell module antigen comprising” are meant to convey that the category of antigen includes multiple species of antigens therein and that each antigen need not be encoded in each segment encoding an EBV antigen on each of the EBV antigen-encoding nucleic acid constructs (e.g. EBV antigen- encoding mRNA construct). See e.g., “the EBV antigens comprising an EBV B cell module antigen and an EBV T cell module antigen; the EBV B cell module antigen comprising an EBV glycoprotein- 220 (gp220) antigen; and the EBV T cell module antigen comprising at least two, at least three, or at least four of: (a) an EBV latent membrane protein-1 (LMP1) antigen; (b) an EBV latent membrane protein-2 (LMP2) antigen; (c) an EBV nuclear antigen-1 (EBNA1) antigen; (d) an EBV nuclear antigen-3A (EBNA3A) antigen; and the a BamHI Z EBV replication activator (ZEBRA) antigen.” “Each” or some other equivalent modifier will be stated when each of the at least two EBV antigen- encoding mRNA constructs must contain a particular feature in order to, for example, provide for the distribution of the immunogens across two or more nucleic acid constructs (e.g. two or more EBV antigen-encoding mRNA constructs). See e.g. “each of the at least two EBV antigen-encoding mRNA constructs comprising a segment that encodes an Epstein-Barr virus (EBV) antigen.” In this example Attorney Docket No: 70488WO01 accordingly, if there are at least two EBV antigen-encoding nucleic acid constructs (e.g. EBV antigen-encoding mRNA constructs) and if each of the at least two EBV antigen-encoding mRNA constructs comprises, consists of, or is a segment that encodes an Epstein-Barr virus (EBV) antigen, then there must be at least two EBV antigens encoded across, or collectively by, the at least two EBV antigen-encoding nucleic acid constructs (e.g. at least two EBV antigen-encoding mRNA constructs), and then accordingly the EBV antigen comprises, consists of, or is at least two EBV antigens, and hence in the example above, at least one T cell module antigen and at least one B cell module antigen, which must comprise at least gp220. In this regard, recombinant antigens are contemplated, which contemplates that the recombinant antigen comprises, consists of, or is an EBV protein or an EBV protein fragment fused with at least one other EBV protein or EBV protein fragment either directly or indirectly (i.e. through a linker to provide for the fusing). “Mosaic” (i.e. a fused protein comprising an EBV protein or an EBV protein fragment fused with at least one other EBV protein or EBV protein fragment either directly or indirectly) in this context has the same meaning as “recombinant.” “EBV T cell module antigens” includes (by way of illustration) EBNA1, EBNA2, EBNA3A, EBNA3B, EBNA3C, EBNA leader protein (EBNA-LP), LMP1, LMP2, ZEBRA, BRLF1, and BNLF2, BCRF1 full length proteins, fragments thereof, and recombinant proteins comprising the full-length proteins and protein fragments at least because when presented, they can steer the Th1- and Th2- mediated immune responses. See definitions below related to “antigen.” “EBV B cell module antigens” includes (by way of illustration) gH, gL, gB, gp42, gp220, and gp350 proteins, fragments thereof, and recombinant proteins comprising the full-length proteins and protein fragments at least because these full-length proteins help the virus infect B cells. See definitions below related to “antigen.” In this regard, by “FL1”, “FL1 protein”, or “EBV full-length T cell module” is meant a subcategory of T cell module antigens (i.e. a protein, c.f. nucleic acid encoding the protein), and a subcategory of recombinant T cell module antigens, consisting of SEQ ID NO: 27. Accordingly, in some embodiments, the T cell module antigen comprises a sequence that that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 27. Accordingly in some embodiments, the T cell module protein comprises, consists of, or is FL1 (and thereby comprises, consists of, or is SEQ ID NO: 27). In some embodiments, the T cell module antigen comprises FL1 and further comprises an hli sequence. In some embodiments, the hli sequence is located at the N- terminus of FL1. In other embodiments, the hli sequence is located at the C-terminus of FL1. In additional embodiments, the T cell module antigen comprises FL1 and further comprises an N- terminal methionine residue. In other embodiments, the T cell module antigen comprises FL1 and further comprises an N-terminal signal sequence. EBV antigen-encoding mRNA constructs comprising segments that encode FL1 and plasmids thereto, including those with 5’ and 3’ untranslated regions, capping consensus regions, poly(adenosine monophosphate), and backbones of plasmids, are also described and are also marked and are described with “mRNA” or “plasmid” Attorney Docket No: 70488WO01 respectively to distinguish from the protein. By “full-length T cell module mosaic mRNA construct” or “full-length T cell module mosaic mRNA” or “EBV full-length T cell module mosaic mRNA” is meant a messenger RNA (mRNA) that encodes FL1. By “FL1.1A” is meant a subcategory of T cell module antigens, and a subcategory of recombinant T cell module antigens, consisting of SEQ ID NO: 29. Accordingly, in some embodiments, the T cell module antigen comprises a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 29. Accordingly in some embodiments, the T cell module protein comprises, consists of, or is FL1.1A (and thereby comprises, consists of, or is SEQ ID NO: 29). Accordingly in some embodiments, the T cell module protein comprises, consists of, or is FL1.1A. In some embodiments, the T cell module antigen comprises, consists of, or is FL1.1A. In some embodiments, the T cell module antigen comprises FL1.1A and further comprises an hli sequence. In some embodiments, the hli sequence is located at the N- terminus of FL1.1A. In other embodiments, the hli sequence is located at the C-terminus of FL1.1A. In additional embodiments, the T cell module antigen comprises FL1.1A and further comprises an N- terminal methionine residue. In other embodiments, the T cell module antigen comprises FL1.1A and further comprises an N-terminal signal sequence. EBV antigen-encoding mRNA constructs comprising segments that encode FL1.1A and plasmids thereto, including those with 5’ and 3’ untranslated regions, capping consensus regions, poly(adenosine monophosphate), and backbones of plasmids, are also described and are also marked and are described with “mRNA” or “plasmid” respectively to distinguish from the protein. By “FL1.1B” is meant a subcategory of T cell module antigens, and a subcategory of recombinant T cell module antigens, consisting of SEQ ID NO: 31. Accordingly, in some embodiments, the T cell module antigen comprises a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 31. Accordingly in some embodiments, the T cell module protein comprises, consists of, or is FL1.1B (and thereby comprises, consists of, or is SEQ ID NO: 31). In some embodiments, the T cell module antigen comprises FL1.1B and further comprises an hli sequence. In some embodiments, the hli sequence is located at the N-terminus of FL1.1B. In other embodiments, the hli sequence is located at the C-terminus of FL1.1B. In additional embodiments, the T cell module antigen comprises FL1.1B and further comprises an N-terminal methionine residue. In other embodiments, the T cell module antigen comprises FL1.1B and further comprises an N-terminal signal sequence. EBV antigen-encoding mRNA constructs comprising segments that encode FL1.1B and plasmids thereto, including those with 5’ and 3’ untranslated regions, capping consensus regions, poly(adenosine monophosphate), and backbones of plasmids, are also described and are also marked and are described with “mRNA” or “plasmid” respectively to distinguish from the protein. FL1.1A and FL1.1B are collectively referred to herein as “2-part,” “2-split,” “2-split design,” “2-split mosaic,” “2-split mosaic design,” “2-split T cell module,” or “2-split T cell module mosaic.” Attorney Docket No: 70488WO01 By “FL1.2A” is meant a subcategory of T cell module antigens consisting of SEQ ID NO: 33. Accordingly, in some embodiments, the T cell module antigen, and a subcategory of recombinant T cell module antigens, comprises a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 33. Accordingly in some embodiments, the T cell module protein comprises, consists of, or is FL1.2A (and thereby comprises, consists of, or is SEQ ID NO: 33). In some embodiments, the T cell module antigen comprises FL1.2A and further comprises an hli sequence. In some embodiments, the hli sequence is located at the N-terminus of FL1.2A. In other embodiments, the hli sequence is located at the C-terminus of FL1.2A. In additional embodiments, the T cell module antigen comprises FL1.2A and further comprises an N-terminal methionine residue. In other embodiments, the T cell module antigen comprises FL1.2A and further comprises an N-terminal signal sequence. EBV antigen-encoding mRNA constructs comprising segments that encode FL1.2A and plasmids thereto, including those with 5’ and 3’ untranslated regions, capping consensus regions, poly(adenosine monophosphate), and backbones of plasmids, are also described and are also marked and are described with “mRNA” or “plasmid” respectively to distinguish from the protein. By “FL1.2B” is meant a subcategory of T cell module antigens, and a subcategory of recombinant T cell module antigens, consisting of SEQ ID NO: 35. Accordingly, in some embodiments, the T cell module antigen comprises a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 35. Accordingly in some embodiments, the T cell module protein comprises, consists of, or is FL1.2B (and thereby comprises, consists of, or is SEQ ID NO: 35). In some embodiments, the T cell module antigen comprises FL1.2B and further comprises an hli sequence. In some embodiments, the hli sequence is located at the N-terminus of FL1.2B. In other embodiments, the hli sequence is located at the C-terminus of FL1.2B. In additional embodiments, the T cell module antigen comprises FL1.2B and further comprises an N-terminal methionine residue. In other embodiments, the T cell module antigen comprises FL1.2B and further comprises an N-terminal signal sequence. EBV antigen-encoding mRNA constructs comprising segments that encode FL1.2B and plasmids thereto, including those with 5’ and 3’ untranslated regions, capping consensus regions, poly(adenosine monophosphate), and backbones of plasmids, are also described and are also marked and are described with “mRNA” or “plasmid” respectively to distinguish from the protein. By “FL1.2C” is meant a subcategory of T cell module antigens, and a subcategory of recombinant T cell module antigens, consisting of SEQ ID NO: 37. Accordingly, in some embodiments, the T cell module antigen comprises a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 37. Accordingly in some embodiments, the T cell module protein comprises, consists of, or is FL1.2C (and thereby comprises, consists of, or is SEQ ID NO: 37). In some embodiments, the T cell module antigen comprises FL1.2C and further comprises an hli sequence. In some embodiments, the hli sequence is located at the N-terminus of FL1.2C. In other embodiments, the hli sequence is located at the C-terminus of Attorney Docket No: 70488WO01 FL1.2C. In additional embodiments, the T cell module antigen comprises FL1.2C and further comprises an N-terminal methionine residue. In other embodiments, the T cell module antigen comprises FL1.2C and further comprises an N-terminal signal sequence. In some embodiments, FL1.2C consists of SEQ ID NO: 37. EBV antigen-encoding mRNA constructs comprising segments that encode FL1.2C and plasmids thereto, including those with 5’ and 3’ untranslated regions, capping consensus regions, poly(adenosine monophosphate), and backbones of plasmids, are also described and are also marked and are described with “mRNA” or “plasmid” respectively to distinguish from the protein. FL1.2A, FL1.2B, and FL1.2C are collectively referred to herein as “3-part,” “3-split,” “3-split design,” “3-split mosaic,” “3-split mosaic design,” “3-split T cell module,” or “3-split T cell module mosaic.” “EBV latent membrane protein-2” (LMP2) includes LMP2A and LMP2B (see Genbank No. P13285), which lacks the first (N-terminal) 119 amino acids of LMP2A. "About" as used herein when referring to a measurable value such as an amount, a temporal duration, a quantum of measurement, and the like, is meant to encompass variations of + / - 20%, + / - 10%, + / - 5%, + / -1%, or + / - 0.1% from the specified value that distinguishes the value from the adjacent ordered values in the list. The term "antibody," as used herein, refers to an immunoglobulin molecule, which comprises three heavy-chain complementary-determining regions and three light-chain complementary- determining regions (collectively an antigen-determining region), and therefrom specifically binds with an antigen. An antibody can comprise the quintessential “Y” shaped immunoglobulin which comprises two arms and a stem and which comprises two heavy-chains and two light-chains. Each arm comprises a variable region which comprises said light-chain and heavy-chain complementary- determining regions, and each arm comprising a light-chain and a portion (CH1 region) of the heavy- chain. Each stem comprises two portions of a heavy-chain, each portion comprising a CH2 region and a CH3 region. That is, antibodies can be intact immunoglobulins derived from natural sources or from recombinant sources and can be immunoreactive portions of intact immunoglobulins. Antibodies can also be fragments of said intact antibody, wherein the fragment comprises said three heavy-chain complementary-determining regions and said three light-chain complementary- determining regions (i.e. said antigen-determining regions), and therefrom specifically binds with an antigen. The antibodies may exist in a variety of forms including, for example, Fv, Fab, F(ab)2, linear antibodies, and single chain antibodies (scFv). Antibodies can include polyclonal antibodies, monoclonal antibodies, humanized antibodies, human antibodies, bispecific antibodies, and multi- specific antibodies (Harlow et al., 1999, In: Using Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory Press, NY; Harlow et al., 1989, In: Antibodies: A Laboratory Manual, Cold Spring Harbor, N.Y.; Houston et al., 1988, Proc. Natl. Acad. Sci. USA 85:5879-5883; Bird et al., 1988, Science 242:423-426). Attorney Docket No: 70488WO01 “Sequence,” “segment,” “nucleic acid,” or “region” as used within the context of a nucleic acid includes information about the sense (i.e. positive) and anti-sense (i.e. negative, e.g. reverse complementary) sequences of the same nucleic acid. A “segment,” “sequence,” “nucleic acid,” or “region” that “encodes” a coding sequence, wherein the coding sequence is transcribed and / or translated, includes information about the sense and antisense (e.g. reverse complementary) sequences of the same nucleic acid. In some embodiments, the coding sequences encode an antigen (a.k.a. an immunogen). In this regard, since “an” includes plurals, “the segment that encodes an antigen” includes “the segment that encodes two or more antigens.” For example, in some embodiments, fragments of EBV proteins are identified and are recombined with fragments of other EBV proteins to make a recombinant EBV antigen. This recombinant EBV antigen comprises multiple antigens from the multiple fragments, and the “an” “the segment that encodes an antigen” contemplates the multiple antigens provided by the multiple fragments in the recombinant antigen. Similarly, whole endogenous EBV proteins (e.g. gp220) may comprise multiple epitopes (i.e. TCR- MHC binding epitopes), which are antigens. Accordingly, the segment that encodes the endogenous EBV protein may comprise multiple antigens. This contemplation and support of both sense and antisense strands for the segment, sequence, nucleic acid, or region is due to the property of a nucleic acid to undergo semi-conservative replication whereby genetic information is retained. In semi-conservative replication, the two strands of double-stranded nucleic acid are separated (i.e. melt or are separated by a helicase), and each of the two strands are used as a template from which a newly synthesized, reverse complementary strand is formed. That is, in semi-conservative replication, the genetic information, whether as sense or antisense is preserved, and a protein, immunogen, miRNA, or promoter, for example, may be produced from the initial strand or strands synthesized therefrom regardless of whether the initial strand is sense or antisense. In some embodiments, the mRNA construct can be a self-replicating (a.k.a. self-amplifying) mRNA or a pluralities of mRNAs that are collectively called trans-amplifying mRNA. Within the context of self-amplifying mRNA and trans-amplifying mRNA, semi-conservative replication provides for the propagation of, for example, the information encoding the antigen regardless of whether the segment encoding the antigen was sense or antisense. In this regard, it is understood that the self- replicating mRNA or the trans-amplifying mRNA can comprise one or more segments or sequences that encode one or more proteins necessary for replicating the self-replicating mRNA or trans- amplifying mRNA in an intracellular environment, and that these segments or sequences that encode the one or more proteins necessary for replicating the a self-replicating mRNA or trans-amplifying mRNA in an intracellular environment are encoded in a sense or positive-strand orientation. It is at least the translation of the one or more proteins necessary for replicating the self-replicating mRNA or trans-amplifying mRNA from the self-replicating mRNA or trans-amplifying mRNA in its original form (c.f. daughter mRNA molecules or replicated mRNAs molecules), and as it entered the cell that Attorney Docket No: 70488WO01 does the translating, that at least qualify self-replicating mRNA or trans-amplifying mRNA as being messenger RNA. The above-noted support and contemplation of sense and antisense strands applies not only to a self-replicating mRNA or trans-amplifying mRNA, but also to the making and use of a conventional RNA, which is often transcribed from DNA and plasmids, which may encode sense or antisense information, depending upon the step of in the manufacture of the mRNA. To illustrate how “sequence,” “segment,” “nucleic acid,” or “region” as used within the context of a nucleic acid includes information about the sense (i.e. positive) and anti-sense, if a specific sequence, called “A”, is listed as having the sequence of 5’-ATGG-3’ in the sense strand (i.e. positive strand) then it is contemplated and supported that A also has the sequence of 3’-TACC-5’ in the antisense strand (i.e. negative strand) or complementary strand (i.e. A comprises 5’-ATGG-3’ or 3’-TACC-5’), if present. As statements above provide, “sequence,” “region,” or “segment” as used herein, unless otherwise specified, also contemplates and supports sequences incorporating different forms of nucleic acids, i.e. RNA and DNA, of the same information, or sequences incorporating differing nucleotides found in the different forms of the nucleic acids (i.e. uridines in RNA and thymidines in DNA), as well as sense and anti-sense (e.g. reverse complementary) information therein. For example, RNA may be produced from plasmids of DNA, and thereby the sequence of the plasmid contemplates and supports the sequence of the RNA and vice versa. Since the substitution standard nucleotides with modified nucleotides are contemplated herein (i.e. the substitution of uridines with N1-methylpseudouridines (N1Ψ) is contemplated herein), a sequence, region, or segment herein also contemplates and supports sequences incorporating analogs of the standard nucleotides (i.e. uridines) herein. To illustrate, if A in RNA (sense) is 5’-AUGG-3’, A also comprises 5’-ATGG-3’, being the sense DNA, and 3’-TACC-5’ being the anti-sense DNA, as well as 3’-UACC-5’, being the antisense RNA. To also illustrate, 5’-AUGG-3’ also supports and contemplates the sequence of 5’- A(N1Ψ)GG-3’, as well as 3’-(N1Ψ)ACC-5.’ To distinguish between sense and anti-sense (e.g. complementary) sequences, a prime symbol (‘) may be used, i.e. for ease of tracking original genomic material, transcripts, first strand synthesis, second strand synthesis, sense, and antisense strands. To further illustrate, if a first single-stranded region comprises 5’- AATGATACGGCGACCACCGA-3’, then that first single-stranded region also supports and comprises 5’-TCGGTGGTCGCCGTATCATT-3’. In some embodiments, a “first” and a “second” are provided, such as “a first segment” and “a second segment” or “a first fragment” and “a second fragment”. It is to be understood that the second RNA segment is not necessarily downstream (3’) of the first RNA segment or that it is not necessarily upstream (5’) of the first RNA segment either. It is to be understood that the second fragment is not necessarily downstream (i.e. toward the N-terminal of the protein) of the first fragment or that it is not necessarily upstream (i.e. toward the C-terminal of the protein) of the first fragment either. “First” or “second” with regard to an “RNA segment” is not meant to connote the order along a stand-alone molecule, but rather “first” and “second” are used for nominative convenience. In some Attorney Docket No: 70488WO01 embodiments, “first” and “second” lipids are provided. In this regard, a “first” or “second” or any numbered thing is to be understood to use such numbering as to differentiate between said things within an embodiment. “Identity,” “homology,” and within this context, “percent identity” or “percent homology” take the following definitions depending upon whether it is an amino acid sequence or a nucleic acid sequence. “Identity” or “homology” (i.e. percent identity) with respect to an amino acid sequence is defined herein as the percentage of amino acid residues in the candidate sequence that are identical with the reference amino acid sequence after aligning the sequences and introducing gaps, if necessary, to achieve the maximum percent sequence identity, and not considering any conservative substitutions as part of the sequence identity. The percent identity is defined as the nucleotide or protein basic local alignment search tool (BLAST) from the United States Government’s National Library of Medicine, National Center for Biotechnology Information (blast.ncbi.nlm.nih.gov / Blast.cgi) as available on the earliest effective priority date of these corresponding applications using align two or more sequences and optimized for default settings. For nucleotide sequences, the default settings are to include highly similar sequences, 100 max target sequences, automatically adjusting parameters for short input sequences, expected threshold of 0.05, word size of 28, max matches in a query range of 0, match / mismatch scores of 1 / -2, linear gap costs, filtering low complexity regions, and mas for lookup tables. For protein sequences, the default settings are to include non-redundant protein sequences, “blastp (protein-protein BLAST),” max target sequences of 100, automatically adjusting parameters for short input sequences, expected threshold of 0.05, word size of 3, max matches in a query range of 0, matrix of BLOSUM62, gap costs of Existence: 11, Extension: 1, compositional adjustments of conditional composition score matrix adjustment, no filters for low complexity regions, and no masting for lookup table or lower case letters. “Identity” or “homology” (i.e. percent identity) with respect to a nucleic acid sequence is defined herein as the percentage of nucleotides in the candidate sequence that are identical with the reference nucleic acid sequence after aligning the sequences and introducing gaps, if necessary, to achieve the maximum percent sequence identity. The exchange of uridine and thymidine shall be equivalent (i.e. not taken into account) for calculating percent identity. The substitution of uridine or thymidine with a uridine- or thymidine-substitutable modified nucleotide (i.e. U substituted with N1Ψ) shall be equivalent (i.e. not taken into account) for calculating percent identity. The substitution of adenosine with an adenosine-substitutable modified nucleotide shall be equivalent (i.e. not taken into account) for calculating percent identity. The substitution of guanosine with a guanosine-substitutable modified nucleotide shall be equivalent (i.e. not taken into account) for calculating percent identity. The substitution of cytosine with a cytosine-substitutable modified nucleotide shall be equivalent (i.e. not taken into account) for calculating percent identity. Where the present disclosure refers to a sequence by reference to a UniProt or Genbank accession code, the sequence referred to is the current version at the filing date of the earliest effective filing date. Attorney Docket No: 70488WO01 “Nucleic acid,” “polynucleotide,” and “oligonucleotide” as used herein all have the same meaning and they are inherently composed of a sequence of nucleotides, each nucleotide comprising one, two, or three phosphates and a nucleoside, a nucleoside comprising a pentose sugar (e.g. deoxyribose and ribose) and a nucleobase (e.g. a purine comprising adenine or guanine and a pyrimidine comprising cytosine, uracil, N1-methyluracil, and thymine). In some embodiments, the nucleoside (i.e. sugar and nucleobase) can be standard nucleosides (i.e. adenosine, deoxyadenosine, guanosine, deoxyguanosine, thymidine (a.k.a. deoxythymidine), uridine, deoxyuridine, cytidine, or deoxycytidine, or methylates thereof (i.e.5’-methyluridine) or they may be modified nucleosides (i.e. pseudouridine (a.k.a.5-(β-D-Ribofuranosyl)pyrimidine-2,4(1H,3H)-dione or 5-[(2S,3R,4S,5R)-3,4-Dihydroxy-5-(hydroxymethyl)oxolan-2-yl]pyrimidine-2,4(1H,3H)-dione, CAS No. 1445-07-4, PubChem CID 15047), N1-methyluridine, N1-methylpseudouridine (a.k.a.5- [(2S,3R,4S,5R)-3,4-Dihydroxy-5-(hydroxymethyl)oxolan-2-yl]-1-methylpyrimidine-2,4-dione, CAS No. 13860-38-3, PubChem CID 99543), or deoxyribose-containing or ribose-containing forms thereof). A “nucleic acid,” “polynucleotide,” and “oligonucleotide” can be a stand-alone molecule (i.e. an RNA molecule) or they may be “region,” “sequence,” or “segment” therein, and in this regard, the use of “region,” “sequence,” or “segment” is used to distinguish between such and a stand-alone molecule. In this regard, “construct” is used herein, such as in “a messenger ribonucleic acid construct,” to distinguish between two or more ribonucleic acids having different sequences. (C.f. two or more ribonucleic acid molecules, which have the same sequences, would be having two molecules of the same ribonucleic acid construct and same sequences. Such would be having twice the amount or concentration of the same molecule.) “At least two messenger ribonucleic acid constructs” are not intended to convey that they have the same sequences and therefore have twice the amount or concentration of the same molecule. “Not adjacent” (or equivalent) means that the at least two fragments do not form a contiguous amino acid sequence in the EBV antigen. “The lipids encapsulating the at least two EBV antigen-encoding mRNA constructs, thereby forming lipid nanoparticles (LNPs)” means—when not specifying that the lipids encapsulate a numerical quantity of the at least two EBV-encoding mRNA constructs—that the lipids encapsulate at least some of the molecules of each of the at least two EBV antigen-encoding mRNA constructs, to thereby form lipid nanoparticles, such that the entire length of the encapsulated-molecule of each of the at least two EBV antigen-encoding mRNA constructs is encapsulated by the lipids (i.e. is not exterior to the lipid nanoparticle), and such that the lipids do not necessarily encapsulate all of the at least two EBV antigen-encoding mRNA constructs in the pharmaceutical composition (i.e. some of the of the molecules of the at least two EBV antigen-encoding mRNA constructs may be exterior to the lipids and the lipid nanoparticle, i.e. each and every molecule of the at least two EBV antigen- encoding mRNA constructs are not necessarily encapsulated by the lipids), unless such quantity is specified wherein all of the molecules of the at least two EBV antigen-encoding mRNA constructs are encapsulated (e.g. the lipids encapsulating 100 mole% of the at least two EBV antigen-encoding Attorney Docket No: 70488WO01 mRNA constructs). With regard to “thereby forming lipid nanoparticles,” the lipid nanoparticles arise from the encapsulation of nucleic acids, such as mRNA constructs. Accordingly, in “the lipids encapsulating the at least two EBV antigen-encoding mRNA constructs, thereby forming lipid nanoparticles (LNPs)” means—when not specifying that the lipids encapsulate a numerical quantity of the at least two EBV-encoding mRNA constructs—it is possible that some of the at least two EBV antigen-encoding mRNA constructs (including when the pharmaceutical composition comprises at least three, at least four, at least five, at least six, at least seven of the EBV antigen-encoding mRNA constructs) are exterior to the lipid nanoparticles (c.f. the lipids encapsulating 100 mole% of the at least two EBV antigen-encoding mRNA constructs). In “polyethylene glycol-2000,” “PEG-2000,” “polyethylene glycol-X,” “PEG-X,” “polyethylene of X Da,” or “PEG of X Da” where “X” is a molecular weight, the “2000” or “X” represents the nearest theoretical molecular weight, which is rounding off to the nearest integer of the number-average of monomers in the measured number-average molecular weight in Daltons of the PEG. For example, the monomer in a PEG-conjugated lipid is ethylene oxide (—CH2—CH2—O—), which has a molecular weight of 44.04 Da. Assume that the sample has a number-averaged molecular weight of 1990.608 Da, which has a number-average of 45.2 ethylene oxides (1990.608 Da / (44.04 Da per ethylene oxide)= 45.2 number-average ethylene oxides).45 ethylene oxides would be the nearest integer to a number average of 45.2 ethylene oxides in the number-average molecular weight of 1990.608 Da.45 monomers would also result in a PEG with a theoretical molecular weight of 1981.8 Da (45 ethylene oxides x 44.04 Da per ethylene oxide =1981.8 Da). Thus, the theoretical molecular weight is 1981.8 Da of a PEG lipid having a number-average of 45.2 ethylene oxides in a number- average molecular weight of 1990.608 Da. The molecule having the theoretical molecular weight of the PEG of 1981.8 would be the “PEG-2000” as it is the closest theoretical weight to 2000 Da from a sample having a number-average molecular weight of 1990.608 Da. A “unit dose” is contemplated and understood to be that dose of the pharmaceutical composition provided in each administration, and several unit doses (i.e. the unit doses from several administrations may be combined) to make a total dose administered to the subject. EBV ANTIGEN-ENCODING MESSENGER RIBONUCLEIC ACID CONSTRUCTS AND THEIR DELIVERY VEHICLES In one aspect, a pharmaceutical composition is provided, the pharmaceutical composition comprising delivery vehicle and at least two EBV antigen-encoding messenger ribonucleic acid (mRNA) constructs. In some embodiments, the delivery vehicle comprises, consists of, or is a lipid delivery vehicle. In some embodiments, the lipid delivery vehicle comprises, consists of, or is a cationic nanoemulsion (CNE) or a liposome. A liposome is comprised of lipids and which together with the at least two EBV antigen-encoding mRNA constructs form lipid nanoparticles (LNPs) when the lipids encapsulate (see definition above about encapsulating being at least some mass percentage of, and not each and every molecule of) the at least two EBV antigen-encoding mRNA constructs. Attorney Docket No: 70488WO01 In one aspect, a pharmaceutical composition is provided, the pharmaceutical composition comprising at least two EBV antigen-encoding messenger ribonucleic acid (mRNA) constructs and a non-viral delivery vehicle. In some embodiments, the non-viral delivery vehicle does not comprise: (1) a viral capsid protein, (2) a virion, or (3) a viral like particle. In some embodiments, the non-viral delivery vehicle comprises, consists of, or is a lipid delivery vehicle. In some embodiments, the non- viral delivery vehicle comprises, consists of, or is a non-lipid based delivery vehicles, such as polymeric microparticles. In one aspect, a pharmaceutical composition is provided, the pharmaceutical composition comprising at least two EBV antigen-encoding messenger ribonucleic acid (mRNA) constructs and a lipid delivery vehicle. In some embodiments the lipid delivery vehicle is a cationic nanoemulsion or a liposome. The liposome being lipids and which together with the at least two EBV antigen-encoding mRNA constructs form lipid nanoparticles (LNPs) when the lipids encapsulate (see definition above about encapsulating being at least some mass percentage of, and not each and every molecule of) the at least two EBV antigen-encoding mRNA constructs. In this aspect, the delivery vehicle that does not comprise: (1) a viral capsid protein, (2) a virion, or (3) a viral like particle includes (i.e. excludes from the aspect of the invention) vaccinia viral-like particles, virions, or capsids obtained therefrom; adenovirus viral-like particles, virions, or capsids obtained therefrom; adeno-associated virus viral-like particles, virions, or capsids obtained therefrom; alphavirus viral-like particles, virions, or capsids obtained therefrom; lentivirus or retrovirus viral-like particles, virions, or capsids obtained therefrom; or RNA virus viral-like particles, virions, or capsids obtained therefrom. Accordingly, in some embodiments, the lipids encapsulate at least 50 mass %, at least 75 mass% of, at least 80 mass%, at least 85 mass%, at least 90 mass%, or at least 95 mass% of the at least two EBV antigen-encoding mRNA constructs, thereby forming the lipid nanoparticles (LNPs). In the aspect, each of the at least two EBV antigen-encoding mRNA constructs comprise a segment that encodes an Epstein-Barr virus (EBV) antigen. Since there are at least two EBV antigen-encoding mRNA constructs, and since each of the at least two EBV antigen-encoding mRNA constructs comprise a segment that encodes the EBV antigen, there are thereby at least two EBV antigens. In the aspect, the EBV antigens comprise, consist of, or are an EBV B cell module antigen or an EBV T cell module antigen. In some (preferred) embodiments, the EBV antigens comprise, consist of, or are an EBV T cell module antigen. In some (preferred) embodiments, the EBV antigens comprises, consists of, or is the EBV B cell module antigen. In some (preferred) embodiments, the EBV antigens comprises, consists of, or is the EBV B cell module antigen and the EBV T cell module antigen. In some embodiments, the EBV T cell module antigen comprises, consists of, or is at least two of: (a) an EBV latent membrane protein-1 (LMP1) antigen; (b) an EBV latent membrane protein-2 (LMP2) antigen; (c) an EBV nuclear antigen-1 (EBNA1) antigen; (d) an EBV nuclear antigen-3A (EBNA3A) antigen; and (e) a BamHI Z EBV replication activator (ZEBRA) antigen. In some embodiments, the EBV T cell module antigen comprises, consists of, or is at least three, at least four, Attorney Docket No: 70488WO01 or each of: (a) an EBV latent membrane protein-1 (LMP1) antigen; (b) an EBV latent membrane protein-2 (LMP2) antigen; (c) an EBV nuclear antigen-1 (EBNA1) antigen; (d) an EBV nuclear antigen-3A (EBNA3A) antigen; and (e) a BamHI Z EBV replication activator (ZEBRA) antigen. In some embodiments, the EBV B cell module antigen comprises, consists of, or is an EBV glycoprotein-220 (gp220) antigen. In some embodiments, the EBV B cell module antigen further comprises, consists of, or is an EBV glycoprotein-42 (gp42) antigen, an EBV glycoprotein-H (gH) antigen, or an EBV glycoprotein-L (gL) antigen. In some embodiments, the EBV B cell module antigen comprises, consists of, or is the EBV gp220 antigen, and two or more of, or each of: the EBV gp42 antigen, the EBV gH antigen, and the EBV gL antigen. In some embodiments the EBV B cell module antigen comprises, consists of, or is the EBV gp220 antigen, the EBV gp42 antigen, the EBV gH antigen, and the EBV gL antigen. EBV ANTIGEN-ENCODING MRNA CONSTRUCTS COMPRISING A SEGMENT THAT ENCODES A T CELL MODULE ANTIGEN In some embodiments: i. the EBV LMP1 antigen comprises, consists of, or is an EBV LMP1 protein or an EBV LMP1 protein fragment; ii. the EBV LMP2 antigen comprises, consists of, or is an EBV LMP2 protein or an EBV LMP2 protein fragment; iii. the EBNA1 antigen comprises, consists of, or is an EBNA1 protein or an EBNA1 protein fragment; iv. the EBNA3A antigen comprises, consists of, or is an EBNA3A protein or an EBNA3A protein fragment; and / or v. the ZEBRA antigen comprises, consists of, or is the ZEBRA protein or a ZEBRA protein fragment. In some embodiments, the EBV LMP1 antigen comprises, consists of, or is the EBV LMP1 protein. In some embodiments, the EBV LMP2 antigen comprises, consists of, or is the EBV LMP2 protein. In some embodiments, the EBNA1 antigen comprises, consists of, or is the EBNA1 protein. In some embodiments, the EBNA3A antigen comprises, consists of, or is the EBNA3A protein. In some embodiments, the ZEBRA antigen comprises, consists of, or is the ZEBRA protein. In some embodiments, the EBV LMP1 antigen comprises, consists of, or is the EBV LMP1 protein; the EBV LMP2 antigen comprises, consists of, or is the EBV LMP2 protein; the EBNA1 antigen comprises, consists of, or is the EBNA1 protein; the EBNA3A antigen comprises, consists of, or is the EBNA3A protein; or the ZEBRA antigen comprises, consists of, or is the ZEBRA protein. In some embodiments, the EBV LMP1 antigen comprises, consists of, or is the EBV LMP1 protein; the EBV LMP2 antigen comprises, consists of, or is the EBV LMP2 protein; the EBNA1 antigen comprises, consists of, or is the EBNA1 protein; the EBNA3A antigen comprises, consists of, or is the EBNA3A protein; and the ZEBRA antigen comprises, consists of, or is the ZEBRA protein. Attorney Docket No: 70488WO01 In some embodiments, the T cell module antigen comprises, consists of, or is the EBV LMP2 protein and the EBNA3A protein. In some embodiments, the T cell module antigen comprises, or in the case of embodiments in this paragraph further comprises, the EBV LMP1 protein. In some embodiments, the T cell module antigen comprises, or in the case of embodiments in this paragraph further comprises, the EBNA1 protein. In some embodiments, the T cell module antigen comprises, or in the case of embodiments in this paragraph further comprises, ZEBRA protein. In some embodiments, the EBV LMP1 protein has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 1. In some embodiments, the EBV LMP1 protein fragment has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, or SEQ ID NO: 5. In some embodiments, the EBV LMP2 protein has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 6 or SEQ ID NO: 7. In some embodiments, the EBV LMP2 protein fragment has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, or SEQ ID NO: 11. In some embodiments, the EBNA1 protein has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 12. In some embodiments, the EBNA1 protein fragment has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 13, SEQ ID NO: 14, or SEQ ID NO: 15. In some embodiments, the EBNA3A protein has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 16. In some embodiments, the EBNA3A protein fragment has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 22, or SEQ ID NO: 23. In some embodiments, the ZEBRA protein has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 24. In some embodiments, the ZEBRA protein fragment has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 25 or SEQ ID NO: 26. In some embodiments, the EBV LMP1 antigen comprises, consists of, or is the EBV LMP1 protein fragment. In some embodiments, the EBV LMP2 antigen comprises, or further comprises, consists of, or is in the case of embodiments in this paragraph, the EBV LMP2 protein fragment. In some embodiments, the EBNA1 antigen comprises, or further comprises, consists of, or is in the case of embodiments in this paragraph, the EBNA1 protein fragment. In some embodiments, the EBNA3A antigen comprises, or further comprises, consists of, or is in the case of embodiments in this paragraph, the EBNA3A protein fragment. In some embodiments, the ZEBRA antigen comprises, or further comprises, consists of, or is in the case of embodiments in this paragraph, the ZEBRA antigen protein fragment. In some embodiments, the EBV LMP1 antigen comprises, consists of, or is the EBV LMP1 protein fragment; the EBV LMP2 antigen comprises, consists of, or is the EBV LMP2 protein fragment; the EBNA1 antigen comprises, consists of, or is the EBNA1 protein Attorney Docket No: 70488WO01 fragment; the EBNA3A antigen comprises, consists of, or is the EBNA3A protein fragment; or the ZEBRA antigen comprises, consists of, or is the ZEBRA protein fragment. In some embodiments, the EBV LMP1 antigen comprises, consists of, or is the EBV LMP1 protein fragment; the EBV LMP2 antigen comprises, consists of, or is the EBV LMP2 protein fragment; the EBNA1 antigen comprises, consists of, or is the EBNA1 protein fragment; the EBNA3A antigen comprises, consists of, or is the EBNA3A protein fragment; and the ZEBRA antigen comprises, consists of, or is the ZEBRA protein fragment. Thus, in some embodiments, the EBV T cell module antigen comprises, consists of, or is at least one, two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, sixteen, seventeen, eighteen, nineteen, or at least twenty fragments of one or more proteins including, but not limited to, LMP1, LMP2, EBNA1, EBNA3A, and ZEBRA. In some embodiments, an EBV T cell module antigen comprises: (1) one, two, three, or four LMP1 protein fragments; (2) one, two, three, or four LMP2 protein fragments; (3) one, two, or three EBNA1 protein fragments; (4) one, two, three, four, five, six, or seven EBNA3A fragments; and / or (5) one or two ZEBRA protein fragments. In some embodiments, an EBV T cell module antigen comprises, consists of, or is one, two, three, four, or five of the following numerals (i.e. (1), (2), (3), (4), or (5)): (1) one, two, three, or four LMP1 protein fragments; (2) one, two, three, or four LMP2 protein fragments; (3) one, two, or three EBNA1 protein fragments; (4) one, two, three, four, five, six, or seven EBNA3A fragments; and / or (5) one or two ZEBRA protein fragments. A “protein fragment” (sometimes shortened to just “fragment”) of an EBV protein, as used herein, means a fragment smaller than a full-length, endogenous EBV protein (note gp220 is not a fragment of gp350 at least because it is the result of translation of an internal splice variant of different mRNA, nor is LMP2B a fragment of LMP2A because both are encoded on different genes and because of accepted nomenclature). Protein fragments include fragments of at least 8, at least 9, at least 10, at least 11, at least 12, at least 13, at least 14, at least 15, at least 20, at least 30, at least 40, at least 50, at least 60, at least 70, at least 80, at least 90 and at least 100 amino acids of the full-length protein. In some embodiments, protein fragments consist of about 8, about 9, about 10, about 11, about 12, about 13, about 14, about 15, about 20, about 30, about 40, about 50, about 60, about 70, about 80, about 90 and about 100 amino acids of the full-length protein. Protein fragments may have one or more substitutions, deletions, or insertions relative to the full- length protein from which the fragment is derived. Thus, protein fragments include fragments at least 0.1%, at least 0.5%, at least 1%, at least 2%, at least 3%, at least 4%, at least 5%, at least 6%, at least 7%, at least 8%, at least 9%, at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identical to the corresponding region of the full-length protein. In certain embodiments, an EBV antigen comprises, consists of, or is an EBV latent membrane protein-1 (LMP1) antigen. EBV LMP1, as a protein, (c.f. EBV LMP1 antigen) is a 386 amino acid protein expressed during the latent stage of the EBV viral life cycle. In some embodiments, the EBV Attorney Docket No: 70488WO01 LMP1 protein comprises, consists of, or is the amino acid sequence of SEQ ID NO: 1. In some embodiments, LMP1 protein fragments include fragments of at least 8, at least 9, at least 10, at least 11, at least 12, at least 13, at least 14, at least 15, at least 20, at least 30, at least 40, at least 50, at least 60, at least 70, at least 80, at least 90 and at least 100 amino acids of SEQ ID NO: 1. In some embodiments, LMP1 protein fragments consist of about 8, about 9, about 10, about 11, about 12, about 13, about 14, about 15, about 20, about 30, about 40, about 50, about 60, about 70, about 80, about 90 and about 100 amino acids of SEQ ID NO: 1. In other embodiments, LMP1 protein fragment antigens include fragments at least 0.1%, at least 0.5%, at least 1%, at least 2%, at least 3%, at least 4%, at least 5%, at least 6%, at least 7%, at least 8%, at least 9%, at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identical to the corresponding region of SEQ ID NO: 1. In some embodiments, the EBV LMP1 protein fragment comprises, consists of, or is one or more T cell epitopes. In certain embodiments, LMP1 protein fragment includes, but are not limited to, one or more of SEQ ID NOs: 2-5 and fragments that have at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NOs: 2-5. In some embodiments, the EBV LMP1 protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 2. In some embodiments, the EBV LMP1 protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 3. In some embodiments, the EBV LMP1 protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 4. In some embodiments, the EBV LMP1 protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 5. In some embodiments, the EBV LMP1 protein fragment comprises, consists of, or is or consists of SEQ ID NO: 2. In some embodiments, the EBV LMP1 protein fragment comprises, consists of, or is or consists of SEQ ID NO: 3. In some embodiments, the EBV LMP1 protein fragment comprises, consists of, or is or consists of SEQ ID NO: 4. In some embodiments, the EBV LMP1 protein fragment comprises, consists of, or is or consists of SEQ ID NO: 5. In some embodiments, an EBV antigen comprises, consists of, or is a Latent Membrane Protein 2 (LMP2) antigen, which includes LMP2A and LMP2B. See definition above. LMP2A is a 497 amino acid protein and LMP2B is a 378 amino acid protein, each of which are expressed during the latent stage of the EBV viral life cycle. In certain embodiments, the EBV LMP2 protein comprises, consists of, or is the amino acid sequence of SEQ ID NO: 6 (LMP2A) and SEQ ID NO: 7 (LMP2B). In some embodiments, LMP2 protein fragment includes fragments of at least 8, at least 9, at least 10, at least 11, at least 12, at least 13, at least 14, at least 15, at least 20, at least 30, at least 40, at least 50, at least 60, at least 70, at least 80, at least 90 and at least 100 amino acids of SEQ ID NO: 6. In some embodiments, LMP2 protein fragment consists of about 8, about 9, about 10, about 11, about 12, about 13, about 14, about 15, about 20, about 30, about 40, about 50, about 60, about 70, about 80, Attorney Docket No: 70488WO01 about 90 and about 100 amino acids of SEQ ID NO: 6. In some embodiments, LMP2 protein fragment includes fragments at least 0.1%, at least 0.5%, at least 1%, at least 2%, at least 3%, at least 4%, at least 5%, at least 6%, at least 7%, at least 8%, at least 9%, at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identical to the corresponding region of SEQ ID NO: 6. In some embodiments, the EBV LMP2 protein fragment comprises, consists of, or is one or more T cell epitopes. In some embodiments, LMP2 protein fragment includes, but are not limited to, one or more of SEQ ID NOs: 8-11, and fragments that have at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NOs: 8-11. In some embodiments, the EBV LMP2 protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 8. In some embodiments, the EBV LMP2 protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 9. In some embodiments, the EBV LMP2 protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 10. In some embodiments, the EBV LMP2 protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 11. In some embodiments, the EBV LMP2 protein fragment comprises, consists of, or is or consists of SEQ ID NO: 8. In some embodiments, the EBV LMP2 protein fragment comprises, consists of, or is or consists of SEQ ID NO: 9. In some embodiments, the EBV LMP2 protein fragment comprises, consists of, or is or consists of SEQ ID NO: 10. In some embodiments, the EBV LMP2 protein fragment comprises, consists of, or is or consists of SEQ ID NO: 11. In certain embodiments, an EBV antigen comprises, consists of, or is an Epstein-Barr Nuclear Antigen 1 (EBNA1) antigen. EBNA1 is a 641 amino acid protein expressed during the latent stage of the EBV viral life cycle. In certain embodiments, the EBNA1 protein comprises, consists of, or is the amino acid sequence of SEQ ID NO: 12. In some embodiments, EBNA1 protein fragment includes fragments of at least 8, at least 9, at least 10, at least 11, at least 12, at least 13, at least 14, at least 15, at least 20, at least 30, at least 40, at least 50, at least 60, at least 70, at least 80, at least 90 and at least 100 amino acids of SEQ ID NO: 12. In some embodiments, EBNA1 protein fragment consists of about 8, about 9, about 10, about 11, about 12, about 13, about 14, about 15, about 20, about 30, about 40, about 50, about 60, about 70, about 80, about 90 and about 100 amino acids of SEQ ID NO: 12. In other embodiments, EBNA1 protein fragment includes fragments at least 80%, at least 0.1%, at least 0.5%, at least 1%, at least 2%, at least 3%, at least 4%, at least 5%, at least 6%, at least 7%, at least 8%, at least 9%, at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 85%, at least 90%, at least 95% or at least 99% identical to the corresponding region of SEQ ID NO: 12. In some embodiments, an EBNA1 protein fragment comprises, consists of, or is one or more T cell epitopes. In certain embodiments, EBNA1 protein fragment includes, but are not limited to, one Attorney Docket No: 70488WO01 or more of SEQ ID NOs: 13-15, and fragments at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identical to SEQ ID NOs: 13-15. In some embodiments, the EBNA1 protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 13. In some embodiments, the EBNA1 protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 14. In yet other embodiments, the EBNA1 protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 15. In some embodiments, the EBNA1 protein fragment comprises, consists of, or is or consists of SEQ ID NO: 13. In some embodiments, the EBNA1 protein fragment comprises, consists of, or is or consists of SEQ ID NO: 14. In some embodiments, the EBNA1 protein fragment comprises, consists of, or is or consists of SEQ ID NO: 15. In additional embodiments, the EBNA1 protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to a contiguous stretch of amino acid residues 1-22 and 66-86 of SEQ ID NO: 12. In other embodiments, the EBNA1 protein fragment comprises, consists of, or is a sequence that is identical to a contiguous stretch of amino acid residues 1-22 and 66-86 of SEQ ID NO: 12. Thus, In some embodiments, the EBNA1 protein fragment (that comprises, consists of, or is a sequence that is identical to a contiguous stretch of amino acid residues 1-22 and 66-86 of SEQ ID NO: 12) has a deletion of amino acid residues 23-65 of SEQ ID NO: 12. In some embodiments, amino acid residues 23-65 of EBNA1 (SEQ ID NO: 11) displays homology to Ro and SmD1 proteins (James and Harley, J. Immunol., 1992; McCain et al., Nat. Med., 2015). Ro and SmD1 proteins are known cross-reacting epitopes that have been reported as targets of autoantibodies in autoimmune disease, such as systemic lupus erythematosus (SLE). Thus, in certain embodiments, the EBNA1 protein fragment that has a deletion of amino acid residues 23-65 of SEQ ID NO: 12 shows reduced cross-reactivity to Ro and / or SmD1 proteins compared to a EBNA1 fragment that does not have a deletion of amino acid residues 23-65 of SEQ ID NO: 12. In further embodiments, the EBNA1 protein fragment that has a deletion of amino acid residues 23-65 of SEQ ID NO: 12 does not cross-react with Ro and / or SmD1 proteins. In yet other embodiments, the EBNA1 protein fragment that has a deletion of amino acid residues 23-65 of SEQ ID NO: 12 shows reduced autoantibody formation compared to a EBNA1 fragment that does not have a deletion of amino acid residues 23-65 of SEQ ID NO: 12. In still other embodiments, the EBNA1 protein fragment that has a deletion of amino acid residues 23-65 of SEQ ID NO: 12 does show any autoantibody formation. In additional embodiments, the EBNA1 protein fragment that has a deletion of amino acid residues 23-65 of SEQ ID NO: 12 comprises, consists of, or is SEQ ID NO: 13. C-terminal of EBNA1 (e.g., amino acid residues 454-619 of SEQ ID NO: 12) contains most of the known human T cell epitopes (Thomas OG, et al. Sci Adv 2023; Lanz TV, et al. Nature 2022; James JA, et al. Arthritis Rheumatol, 2001; McClain MT, et al J Med Virol 2003; Mechelli R, et al. Mult Scler, Attorney Docket No: 70488WO01 2011; Jog NR, et al. J Autoimmun, 2020; Tengvall K, et al. PNAS 2019). This region of C-terminal EBNA1 (i.e., amino acid residues 454-619 of SEQ ID NO: 12) also excludes known molecular mimicry sequences linked to autoantibody reactivity in MS. Additionally, splitting the immunogenic C- terminal of EBNA1 in two fragments (e.g., to amino acid residues 454-503 and 504-619) abrogates residual EBNA1 activity. Thus, in additional embodiments, the EBNA1 protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to amino acid residues 454-503 of SEQ ID NO: 12. In yet other embodiments, the EBNA1 protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to amino acid residues 504-619 of SEQ ID NO: 12. In additional embodiments, the EBNA1 protein fragment comprises, consists of, or is or consists of a contiguous stretch of amino acid residues 1-22 and 66-86 of SEQ ID NO: 12. In other embodiments, the EBNA1 protein fragment comprises, consists of, or is or consists of amino acid residues 454-503 of SEQ ID NO: 12. In yet other embodiments, the EBNA1 protein fragment comprises, consists of, or is or consists of amino acids 505-619 of SEQ ID NO: 12. FIG.49 shows an embodiment of a schematic representation of full length EBNA1 protein (SEQ ID NO: 12) and EBNA1 protein fragments (EBNA1 fragment 1: SEQ ID NO: 13; EBNA1 fragment 2: SEQ ID NO: 14; and EBNA1 fragment 3: SEQ ID NO: 15). In certain embodiments, an EBV antigen comprises, consists of, or is an Epstein-Barr Nuclear Antigen 3A (EBNA3A) antigen. EBNA3A is a 944 amino acid protein expressed during the latent stage of the EBV viral life cycle. In certain embodiments, the EBNA3A protein comprises, consists of, or is the amino acid sequence of SEQ ID NO: 16. In some embodiments, EBNA3A protein fragment includes fragments of at least 8, at least 9, at least 10, at least 11, at least 12, at least 13, at least 14, at least 15, at least 20, at least 30, at least 40, at least 50, at least 60, at least 70, at least 80, at least 90 and at least 100 amino acids of SEQ ID NO: 16. In some embodiments, EBNA3A protein fragment consists of about 8, about 9, about 10, about 11, about 12, about 13, about 14, about 15, about 20, about 30, about 40, about 50, about 60, about 70, about 80, about 90 and about 100 amino acids of SEQ ID NO: 16. In other embodiments, EBNA3A protein fragment includes fragments at least 0.1%, at least 0.5%, at least 1%, at least 2%, at least 3%, at least 4%, at least 5%, at least 6%, at least 7%, at least 8%, at least 9%, at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identical to the corresponding region of SEQ ID NO: 16. In some embodiments, the EBNA3a protein fragment comprises, consists of, or is one or more T cell epitopes. In certain embodiments, EBNA3A protein fragment includes, but are not limited to, one or more of SEQ ID Nos: 17-23, and fragments at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identical to SEQ ID NOs: 17-23. In some embodiments, the EBNA3a protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 17. In some embodiments, the EBNA3a protein Attorney Docket No: 70488WO01 fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 18. In some embodiments, the EBNA3a protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 19. In some embodiments, the EBNA3a protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 20. In some embodiments, the EBNA3a protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 21. In some embodiments, the EBNA3a protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 22. In some embodiments, the EBNA3a protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 23. In some embodiments, the EBNA3a protein fragment comprises, consists of, or is or consists of SEQ ID NO: 17. In some embodiments, the EBNA3a protein fragment comprises, consists of, or is or consists of SEQ ID NO: 18. In some embodiments, the EBNA3a protein fragment comprises, consists of, or is or consists of SEQ ID NO: 19. In some embodiments, the EBNA3a protein fragment comprises, consists of, or is or consists of SEQ ID NO: 20. In some embodiments, the EBNA3a protein fragment comprises, consists of, or is or consists of SEQ ID NO: 21. In some embodiments, the EBNA3a protein fragment comprises, consists of, or is or consists of SEQ ID NO: 22. In some embodiments, the EBNA3a protein fragment comprises, consists of, or is or consists of SEQ ID NO: 23. In certain embodiments, an EBV antigen comprises, consists of, or is a ZEBRA antigen. ZEBRA is a 245 amino acid protein expressed during the lytic stage of the EBV viral life cycle. In certain embodiments, the EBV ZEBRA protein comprises, consists of, or is the amino acid sequence of SEQ ID NO: 24. In some embodiments, the ZEBRA protein fragments include fragments of at least 8, at least 9, at least 10, at least 11, at least 12, at least 13, at least 14, at least 15, at least 20, at least 30, at least 40, at least 50, at least 60, at least 70, at least 80, at least 90 and at least 100 amino acids of SEQ ID NO: 24. In some embodiments, the ZEBRA protein fragments consist of about 8, about 9, about 10, about 11, about 12, about 13, about 14, about 15, about 20, about 30, about 40, about 50, about 60, about 70, about 80, about 90 and about 100 amino acids of SEQ ID NO: 24. In other embodiments, the ZEBRA protein fragments include fragments at least 0.1%, at least 0.5%, at least 1%, at least 2%, at least 3%, at least 4%, at least 5%, at least 6%, at least 7%, at least 8%, at least 9%, at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identical to the corresponding region of SEQ ID NO: 24. In some embodiments, the ZEBRA protein fragment comprises, consists of, or is one or more T cell epitopes. In certain embodiments, the ZEBRA protein fragment includes, but are not limited to, one or more of SEQ ID NOs: 25-26, and fragments at least 80%, at least 85%, at least 90%, at least Attorney Docket No: 70488WO01 95% or at least 99% identical to SEQ ID NOs: 25-26. In some embodiments, the ZEBRA protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 25. In some embodiments, the ZEBRA protein fragment comprises, consists of, or is a sequence that has at least 80%, at least 85%, at least 90%, at least 95% or at least 99% identity to SEQ ID NO: 26. In some embodiments, the ZEBRA protein fragment comprises, consists of, or is or consists of SEQ ID NO: 25. In some embodiments, the ZEBRA protein fragment comprises, consists of, or is or consists of SEQ ID NO: 26. In some embodiments, T cell module antigen comprises, consists of, or is a recombinant (a.k.a. mosaic) T cell module antigen. In some embodiments, the recombinant T cell module antigen comprises: (i) at least two EBV LMP1 protein fragments; (ii) at least two EBV LMP2 protein fragments; (iii) at least two EBNA1 protein fragments; (iv) at least two EBNA3A protein fragments; or (v) at least two ZEBRA protein fragments. In some embodiments, the recombinant T cell module antigen comprises, consists of, or is at least two of, at least three of, or at least four of (i), (ii), (iii), (iv), or (v), which follow: (i) at least two EBV LMP1 protein fragments; (ii) at least two EBV LMP2 protein fragments; (iii) at least two EBNA1 protein fragments; (iv) at least two EBNA3A protein fragments; and (v) at least two ZEBRA protein fragments. In some embodiments, the recombinant T cell module antigen comprises: (i) at least two EBV LMP1 protein fragments; (ii) at least two EBV LMP2 protein fragments; (iii) at least two EBNA1 protein fragments; (iv) at least two EBNA3A protein fragments; and (v) at least two ZEBRA protein fragments. In some embodiments, the recombinant T cell module antigen comprises: (i) at least two EBV LMP1 protein fragments, which are not adjacent to each other on the recombinant T cell module antigen; (ii) at least two EBV LMP2 protein fragments, which are not adjacent to each other on the recombinant T cell module antigen; (iii) at least two EBNA1 protein fragments, which are not adjacent to each other on the recombinant T cell module antigen; (iv) at least two EBNA3A protein fragments, which are not adjacent to each other on the recombinant T cell module antigen; or (v) at least two ZEBRA protein fragments, which are not adjacent to each other on the recombinant T cell module antigen. In some embodiments, the recombinant T cell module antigen comprises, consists of, or is at least two of, at least three of, or at least four of (i), (ii), (iii), (iv), or (v), which follow: (i) at least two EBV LMP1 protein fragments, which are not adjacent to each other on the recombinant T cell module antigen; (ii) at least two EBV LMP2 protein fragments, which are not adjacent to each other on the recombinant T cell module antigen; (iii) at least two EBNA1 protein fragments, which are not adjacent to each other on the recombinant T cell module antigen; (iv) at least two EBNA3A protein fragments, which are not adjacent to each other on the recombinant T cell module antigen; or (v) at least two ZEBRA protein fragments, which are not adjacent to each other on the recombinant T cell module antigen. In some embodiments, the recombinant T cell module antigen comprises: (i) at least two EBV LMP1 protein fragments, which are not adjacent to each other on the recombinant T cell module antigen; (ii) at least two EBV LMP2 protein fragments, which are not adjacent to each other on the recombinant T cell module antigen; (iii) at least two EBNA1 protein fragments, which are not adjacent to each other on the recombinant T Attorney Docket No: 70488WO01 cell module antigen; (iv) at least two EBNA3A protein fragments, which are not adjacent to each other on the recombinant T cell module antigen; and (v) at least two ZEBRA protein fragments, which are not adjacent to each other on the recombinant T cell module antigen. In some embodiments, the recombinant T cell module antigen comprises, consists of, or is at least two EBV LMP2 protein fragments, which are not adjacent to each other on the recombinant T cell module antigen, and at least two EBNA3A protein fragments, which are not adjacent to each other on the recombinant T cell module antigen. In some embodiments, the recombinant T cell module antigen comprises, or further comprises, consists of, or is in the case of the embodiments noted in this paragraph, at least two EBV LMP1 protein fragments, which are not adjacent to each other on the recombinant T cell module antigen. In some embodiments, the recombinant T cell module antigen comprises, or further comprises, consists of, or is in the case of the embodiments noted in this paragraph, at least two EBNA1 protein fragments, which are not adjacent to each other on the recombinant T cell module antigen. In some embodiments, the recombinant T cell module antigen comprises, , or further comprises, consists of, or is in the case of the embodiments noted in this paragraph, two of the ZEBRA fragments; each ZEBRA fragment being not adjacent to the other on the T cell module antigen. In some embodiments, the pharmaceutical composition comprises at least three of the EBV antigen-encoding mRNA constructs. In some embodiments, the pharmaceutical composition comprises, consists of, or is at least three of the EBV antigen-encoding mRNA constructs; the EBV antigens comprises, consists of, or is at least two of the recombinant T cell module antigens. In some embodiments, the pharmaceutical composition comprises, consists of, or is at least three of the EBV antigen-encoding mRNA constructs; the EBV antigens comprises, consists of, or is at least two of the recombinant T cell module antigens; the first of the EBV antigen-encoding mRNA constructs comprises, consists of, or is the segment that encodes the first of the recombinant T cell module antigens; the second of the EBV antigen-encoding mRNA constructs comprises, consists of, or is the segment that encodes the second of the recombinant T cell module antigens. 2-SPLIT T CELL MODULE DESIGNS AND OTHER EBV ANTIGEN-ENCODING MRNA CONSTRUCTS THEREIN In some embodiments, the pharmaceutical composition comprises, consists of, or is at least three of the EBV antigen-encoding mRNA constructs; the EBV antigens comprises, consists of, or is at least two of the recombinant T cell module antigens; the first of the EBV antigen-encoding mRNA constructs comprises, consists of, or is the segment that encodes the first of the recombinant T cell module antigens; the second of the EBV antigen-encoding mRNA constructs comprises, consists of, or is the segment that encodes the second of the recombinant T cell module antigens; the at least two of the recombinant T cell module antigens comprises: (a) at least four of the EBV LMP1 protein fragments, (b) at least four of the EBV LMP2 protein fragments, (c) at least three of the EBNA1 protein fragments, and (d) at least seven of the EBNA3A protein fragments. In some embodiments, the pharmaceutical composition comprises, consists of, or is at least three of the EBV antigen- Attorney Docket No: 70488WO01 encoding mRNA constructs; the EBV antigens comprises, consists of, or is at least two of the recombinant T cell module antigens; the first of the EBV antigen-encoding mRNA constructs comprises, consists of, or is the segment that encodes the first of the recombinant T cell module antigens; the second of the EBV antigen-encoding mRNA constructs comprises, consists of, or is the segment that encodes the second of the recombinant T cell module antigens; the at least two of the recombinant T cell module antigens comprises: (a) at least four of the EBV LMP1 protein fragments, (b) at least four of the EBV LMP2 protein fragments, (c) at least three of the EBNA1 protein fragments, and (d) at least seven of the EBNA3A protein fragments; the first of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 2; the second of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 3; the third of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 4; the fourth of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 5; the first of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 8; the second of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 9; the third of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 10; the fourth of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 11; the first of the EBNA1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 13; the second of the EBNA1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 14; the third of the EBNA1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 15; the first of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 17; the second of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 18; the third of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 19; the fourth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 20; the fifth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 21; the sixth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 22; and the seventh of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 23. In some embodiments, the pharmaceutical composition comprises, consists of, or is at least three of the EBV antigen-encoding mRNA constructs; the EBV antigens comprises, consists of, or is at least two of the recombinant T cell module antigens; the first of the EBV antigen-encoding mRNA Attorney Docket No: 70488WO01 constructs comprises, consists of, or is the segment that encodes the first of the recombinant T cell module antigens; the second of the EBV antigen-encoding mRNA constructs comprises, consists of, or is the segment that encodes the second of the recombinant T cell module antigens; the at least two of the recombinant T cell module antigens comprises: (a) at least four of the EBV LMP1 protein fragments, (b) at least four of the EBV LMP2 protein fragments, (c) at least three of the EBNA1 protein fragments, and (d) at least seven of the EBNA3A protein fragments; the first of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 2; the second of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 3; the third of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 4; the fourth of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 5; the first of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 8; the second of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 9; the third of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 10; the fourth of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 11; the first of the EBNA1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 13; the second of the EBNA1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 14; the third of the EBNA1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 15; the first of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 17; the second of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 18; the third of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 19; the fourth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 20; the fifth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 21; the sixth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 22; the seventh of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 23; at least two of, or at least three of, the first, second, third, and fourth of the EBV LMP1 protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens; at least two of, or at least three of, the first, second, third, and fourth of the EBV LMP2 protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens; at least two of the first, second, and third of the EBNA1 protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens; and at least two of, at least Attorney Docket No: 70488WO01 three of, at least four of, at least five of, or at least six of the first, second, third, fourth, fifth, sixth, and seventh of the EBNA3A protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens. In some embodiments therein; the first, second, third, and fourth of the EBV LMP1 protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens; the first, second, third, and fourth of the EBV LMP2 protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens; the first, second, and third of the EBNA1 protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens; and the first, second, third, fourth, fifth, sixth, and seventh of the EBNA3A protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens. In some embodiments therein, the at least two recombinant T cell module antigens further comprise a first of the ZEBRA protein fragments, which has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 25, and a second of the ZEBRA protein fragments, which has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO:26. In some embodiments therein, the at least two recombinant T cell module antigens further comprise a first of the ZEBRA protein fragments, which has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 25, and a second of the ZEBRA protein fragments, which has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO:26; the first of the recombinant T cell module antigens comprises, from N-terminus to C-terminus, the second of the EBNA1 protein fragments, the seventh of the EBNA3A protein fragments, the fourth of the EBV LMP2 protein fragments, the second of the ZEBRA protein fragments, the first of the EBNA3A protein fragments, the second of the EBV LMP1 protein fragments, the sixth of the EBNA3A protein fragments, the third of the EBV LMP2 protein fragments, the third of the EBV LMP1 protein fragments, and the fifth of the EBNA3A protein fragments. In some embodiments therein, the segment that encodes the first of the recombinant T cell module antigens comprising a sequence having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 30 or SEQ ID NO: 120. In some embodiments of the last paragraph, the second of the recombinant T cell module antigens comprises, from N-terminus to C-terminus, the second of the EBV LMP2 protein fragments, the fourth of the EBV LMP1 protein fragments, the fourth of the EBNA3A protein fragments, the first of the EBV LMP1 protein fragments, the first of the EBNA1 protein fragments, the third of the EBNA3A protein fragments, the first of the EBV LMP2 protein fragments, the second of the EBNA3A protein fragments, the first of the ZEBRA protein fragments, and the third of the EBNA1 protein fragments. In some embodiments therein, the segment that encodes the second of the recombinant T cell module antigens comprising a sequence having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 32 or SEQ ID NO: 121. Accordingly, in some embodiments, the first of the recombinant T cell module antigens has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 29; and Attorney Docket No: 70488WO01 the second of the recombinant T cell module antigens has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 31 In some embodiments therein, the pharmaceutical composition comprises, consists of, or is at least six of the EBV antigen-encoding mRNA constructs; the third of the EBV antigen-encoding mRNA constructs comprises, consists of, or is the segment that encodes the EBV gp42 antigen; the fourth of the EBV antigen-encoding mRNA constructs comprises, consists of, or is the segment that encodes the EBV gH antigen; the fifth of the EBV antigen-encoding mRNA constructs comprises, consists of, or is the segment that encodes the EBV gL antigen; and the sixth of the EBV antigen- encoding mRNA constructs comprises, consists of, or is the segment that encodes the EBV gp220 antigen. Accordingly, some embodiments will have one, two, three, or each of (i), (ii), (iii), and (iv) which follow: (i) the EBV gp42 antigen comprising an EBV gp42 protein or an EBV gp42 protein fragment, the EBV gp42 protein comprising a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 43; (ii) the EBV gH antigen comprising an EBV gH protein or an EBV gH protein fragment; the EBV gH protein comprising a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 39; (iii) the EBV gL antigen comprising an EBV gL protein or an EBV gL protein fragment, the EBV gL protein comprising a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 41; and / or (iv) the EBV gp220 antigen comprising an EBV gp220 protein or an EBV gp220 protein fragment, the EBV gp220 protein comprising a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 45. In some embodiments, the EBV gp42 antigen comprises, consists of, or is the EBV gp42 protein, the at least two EBV antigen-encoding mRNA constructs thereby comprising a segment that encodes the EBV gp42 protein; the EBV gH antigen comprises, consists of, or is the EBV gH protein, the at least two EBV antigen-encoding mRNA constructs thereby comprising a segment that encodes the EBV gH protein; the EBV gL antigen comprises, consists of, or is the EBV gL protein, the at least two EBV antigen-encoding mRNA constructs thereby comprising a segment that encodes the EBV gL protein; and / or the EBV gp220 antigen comprises, consists of, or is the EBV gp220 protein, the at least two EBV antigen-encoding mRNA constructs thereby comprising a segment that encodes the EBV gp220 protein. In some embodiments, the pharmaceutical composition comprises, consists of, or is at least four of the EBV antigen-encoding mRNA constructs. In some embodiments, the pharmaceutical composition comprises, consists of, or is at least four of the EBV antigen-encoding mRNA constructs; the EBV antigens comprises, consists of, or is at least three of the recombinant T cell module antigens; the first of the EBV antigen-encoding mRNA constructs comprises, consists of, or is the segment that encodes the first of the recombinant T cell module antigens; the second of the EBV antigen-encoding mRNA constructs comprises, consists of, or is the segment that encodes the second of the recombinant T cell module antigens; and the third of the EBV antigen-encoding mRNA Attorney Docket No: 70488WO01 constructs comprises, consists of, or is the segment that encodes the third of the recombinant T cell module antigens. In some embodiments, the pharmaceutical composition comprises, consists of, or is at least four of the EBV antigen-encoding mRNA constructs; the EBV antigens comprises, consists of, or is at least three of the recombinant T cell module antigens; the first of the EBV antigen- encoding mRNA constructs comprises, consists of, or is the segment that encodes the first of the recombinant T cell module antigens; the second of the EBV antigen-encoding mRNA constructs comprises, consists of, or is the segment that encodes the second of the recombinant T cell module antigens; and the third of the EBV antigen-encoding mRNA constructs comprises, consists of, or is the segment that encodes the third of the recombinant T cell module antigens; the at least three of the recombinant T cell module antigens comprises: (a) at least four of the EBV LMP1 protein fragments, (b) at least four of the EBV LMP2 protein fragments, (c) at least three of the EBNA1 protein fragments, and (d) at least seven of the EBNA3A protein fragments; the first of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 2; the second of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 3; the third of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 4; the fourth of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 5; the first of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 8; the second of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 9; the third of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 10; the fourth of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 11; the first of the EBNA1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 13; the second of the EBNA1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 14; the third of the EBNA1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 15; the first of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 17; the second of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 18; the third of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 19; the fourth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 20; the fifth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 21; the sixth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 22; and the seventh of the Attorney Docket No: 70488WO01 EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 23. 3-SPLIT T CELL MODULE DESIGNS AND OTHER EBV ANTIGEN-ENCODING MRNA CONSTRUCTS THEREIN In some embodiments, the pharmaceutical composition comprises, consists of, or is at least four of the EBV antigen-encoding mRNA constructs; the EBV antigens comprises, consists of, or is at least three of the recombinant T cell module antigens; the first of the EBV antigen-encoding mRNA constructs comprises, consists of, or is the segment that encodes the first of the recombinant T cell module antigens; the second of the EBV antigen-encoding mRNA constructs comprises, consists of, or is the segment that encodes the second of the recombinant T cell module antigens; and the third of the EBV antigen-encoding mRNA constructs comprises, consists of, or is the segment that encodes the third of the recombinant T cell module antigens; the at least three of the recombinant T cell module antigens comprises: (a) at least four of the EBV LMP1 protein fragments, (b) at least four of the EBV LMP2 protein fragments, (c) at least three of the EBNA1 protein fragments, and (d) at least seven of the EBNA3A protein fragments; the first of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 2; the second of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 3; the third of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 4; the fourth of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 5; the first of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 8; the second of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 9; the third of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 10; the fourth of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 11; the first of the EBNA1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 13; the second of the EBNA1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 14; the third of the EBNA1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 15; the first of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 17; the second of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 18; the third of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 19; the fourth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 20; the fifth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: Attorney Docket No: 70488WO01 21; the sixth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 22; and the seventh of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 23; at least two of, or at least three of, the first, second, third, and fourth of the EBV LMP1 protein fragments are not adjacent to each other on the at least three recombinant T cell module antigens; at least two of, or at least three of, the first, second, third, and fourth of the EBV LMP2 protein fragments are not adjacent to each other on the at least three recombinant T cell module antigens; at least two of the first, second, and third of the EBNA1 protein fragments are not adjacent to each other on the at least three recombinant T cell module antigens; and at least two of, at least three of, at least four of, at least five of, or at least six of the first, second, third, fourth, fifth, sixth, and seventh of the EBNA3A protein fragments are not adjacent to each other on the at least three recombinant T cell module antigens. In some embodiments therein, the first, second, third, and fourth of the EBV LMP1 protein fragments are not adjacent to each other on the at least three recombinant T cell module antigens; the first, second, third, and fourth of the EBV LMP2 protein fragments are not adjacent to each other on the at least three recombinant T cell module antigens; the first, second, and third of the EBNA1 protein fragments re not adjacent to each other on the at least three recombinant T cell module antigens; and the first, second, third, fourth, fifth, sixth, and seventh of the EBNA3A protein fragments are not adjacent to each other on the at least three recombinant T cell module antigens. In some embodiments therein, the at least three recombinant T cell module antigens further comprise a first of the ZEBRA protein fragments, which has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 25, and a second of the ZEBRA protein fragments, which has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO:26; the first of the recombinant T cell module antigens comprising, from N-terminus to C-terminus, the second of the EBNA1 protein fragments, the seventh of the EBNA3A protein fragments, the fourth of the EBV LMP2 protein fragments, the second of the ZEBRA protein fragments, the first of the EBNA3A protein fragments, the second of the EBV LMP1 protein fragments, and the sixth of the EBNA3A protein fragments. In some embodiments therein, the segment that encodes the first of the recombinant T cell module antigens comprises, consists of, or is a sequence having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 34 or SEQ ID NO: 122. In some embodiments, the second of the recombinant T cell module antigens comprises, from N- terminus to C-terminus, the third of the EBV LMP2 protein fragments, the third of the EBV LMP1 protein fragments, the fifth of the EBNA3A protein fragments, the second of the EBV LMP2 protein fragments, the fourth of the EBV LMP1 protein fragments, the fourth of the EBNA3A protein fragments, and the first of the EBV LMP1 protein fragments. In some embodiments, the segment that encodes the second of the recombinant T cell module antigens comprises, consists of, or is a Attorney Docket No: 70488WO01 sequence having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 36 or SEQ ID NO: 123. In some embodiments, the third of the recombinant T cell module antigens comprising, from N- terminus to C-terminus, the first of the EBNA1 protein fragments, the third of the EBNA3A protein fragments, the first of the EBV LMP2 protein fragments, the second of the EBNA3A protein fragments, the first of the ZEBRA protein fragments, and the third of the EBNA1 protein fragments. In some embodiments, the segment that encodes the third of the recombinant T cell module antigens comprising a sequence having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 38 or SEQ ID NO: 124. Accordingly, in some embodiments, the first of the recombinant T cell module antigens has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 33; the second of the recombinant T cell module antigens has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 35; and the third of the recombinant T cell module antigens has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 37. In some embodiments therein, the pharmaceutical composition comprises, consists of, or is at least seven of the EBV antigen-encoding mRNA constructs; the fourth of the EBV antigen-encoding mRNA constructs comprising the segment that encodes the EBV gp42 antigen; the fifth of the EBV antigen-encoding mRNA constructs comprising the segment that encodes the EBV gH antigen; the sixth of the EBV antigen-encoding mRNA constructs comprising the segment that encodes the EBV gL antigen; and the seventh of the EBV antigen-encoding mRNA constructs comprising the segment that encodes the EBV gp220 antigen. Accordingly, in some embodiments, they will have one, two, three, or each of (i), (ii), (iii), and (iv) which follow: (i) the EBV gp42 antigen comprising an EBV gp42 protein or an EBV gp42 protein fragment, the EBV gp42 protein comprising a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 43; (ii) the EBV gH antigen comprising an EBV gH protein or an EBV gH protein fragment; the EBV gH protein comprising a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 39; (iii) the EBV gL antigen comprising an EBV gL protein or an EBV gL protein fragment, the EBV gL protein comprising a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 41; and / or (iv) the EBV gp220 antigen comprising an EBV gp220 protein or an EBV gp220 protein fragment, the EBV gp220 protein comprising a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 45. In some embodiments, the EBV gp42 antigen comprises, consists of, or is the EBV gp42 protein, the at least two EBV antigen-encoding mRNA constructs thereby comprising a segment that encodes the EBV gp42 protein; the EBV gH antigen comprises, consists of, or is the EBV gH protein, the at least two EBV antigen-encoding mRNA constructs thereby comprising a segment that encodes the EBV gH protein; the EBV gL antigen comprises, consists of, or is the EBV gL protein, the at least two Attorney Docket No: 70488WO01 EBV antigen-encoding mRNA constructs thereby comprising a segment that encodes the EBV gL protein; and / or the EBV gp220 antigen comprises, consists of, or is the EBV gp220 protein, the at least two EBV antigen-encoding mRNA constructs thereby comprising a segment that encodes the EBV gp220 protein. EBV ANTIGEN-ENCODING MRNA CONSTRUCTS COMPRISING A SEGMENT THAT ENCODES A B CELL MODULE ANTIGEN In some embodiments, they will have one, two, three, or each of (i), (ii), (iii), and (iv) which follow: (i) the EBV gp42 antigen comprising, consisting of, or being an EBV gp42 protein or an EBV gp42 protein fragment, the EBV gp42 protein comprising, consisting of, or being a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 43; (ii) the EBV gH antigen comprising, consisting of, or being an EBV gH protein or an EBV gH protein fragment; the EBV gH protein comprising, consisting of, or being a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 39; (iii) the EBV gL antigen comprising, consisting of, or being an EBV gL protein or an EBV gL protein fragment, the EBV gL protein comprising, consisting of, or being a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 41; and / or (iv) the EBV gp220 antigen comprising, consisting of, or being an EBV gp220 protein or an EBV gp220 protein fragment, the EBV gp220 protein comprising, consisting of, or being a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 45. In some embodiments, the EBV gp42 antigen comprises, consists of, or is the EBV gp42 protein, the at least two EBV antigen-encoding mRNA constructs thereby comprising a segment that encodes the EBV gp42 protein; the EBV gH antigen comprises, consists of, or is the EBV gH protein, the at least two EBV antigen-encoding mRNA constructs thereby comprising a segment that encodes the EBV gH protein; the EBV gL antigen comprises, consists of, or is the EBV gL protein, the at least two EBV antigen-encoding mRNA constructs thereby comprising a segment that encodes the EBV gL protein; and / or the EBV gp220 antigen comprises, consists of, or is the EBV gp220 protein, the at least two EBV antigen-encoding mRNA constructs thereby comprising a segment that encodes the EBV gp220 protein. Accordingly, in some embodiments, the segment that encodes the EBV gH protein comprises, consists of, or is a sequence having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 40 or SEQ ID NO: 125; the segment that encodes the EBV gL protein comprises, consists of, or is a sequence having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 42 or SEQ ID NO: 126; the segment that encodes the EBV gp42 protein comprises, consists of, or is a sequence having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 44 or SEQ ID NO: 127; and / or the segment that encodes the EBV gp220 protein comprises, consists of, or is a sequence having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 46 or SEQ ID NO: 128. Attorney Docket No: 70488WO01 These B cell module constructs can be combined with the T cell module constructs described above, including the FL, 2-split, and 3-split designs. EBV ANTIGEN-ENCODING MRNA CONSTRUCTS COMPRISING A SEGMENT THAT ENCODES A B CELL MODULE ANTIGEN WITHOUT NECESSARILY COMPRISING A SEGMENT THAT ENCODES A T CELL MODULE ANTIGEN In another aspect, a pharmaceutical composition comprising lipids and at least two EBV antigen- encoding mRNA constructs is provided; the lipids encapsulate the at least two EBV antigen-encoding mRNA constructs, thereby forming LNPs; each of the EBV antigen-encoding mRNA constructs comprises a segment that encodes an EBV antigen; the EBV antigens comprises an EBV B cell module antigen, but not necessarily an EBV T cell module antigen (i.e. the EBV antigens comprise an EBV B cell module antigen and the EBV antigens lack an EBV T cell module antigen); the EBV B cell module antigen comprises an EBV gp220 antigen, an EBV gH antigen, an EBV gL antigen, and an EBV gp42 antigen. In some embodiments within this aspect, each of the EBV antigen-encoding mRNA constructs is a conventional (i.e. non-replicating or trans-amplifying) mRNA construct (i.e. each of the EBV antigen-encoding mRNA constructs comprises the segment that encodes the B cell module antigen and does not comprise (i.e. lacks) a segment that encodes an RNA-dependent RNA polymerase, and / or each of the EBV antigen-encoding mRNA constructs comprises the segment that encodes the B cell module antigen and does not comprise (i.e. lacks) a segment that encodes a replicase). In other embodiments within this aspect, each of the EBV antigen-encoding mRNA constructs comprises a segment that encodes the B cell module antigen and a segment that encodes an RNA- dependent RNA polymerase and each of the at least two EBV antigen-encoding mRNA constructs is a self-replicating mRNA construct. The RNA-dependent RNA polymerase can in certain embodiments be from, for example, a Sindbis virus, a Semliki forest virus, an eastern equine encephalitis virus (EEEV), or a Venezuelan equine encephalitis virus (VEEV). Mutant or wild-type virus sequences can be used e.g. the attenuated TC83 mutant of VEEV has been used for self- replicating RNA. Thus, in certain embodiments, the EBV antigen-encoding mRNA construct comprises the segment that encodes the RNA-dependent RNA polymerase and the segment that encodes the EBV B cell module antigen. In certain embodiments, the EBV antigen-encoding mRNA construct comprises the segment that encodes the RNA-dependent RNA polymerase and the segment that encodes the EBV B cell module antigen; the segment that encodes the RNA- dependent RNA polymerase is 5’ of the segment that encodes the EBV B cell module antigen. In some embodiments, an internal ribosomal entry site sits between the segment that encodes the RNA-dependent RNA polymerase and the segment that encodes the EBV B cell module antigen. In some embodiments at least one, or each, of the EBV antigen-encoding mRNA constructs comprises the segment that encodes the B cell module antigen and a segment that encodes replicase and the at least one, or each, of the at least two EBV antigen-encoding mRNA constructs is a self-replicating mRNA construct. In some embodiments at least one, or each, of the EBV antigen- Attorney Docket No: 70488WO01 encoding mRNA constructs comprises the segment that encodes the EBV B cell module antigen and the segment that encodes replicase and the at least one, or each, of the at least two EBV antigen- encoding mRNA constructs being a self-replicating mRNA construct; and the replicase comprises alphavirus proteins nsP1, nsP2, nsP3 and nsP4. In some embodiments, alphavirus nsP4 comprises an RNA-dependent RNA polymerase. Such alphavirus-based self-replicating RNA can use a replicase from, for example, a Sindbis virus, a Semliki forest virus, an eastern equine encephalitis virus (EEEV), or a Venezuelan equine encephalitis virus (VEEV). Mutant or wild-type virus sequences can be used e.g. the attenuated TC83 mutant of VEEV has been used for self-replicating RNA. Thus, in certain embodiments, the EBV antigen-encoding mRNA construct comprises the segment that encodes the replicase and the segment that encodes the EBV B cell module antigen. In certain embodiments, the EBV antigen-encoding mRNA construct comprises the segment that encodes the replicase and the segment that encodes the EBV antigen; the segment that encodes the replicase is 5’ of the segment that encodes the EBV antigen. In some embodiments, an internal ribosomal entry site sits between the segment that encodes the replicase and the segment that encodes the EBV antigen. HLI SEQUENCES Fusing antigens to the major histocompatibility complex (MHC) class II–associated invariant chain (li) has been reported to enhance antigen-specific T cell responses. See, e.g., Capone et al., Mol Ther.2014 May; 22(5): 1039–1047. It is further known that the immune response against an antigen is increased when a fusion of invariant chain and said antigen is used for vaccination (see WO2007 / 062656, which is incorporated by reference herein), i.e. the invariant chain enhances the immunogenicity of the antigen, which was expressed after delivery by an adenovirus. Thus, In some embodiments, the EBV antigens comprises a human invariant chain (hli) sequence. In some embodiments, the EBV antigens comprise an N-terminal methionine residue. In some embodiments, the EBV antigens comprise an N-terminal signal sequence. In some embodiments, the EBV antigens comprise an hli sequence. In other embodiments, the EBV antigens comprise an N-terminal methionine residue. In some embodiments, the hli sequence is located at the N-terminus of the EBV antigens. In other embodiments, the hli sequence is located at the C-terminus of the EBV antigens. In additional embodiments, the EBV antigen comprises an N- terminal methionine residue. In other embodiments, the EBV antigen protein an N-terminal signal sequence. In some embodiments, the polyvalent EBV antigen protein does not contain junctional neo- epitopes that map to human (i.e. self) proteins. An immunogenic junctional neo-epitope is an epitope that elicits an immune response to the junction of two heterologous protein sequences, wherein the epitope is not present in either of the heterologous protein sequences themselves. T cell responses to junctional neo-epitopes can be identified using methods known in the art, for example immunological assays using peptide pools covering all junctions to be used. Attorney Docket No: 70488WO01 ADDITIONAL AND OPTIONAL FEATURES OF EBV ANTIGEN-ENCODING MRNA (AND OTHER MRNA SUCH AS REPLICASE-ENCODING MRNA) In some embodiments, each of the EBV antigen-encoding mRNA constructs further comprises a 5’ untranslated region (UTR), a 3’ UTR, and a 3’ poly(adenosine monophosphate) (poly(A)) tail; the 5’ UTR being 5’ of the segment that encodes the EBV antigen; the 3’ UTR being 3’ of the segment that encodes the EBV antigen; and the 3’ poly(A) tail being 3’ of the 3’ UTR. In some embodiments, the EBV antigen-encoding mRNA constructs comprises a modified nucleotide. In some embodiments, each of the EBV antigen-encoding mRNA constructs and non-EBV antigen-encoding mRNA constructs (e.g., trans-amplifying mRNA constructs) further comprises a 5’ untranslated region (UTR), a 3’ UTR, and a 3’ poly(adenosine monophosphate) (poly(A)) tail; the 5’ UTR being 5’ of the segment that encodes the EBV antigen; the 3’ UTR being 3’ of the segment that encodes the EBV antigen; and the 3’ poly(A) tail being 3’ of the 3’ UTR. In some embodiments, each of the EBV antigen-encoding mRNA constructs and non-EBV antigen-encoding mRNA constructs (e.g., trans- amplifying mRNA constructs) comprises a modified nucleotide. 5’ CAP In some embodiments, the RNA further comprises a 5’ cap structure. In some embodiments, the 5’ cap structure comprises: a 5’ cap nucleoside (i.e. a 7-methylguanosine or a modified 7- methylguanosine (including an anti-reverse capping agent) such as 7-methyl, 3’-O-methylguanosine or a 7-methyl, 2’-O-methylguanosine), a 5’ first ribonucleoside, an optional 5’ second ribonucleoside, an optional monophosphate, and an optional tri-phosphate bridge. In some embodiments, the 5’ cap nucleoside comprises, consists of, has, or is a 7-methylguanosine or a 7-methyl, 3’-O- methylguanosine. In some embodiments, the 5’ cap nucleoside is linked directly or indirectly 5’-to-5’ to the 5’ first ribonucleoside. In some embodiments, the 5’ cap nucleoside is linked 5’-to-5’ to the 5’ first ribonucleoside by the triphosphate bridge. In some embodiments, the 5’ first ribonucleoside comprises a 2’-methylated ribose (2’-O-Me) (i.e. a cap-1 or cap-2). In some embodiments, the 5’ second ribonucleoside is bound to the 3’ end of the 5’ first ribonucleoside by the monophosphate (i.e. a 3’ to 5’ nucleotide binding). In some embodiments, the 5’ second ribonucleoside comprises a 2’- methylated ribose (2’-O-Me) (i.e. as in a cap-2). In some embodiments, the 5’ first ribonucleoside comprises a 2’-methylated ribose (2’-O-Me) and the 5’ second ribonucleoside comprises a 2’- methylated ribose (2’-O-Me) (i.e. a cap-2). A 5’ cap nucleoside comprises, consists of, has, or is a guanosine or modified guanosine connected to the RNA via a 5’ to 5’ triphosphate linkage by mRNA guanylyltransferase, and wherein the guanine of said guanosine or modified guanosine is methylated at its 7 position. In this context and in some embodiments, a 5’ to 5’ triphosphate linkage occurs when the 5’ end of the ribose of said guanosine or modified guanosine is linked to the 5’ end of the ribose of the RNA via the triphosphate by mRNA guanylyltransferase. In some embodiments, thereafter, the guanine of said guanosine or modified guanosine is methylated at its 7 position by (guanine-N7-)-methyltransferase. In some embodiments, the addition of the 7-methylguanosine 5’-to- Attorney Docket No: 70488WO01 5’ to the 5’ first ribonucleoside occurs at once, without addition of the guanosine or modified guanosine and further methylation thereof to obtain 7-methylguanosine (i.e. CLEANCAP®). In some embodiments, the modified 7-methylguanosine is a 7-methyl (3’-O-methyl), guanosine. In some embodiments, the modified guanosine is a 3’-O-methylguanosine (i.e. which is then methylated at the 7 position by guanine-N7-)-methyltransferase). In some embodiments, the addition of the 7-methylguanosine or modified 7-methylguanoisine 5’- to-5’ to the 5’ first ribonucleoside and the addition of the 5’ first ribonucleoside comprising a 2’- methlyated ribose or 5’ second ribonucleoside comprising a 2’-methylated ribose occurs at once (i.e. CLEANCAP®). In some embodiments, the cap structure is preformed (i.e. as cap-1, cap-2, or cap-0, with or without the addition of the 7 methyl-group on the 5’ guanosine / 7-methylguanosine) and added to the recombinant RNA molecule (i.e. by ligation). In some embodiments, the preformed cap structure is added with a 5’-AG-3’ initiating sequence as described in the CLEANCAP® AG product insert (Trilink catalog number N-7113), which is incorporated by reference). Accordingly, in some embodiments, the 5’ cap is added non-enzymatically through the use of the following reagent: reagent as BIOTECHNOLOGIES). In other embodiments, a cap may be added resulting in the 5’ end of the RNA having the structure m7(3'OMeG)(5')ppp(5')(2'OMeA)pG. This cap may be added non-enzymatically through the use of the following reagent:

[0002] Attorney Docket No: 70488WO01 BIOTECHNOLOGIES). Without further methylation, a 7-methylguanosine bound 5’-to-5’ to the 5’ first ribonucleoside is known as cap-0 and is expressed as 5’(m7Gp)(ppN)[pN]N, wherein the former “N” indicates the first (5’) nucleobase of the RNA, the “pN” indicates a further nucleotide in the RNA, and the addition of “[..]N” in “[pN]N” indicates the repeating polymeric structure of the RNA and thereby collectively each sequentially adjacent nucleotide in the RNA. An additional oxygen-linked methylation by a 2’-0-methyltransferase to the 2’ carbon of the ribose of the nucleoside of the RNA immediately adjacent to said 7-methylguanosine (i.e. the 5’ first ribonucleoside) results in a cap-1 structure, which is expressed as 5’(m7Gp)(ppm2N)[pN]N, wherein the addition of the “m2” indicates the oxygen-linked methylation of the 2’ carbon of the ribose of the nucleoside immediately adjacent (via the triphosphate linkage) to said 7-methylguanosine. And further still, an additional methylation to the 5’ second ribonucleoside (i.e. the next (3’) nucleoside immediately adjacent to the 5’ first nucleoside methylated in cap-1) results in a cap-2 structure, which is expressed as 5′(m7Gp)(ppm2N)(m2pN)[pN]n, wherein the addition of the latter “m2” indicates the methylation of the nucleotide immediately adjacent to the nucleotide methylated in cap-1. This cap-2 methylation is also to the 2’ carbon of the ribose of that immediately adjacent nucleotide (i.e.2’-O- Me). In some embodiments, the 5’ cap is a cap-0, a cap-1, or a cap-2. In some embodiments, the 5’ cap is a cap-0. In some embodiments, the 5’ cap is a cap-1. In some embodiments, the 5’ cap is a cap-2. In some embodiments, the 5’ first ribonucleoside or the 5’ second ribonucleoside is exogenously added to the RNA. In some embodiments, the 5’ first ribonucleoside or the 5’ second ribonucleoside is native to the RNA (i.e. if the native sequence is 5’-UUAAT-3’, then the addition of the m7Gp would result in 5’- m7Gp(ppUUAAT-3’ when there is a triphosphate bride; if the native sequence is the same, then the cap-1 structure would result in 5-′(m7Gp)(ppm2U)UAAT-3’ and the cap-2 structure being 5-′(m7Gp)(ppm2U)(m2U)AAT-3’). Attorney Docket No: 70488WO01 Kits providing all of the materials for a 5’ cap, whether it is cap-1 or cap-2, and supplemental kits adding cap-1 and cap-2 capacity to a cap-0 kit can be used. The methods for 5’ capping can be carried out according to the manufacturer’s instructions. UTR In some embodiments, the 5’ UTR comprises, consists of, or is a sequence that has at least or no more than 1, 2, 3, 4, 5, or 6 additions, deletions, or substitutions to SEQ ID NO: 48, SEQ ID NO: 50, or SEQ ID NO: 52. In some embodiments, the 5’ UTR comprises, consists of, or is a sequence that has 0, 1, 2, 3, 4, 5, or 6 additions, deletions, or substitutions to SEQ ID NO: 48, SEQ ID NO: 50, or SEQ ID NO: 52. In some embodiments, the 3’ UTR comprises, consists of, or is a sequence that has at least or no more than 1, 2, 3, 4, 5, or 6 additions, deletions, or substitutions to SEQ ID NO: 49, SEQ ID NO: 51, or SEQ ID NO: 53. In some embodiments, the 3’ UTR comprises, consists of, or is a sequence that has 0, 1, 2, 3, 4, 5, or 6 additions, deletions, or substitutions to SEQ ID NO: 49, SEQ ID NO: 51, or SEQ ID NO: 53. In some embodiments, the 5’ UTR comprises, consists of, or is a sequence that: (1) has at least 90.0%, 91.0%, 92.0%, 93.0%, 94.0%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98.1%, 98.2%, 98.3%, 98.4%, 98.5%, 98.6%, 98.7%, 98.8%, 98.9%, 99.0%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, or 100% identity to SEQ ID NO: 48, SEQ ID NO: 50, or SEQ ID NO: 52; (2) has 0, 1, 2, 3, 4, 5, or 6 additions, deletions, or substitutions to SEQ ID NO: 48, SEQ ID NO: 50, or SEQ ID NO: 52; or (3) has both (1) and (2). In some embodiments, the 3’ UTR comprises, consists of, or is a sequence that: (1) has at least 90.0%, 91.0%, 92.0%, 93.0%, 94.0%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98.1%, 98.2%, 98.3%, 98.4%, 98.5%, 98.6%, 98.7%, 98.8%, 98.9%, 99.0%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, or 100% identity to SEQ ID NO: 49, SEQ ID NO: 51, or SEQ ID NO: 53; (2) has 0, 1, 2, 3, 4, 5, or 6 additions, deletions, or substitutions to SEQ ID NO: 49, SEQ ID NO: 51, or SEQ ID NO: 53; or (3) has both (1) and (2). In some embodiments, the 5’ UTR comprises, consists of, or is a sequence that: (1) has at least 90.0%, 91.0%, 92.0%, 93.0%, 94.0%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98.1%, 98.2%, 98.3%, 98.4%, 98.5%, 98.6%, 98.7%, 98.8%, 98.9%, 99.0%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, or 100% identity to SEQ ID NO: 48; (2) has 0, 1, 2, 3, 4, 5, or 6 additions, deletions, or substitutions to SEQ ID NO: 48; or (3) has both (1) and (2); and the 3’ UTR comprises, consists of, or is a sequence that: (4) has at least 90.0%, 91.0%, 92.0%, 93.0%, 94.0%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98.1%, 98.2%, 98.3%, 98.4%, 98.5%, 98.6%, 98.7%, 98.8%, 98.9%, 99.0%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, or 100% identity to SEQ ID NO: 49; (5) has 0, 1, 2, 3, 4, 5, or 6 additions, deletions, or substitutions to SEQ ID NO: 49; or (6) has both (4) and (5). In some embodiments, the 5’ UTR comprises, consists of, or is a sequence that: (1) has at least 90.0%, 91.0%, 92.0%, 93.0%, 94.0%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98.1%, Attorney Docket No: 70488WO01 98.2%, 98.3%, 98.4%, 98.5%, 98.6%, 98.7%, 98.8%, 98.9%, 99.0%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, or 100% identity to SEQ ID NO: 50; (2) has 0, 1, 2, 3, 4, 5, or 6 additions, deletions, or substitutions to SEQ ID NO: 50; or (3) has both (1) and (2); and the 3’ UTR comprises, consists of, or is a sequence that: (4) has at least 90.0%, 91.0%, 92.0%, 93.0%, 94.0%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98.1%, 98.2%, 98.3%, 98.4%, 98.5%, 98.6%, 98.7%, 98.8%, 98.9%, 99.0%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, or 100% identity to SEQ ID NO: 51; (5) has 0, 1, 2, 3, 4, 5, or 6 additions, deletions, or substitutions to SEQ ID NO: 51; or (6) has both (4) and (5). In some embodiments, the 5’ UTR comprises, consists of, or is a sequence that: (1) has at least 90.0%, 91.0%, 92.0%, 93.0%, 94.0%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98.1%, 98.2%, 98.3%, 98.4%, 98.5%, 98.6%, 98.7%, 98.8%, 98.9%, 99.0%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, or 100% identity to SEQ ID NO: 52; (2) has 0, 1, 2, 3, 4, 5, or 6 additions, deletions, or substitutions to SEQ ID NO: 52; or (3) has both (1) and (2); and the 3’ UTR comprises, consists of, or is a sequence that: (4) has at least 90.0%, 91.0%, 92.0%, 93.0%, 94.0%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98.1%, 98.2%, 98.3%, 98.4%, 98.5%, 98.6%, 98.7%, 98.8%, 98.9%, 99.0%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, or 100% identity to SEQ ID NO: 53; (5) has 0, 1, 2, 3, 4, 5, or 6 additions, deletions, or substitutions to SEQ ID NO: 53; or (6) has both (4) and (5). 3’ POLY(ADENOSINE MONOPHOSPHATE) TAILS In some embodiments, the poly(A) tail consists of adenosine monophosphate residues (i.e. thereby generating a length of exclusively consecutive monophosphate residues). In some embodiments, the RNA comprises a 3’ segmented poly(A) tail comprising, consisting of, or being a first segment of consecutive adenosine monophosphate residues, a spacer, and a second segment of consecutive adenosine monophosphate residues. In some embodiments, the 3’ segmented poly(A) tail is ordered from 5’ to 3’ as the first segment of consecutive adenosine monophosphate residues, the spacer, and the second segment of consecutive adenosine monophosphate residues. In some embodiments, the 3’ segmented poly(A) tail is 3’ from the 3’ UTR. In some embodiments, the 3’ segmented poly(A)) tail at the 3’ end of the recombinant RNA. In some embodiments, the poly(A) tail comprises, consists of, consists essentially of, has, or is from 50 to: 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100; from 52 to: 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97 or; from 54 to: 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, or 94; from 56 to: 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, or 92; from 58 to: 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, or 90; from 62 to: 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, or 88; from 64 to: 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, or 86; from 66 to: 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, or 84; from 68 to: 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, or 82; or from 70 to: 72, 73, 74, 75, 76, 77, 78, 79, or 80 adenosine monophosphate residues. Attorney Docket No: 70488WO01 In some embodiments, the RNA comprises a 3’ segmented poly(A) tail comprising a first segment of consecutive adenosine monophosphate residues, a spacer, and a second segment of consecutive adenosine monophosphate residues. In some embodiments, the first segment of consecutive adenosine monophosphate residues comprises, consists of, consists essentially of, has, or is from 20 to: 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, or 80; from 22 to: 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, or 74; from 24 to: 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, or 68; from 26 to: 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, or 62; or from 28 to: 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, or 56 consecutive adenosine monophosphate residues. In some embodiments, the second segment of consecutive adenosine monophosphate residues comprises, consists of, or is from 70 to 100 consecutive adenosine monophosphates. In some embodiments, the second segment of consecutive adenosine monophosphate residues comprises, consists of, or is from 30 to 50 consecutive adenosine monophosphates. In some embodiments, the second segment of consecutive adenosine monophosphate residues comprises, consists of, consists essentially of, has, or is from 20 to: 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, or 80; from 22 to: 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, or 74; from 24 to: 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, or 68; from 26 to: 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, or 62; or from 28 to: 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, or 56 consecutive adenosine monophosphate residues. In some embodiments, the poly(A) tail comprises or consists of the sequence of SEQ ID NO: 54. In some embodiments, the poly(A) tail comprises or consists of the sequence of SEQ ID NO: 55. In some embodiments, the poly(A) tail comprises or consists of the sequence of SEQ ID NO: 56. In some embodiments, the poly(A) tail comprises or consists of the sequence of SEQ ID NO: 57. 3-SPLIT DESIGNS WITH UTRs and POLY(A) TAILS In some embodiments with 3-split T cell module antigen constructs, the first of the EBV antigen- encoding mRNA constructs has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 74, 75, 76, 138, 139, or 140; the second of the EBV antigen-encoding mRNA constructs has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity Attorney Docket No: 70488WO01 to SEQ ID NO: 78, 79, 80, 141, 142, or 143; the third of the EBV antigen-encoding mRNA constructs has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 82, 83, 84, 144, 145, or 146. Regarding the B cell module antigen constructs with the 3-split designs, in some embodiments, the fourth of the EBV antigen-encoding mRNA constructs has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 66, 67, 68, 153, 154, or 155; the fifth of the EBV antigen-encoding mRNA constructs has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 58, 59, 60, 147, 148, or 149; the sixth of the EBV antigen-encoding mRNA constructs has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 62, 63, 64, 150, 151, or 152; and / or the seventh of the EBV antigen-encoding mRNA constructs has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 70, 71, 72, 156, 157, or 158. Note that some of SEQ ID NOs: 76, 80, 84, 68, 60, 64, 72, 140, 143, 146, 155, 149, 152, and 158 have representative poly(A) tails in them. While these poly(A) tails were used in many of the examples below, other poly(A) tails, such as those of SEQ ID NOs: 54-57 were also tested and were found to provide more than sufficient expression for vaccination purposes. Accordingly, the designs of poly(A) tails in the section above are readily appreciated as providing sufficient expression for vaccination purpose, and they can be used in the designs of SEQ ID NOs: 76, 80, 84, 68, 60, 64, 72, 140, 143, 146, 155, 149, 152, and 158 replacing the existing split poly(A) tails therein, which have 30 As, then “GCATATGACT”, then another 37 As. 2-SPLIT DESIGNS WITH UTRs and POLY(A) TAILS In some embodiments with 2-split T cell module antigen constructs, the first of the EBV antigen- encoding mRNA constructs has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 89, 90, 91, 132, 133, or 134; the second of the EBV antigen-encoding mRNA constructs has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 92, 93, 94, 135, 136, or 137. Regarding the B cell module antigen constructs with the 3-split designs, in some embodiments, the third of the EBV antigen-encoding mRNA constructs has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 66, 67, or 68, 153, 154, or 155; the fourth of the EBV antigen-encoding mRNA constructs has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 58, 59, 60, 147, 148, or 149; the fifth of the EBV antigen-encoding mRNA constructs has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 62, 63, 64, 150, 151, or 152; and / or the sixth of the EBV antigen- encoding mRNA constructs has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 70, 71, 72, 156, 157, or 158. Note that some of SEQ ID NOs: 91, 94, 68, 60, 64, 72, 134, 137, 155, 149, 152, and 158 have representative poly(A) tails in them. While these poly(A) tails were used in many of the examples below, other poly(A) tails, such as those of SEQ ID NOs: 54-57 were also tested and were found to Attorney Docket No: 70488WO01 provide more than sufficient expression for vaccination purposes. Accordingly, the designs of poly(A) tails in the section above are readily appreciated as providing sufficient expression for vaccination purpose, and they can be used in the designs of SEQ ID NOs: 91, 94, 68, 60, 64, 72, 134, 137, 155, 149, 152, and 158 replacing the existing poly(A) tails therein, which have 80 straight As or a split design of 30 As, then “GCATATGACT”, then another 37. MODIFIED NUCLEOTIDES In some embodiments, the EBV antigen-encoding mRNA constructs comprises a modified nucleotide. In some embodiments, each of the EBV antigen-encoding mRNA constructs and non- EBV antigen-encoding mRNA constructs (e.g., trans-amplifying mRNA constructs) comprises a modified nucleotide. In some embodiments, the modified nucleotides comprise: pseudouridine, N1- methylpseudouridine, N1-ethylpseudouridine, and any others listed in WO2023 / 242817, which is hereby incorporated by reference in its entirety. In some embodiments, the mRNA lacks uridine. Accordingly, in uridine’s place would be a uridine-substitutable modified nucleotide, such as the pseudouridine, N1-methylpseudouridine, or N1-ethylpseudouridine, each of which are preferred. Some would call this embodiments in which 100% of the uridines are substituted with pseudouridine, N1-methylpseudouridine, or N1-ethylpseudouridine. In some embodiments, the percentage of standard As substituted with A-substitutable modified nucleotide (e.g. those above) is at least: 0.1%, 0.5%, 0.8%, 1%, 2%, 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, or at least 99.9%, or 100%. In some embodiments, the percentage of standard As substituted with m6A may be 0.1-5%, in particular 0.5-2%, in particular 0.8-1.2%, such as about 1% (or 1%); in these embodiments the RNA may be circular RNA. Low substitution levels with m6A (e.g.1%) have been shown in inhibit innate immune activation. In some embodiments, the percentage of standard Cs substituted with cytosine- substitutable modified nucleotide (e.g. those above) is at least: 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, or at least 99.9%, or 100%. In some embodiments, the percentage of standard Gs substituted with G-substitutable modified nucleotide (e.g. those above) is at least: 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, or at least 99.9%, or 100%. In preferred embodiments, the percentage of standard Us that are substituted with a U-substitutable modified nucleotide (e.g. those above such as pseudouridine, N1-methylpseudouridine, and N1-ethylpseudouridine) is at least: 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, or at least 99.9%, or preferably 100%; more preferably with N1-methylpseudouridine (1mΨ), pseudouridine (Ψ), or N1- ethylpseudoduridine. In the alternative, with a SAM, the percentage of standardUs that are substituted with U-substitutable modified nucleotide (e.g. those above such as pseudouridine, N1- methylpseudouridine, and N1-ethylpseudouridine) can be from 15% to 75%, such as from 20% to 65%, from 25% to 50%, or any other values that are described in WO2023 / 031855, which is incorporated by reference. In the above embodiments with percentage of substitution, the Attorney Docket No: 70488WO01 percentage is the mole% of standard nucleotides substituted with modified nucleotides in the reaction mixture used to synthesize the EBV antigen-encoding (and non-EBV antigen encoding) mRNA constructs. In such embodiments, the RNA may comprise 1mΨ and / or Ψ, and neither standard U ribonucleotides nor other modified U ribonucleotides (i.e. there are no standard U nucleotides, nor modified U ribonucleotides other than 1mΨ and / or Ψ, in the RNA; i.e.100% U substitution). In particular embodiments, the RNA may comprise 1mΨ and / or Ψ, and neither standard U ribonucleotides nor other modified ribonucleotides (i.e. there are no standard U nucleotides, nor modified ribonucleotides of any type - A, C, G or U substitutable - other than 1mΨ and / or Ψ, in the RNA; i.e.100% U substitution with no other modified nucleotides being allowed). In other embodiments, the RNA may comprise Ψ, and neither standard U ribonucleotides nor other modified U ribonucleotides (i.e.100% U substitution with Ψ). In certain embodiments, the RNA may comprise Ψ, and neither standard U ribonucleotides nor other modified ribonucleotides (i.e.100% U substitution with Ψ with no other modified nucleotides being allowed). In other embodiments, the RNA comprises 1mΨ, and neither standard U ribonucleotides nor other modified U ribonucleotides (i.e.100% U substitution with 1mΨ). In yet other embodiments, the RNA comprises 1mΨ, and neither standard U ribonucleotides nor other modified ribonucleotides (i.e.100% U substitution with 1mΨ with no other modified nucleotides being allowed). In the embodiments in this paragraph, “[may] comprise[s]... and neither [X]...nor [Y]” may be used interchangeably with the wording “[may] comprise[s]... and does not comprise... [X] and / or [Y] ”. CODON OPTIMIZATION AND OTHER MEANS OF STABILIZING RNA AND REDUCING INNATE IMMUNE RESPONSES In additional embodiments, an EBV antigen-encoding (and non-EBV antigen-encoding) mRNA construct is codon-optimized. Codon optimization may provide an elevated GC content, relative to non-codon optimized RNA encoding the same protein(s). The GC content (the percentage of all ribonucleotides (or, defined alternatively, all “nitrogenous bases”) in the RNA which are G or C) of the RNA may be at least 10%, such as at least 20%, 30%, 35% or at least 40%, preferably at least 45%, 46%, 47%, 48%, 49%, or at least 50%. The GC content of the RNA may be 10-70%, such as 20- 65%, 30-65% or 35-65%, preferably 40-60%, 45-55%, 46-53%, 47-51%, or 48-50%. The GC content of the RNA may be 30-70%, such as 40-70%, 45-70%, 50-70%, or 55-70%. Codon optimization may provide an elevated C content relative to non-codon optimized RNA encoding the same protein(s). The percentage of C-optimizable codons in the RNA which have been substituted, as a result of codon optimization, for a codon with greater C content (while encoding the same amino acid) may be least 30%, such as at least 40%, 50%, 55% or at least 60%, preferably at least 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72% or at least 72%. The percentage of C-optimizable codons in the RNA which have been substituted, as a result of codon optimization, for a codon with greater C content (while encoding the same amino acid) may be 30-80%, such as 40-90%, 45-90%, 50-80%, 55-80% or 60-80%, preferably 65-75%, 66-75%, 67-75%, 68-75%, 69-75%, 70-74%, 71-74% or 72-74%. Attorney Docket No: 70488WO01 Optimizations providing at least some of the above-noted approaches are used in the examples as “Stabilization A” and “Stabilization B.” LIPID DELIVERY VEHICLES As noted above, in one aspect, a pharmaceutical composition is provided, the pharmaceutical composition comprising at least two EBV antigen-encoding messenger ribonucleic acid (mRNA) constructs and a lipid delivery vehicle. In particular, lipid delivery vehicle provide a means to protect a polynucleotide, e.g. through encapsulation, and deliver it to target cells for protein expression. In certain embodiments, the lipid delivery vehicle carrier is, or comprises, a cationic nano-emulsion (CNE). With a CNE, the EBV antigen-encoding mRNA constructs (and non-EBV antigen-encoding mRNA constructs) are complexed with a CNE particle, in particular comprising an oil core and a cationic lipid. The (usually strongly charged) cationic lipid can interact with the negatively charged mRNA construct, thereby anchoring the molecule to the emulsion particles. In some embodiments, a lipid delivery vehicle is a lipid inorganic nanoparticle (LION). In some embodiments, a lipid delivery vehicle is lipids, which when the lipids encapsulate the at least some of the EBV antigen-encoding mRNA constructs (and non-EBV antigen-encoding mRNA constructs), thereby forms a lipid nanoparticle (LNP). LIPIDS OF THE LIPID NANOPARTICLE As noted above, LNPs are listed as adjuvants, but in this regard, they also provide another function that is, in some embodiments, co-extensive with, and in some embodiments, independent of adjuvanticity. That is, RNA, by itself and unprotected, may be degraded by the subject’s RNAses. LNPs provide a means to protect the RNA by encapsulating or comprising within them an amount of the EBV antigen-encoding and non-immunogen encoding mRNA constructs of the overall composition or formulation. The LNP’s effects as being in some cases an adjuvant, in other cases a delivery vehicle, and in other cases both, can be cell-dependent. To illustrate but without being bound by a particular theory, the LNP may provide adjuvanticity to peripheral blood mononuclear cells in that the mRNA constructs activate the cells but the segments that encode an immunogen or segments encoding other molecules, such as RNA-dependent RNA polymerases for self-amplifying mRNA and trans-amplifying RNA, may not be translated therein, but the LNP may provide a delivery vehicle, but not adjuvanticity, to other somatic cell types, for arguendo example, skeletal muscle cells. In some embodiments, the pharmaceutically acceptable delivery vehicle comprises, consists of, or is lipids, which when they encapsulate that at least two EBV antigen-encoding mRNA constructs, thereby form a LNP. In this regard, the percentages below reference the mass% of mRNA constructs encapsulated or comprised within the LNPs compared to the mass of the respective mRNA construct in the composition. In some embodiments, the lipids encapsulate, comprise within them, consist within them, consist essentially within them, or have within them at least: 50 mass%, 75 mass%, 85.0 mass%, 86.0 mass%, 87.0 mass%, 88.0 mass%, 89.0 mass%, 90.0 mass%, 91.0 mass%, 92.0 mass%, 92.5 Attorney Docket No: 70488WO01 mass%, 93.0 mass%, 94.0 mass%, 95.0 mass%, 96.0 mass%, 97.0 mass%, 98.0 mass%, 98.5 mass%, 99.0 mass%, 99.5 mass%, 99.9 mass%, or 100 mass% of the EBV antigen-encoding mRNA constructs (and optionally the above-noted amounts of non-EBV antigen-encoding mRNA constructs). The lipids encapsulating at least the above-noted mass% or the above-noted ranges of mass% are determined, and such measures are defined, by the following encapsulation assay. Encapsulation Assay: The fluorescent dye (c.f. the kit) RIBOGREEN®was first described in WO1996 / 13552 and subsequently further characterized in Jones et al. “RNA Quantitation by Fluorescence-Based Solution Assay: RiboGreen Reagent Characterization,” Analytical Biochemistry, Vol.265, Issue 2, (1998) pp368-374. Obtain: QUANT-IT®RIBOGREEN®kit (ThermoFisher Cat. No. R11490); 96 well, flat bottom (chimney well), black, non-binding Microplate (Greiner, Cat. No.655900), DNA LoBind Tubes 1.5 mL and 2.0 mL (Eppendorf, Cat. Nos.022431021 and 022431048, respectively); 12-well reservoirs (VWR, Cat. No.89094-664); nuclease-free, non-DEPC treated water (ThermoFisher Cat. No. AM9937); and 20x concentrate, RNAse-free TE (tris-EDTA) Buffer (ThermoFisher Cat. No. T11493). TE-1 / 2 diluted standards Dilute the 20x TE buffer to 1x with reverse osmosis water (MilliQ water) and then filter through a 0.2 μm filter. From the 100 μg / mL standard in the QUANT-IT®RIBOGREEN®kit make 250 μL of the following standards in 1x TE buffer: 3 μg / mL, 1.5 μg / mL, 0.75 μg / mL, 0.38 μg / mL, and 0.19 μg / mL, and make a 0 μg / mL standard, which is TE buffer alone without any contribution of the standard from the QUANT-IT®RIBOGREEN®kit, thereby obtaining 3 μg / mL, 1.5 μg / mL, 0.75 μg / mL, 0.38 μg / mL, 0.19 μg / mL, and 0 μg / mL TE-diluted standards. Pipette 50 μL of each of 3 μg / mL, 1.5 μg / mL, 0.75 μg / mL, 0.38 μg / mL, 0.19 μg / mL, and 0 μg / mL TE-diluted standards in duplicate into individual wells in the microplate (i.e. two wells, each of 50 μL of 3 μg / mL TE-diluted standards; two wells, each of 50 μL of 1.5 μg / mL TE-diluted standards; two wells, each of 50 μL of 0.75 μg / mL TE-diluted standards; two wells, each of 50 μL of 0.38 μg / mL TE-diluted standards; two wells, each of 50 μL of 0.19 μg / mL TE-diluted standards; and two wells, each of 50 μL of 0 μg / mL TE-diluted standards). Next pipette of 50 μL of 1x TE buffer into each of the wells containing the TE-diluted standards, thereby obtaining TE-1 / 2 diluted standards. Triton X-100 TE-1 / 2 diluted standards Prepare a 1x Triton X-100 TE-buffer by obtaining 10% Triton X-100 (Teknova Cat. No. T1105), weighing 2 g of the 10% Triton X-100, diluting the 2 g of the 10% Triton X-100 into 198 mL of reverse osmosis water (MilliQ water) thereby obtaining a 1% Triton X-100 dilutant, and filtering through a 0.2 μm filter to obtain the 1x Triton X-100 TE-buffer. Upon the banning of Triton X-100 in a jurisdiction, please replace the 1x Triton X-100 TE-buffer with the following buffer in the encapsulation assay to test for the percent encapsulation in that jurisdiction that banned Triton X-100: in 99 mL of 1x TE buffer dilute 1 mL of 10% ECOSURF®SA9 solution (MilliporeSigma Cat. No. STS0007, CAS No. Attorney Docket No: 70488WO01 68937-66-6) thereby obtaining a 1x SA9 TE-buffer. Upon such banning, and the need to replace Triton X-100, please use the same volumes of 1x SA9 TE-buffer as the volume of 1x Triton X-100 TE-buffer below. Next, pipette 50 μL of each of 3 μg / mL, 1.5 μg / mL, 0.75 μg / mL, 0.38 μg / mL, 0.19 μg / mL, and 0 μg / mL TE-diluted standards in duplicate into individual wells in the microplate (i.e. two wells, each of 50 μL of 3 μg / mL TE-diluted standards; two wells, each of 50 μL of 1.5 μg / mL TE- diluted standards; two wells, each of 50 μL of 0.75 μg / mL TE-diluted standards; two wells, each of 50 μL of 0.38 μg / mL TE-diluted standards; two wells, each of 50 μL of 0.19 μg / mL TE-diluted standards; and two wells, each of 50 μL of 0 μg / mL TE-diluted standards). Into each of these wells containing these TE-diluted standards (as opposed to the TE-1 / 2 diluted standards obtained in the paragraph above), next pipette of 50 μL of 1x Triton X-100 TE buffer (or 50 μL of SA9 TE-buffer if the conditions above are met) thereby obtaining Triton X-100 TE-1 / 2 diluted standards (or SA9 TE-1 / 2 diluted standards). Samples Dilute the LNP-formulated samples, which require measurement of the encapsulation percentage, to a concentration of 1.0 – 1.5 μg of mRNA per mL of sample. Such dilution is based on the theoretical μg of mRNA per mL of sample (i.e. the total mass of mRNA put into the formulation) thereby obtaining a diluted sample. For up to twelve samples per 96 well plate, pipette 50 μL of each diluted sample in triplicate into individual wells in the microplate (i.e. having three wells, each with 50 μL of the diluted sample; having three wells, each with 50 μL of another diluted sample; etc.). Into each of these three wells containing these diluted sample, next pipette 50 μL of the 1x TE-buffer, thereby obtaining 1 / 2-diluted TE samples. Separately pipette 50 μL of each diluted sample in triplicate into individual wells in the microplate (i.e. having three wells, each with 50 μL of the diluted sample; having three wells, each with 50 μL of another diluted sample; etc.). Into each of these three wells containing these diluted sample, next pipette 50 μL of the 1x Triton X-100 TE buffer (or 50 μL of SA9 TE-buffer if the conditions above are met), thereby obtaining Triton X-100 TE-1 / 2 diluted samples (or SA9 TE-1 / 2 diluted samples). RIBOGREEN®reagent admixing At room temperate, add the 100 μL of RIBOGREEN®reagent to 19,900 μL of 1x TE-buffer thereby obtaining diluted RIBOGREEN®reagent. Into each of the wells containing the Triton X-100 TE-1 / 2 diluted samples, the 1 / 2-diluted TE samples, the Triton X-100 TE-1 / 2 diluted standards (or SA9 TE-1 / 2 diluted standards), and the TE-1 / 2 diluted standards, add 100 μL of the diluted RIBOGREEN®reagent. After this addition, place the plate on a shaker and mix the plate (and its contents) for 1 minute at 600 revolutions per minute. Check for air bubbles and eliminate any. Do not add the Triton X-100-containing reagents at a excess rate, which would cause air bubbles to form. Fluorescence reading Read the emission fluorescence at a wavelength of 528 nM, with an excitation wavelength of 485 nM and an auto cut off at a wavelength of 515 nm on a SpectraMax M5 plate reader (Molecular Attorney Docket No: 70488WO01 Devices Cat. No. USGS61758). Identify the sample or standard with the maximum fluorescence and compare this to the SpectraMax M5 plate reader’s maximum; if the maximum fluorescence is above the SpectraMax M5 plate reader’s maximum, reduce the instrument’s gain so that the maximum fluorescence is below the maximal detectable fluorescence of the plate reader (or reduce the excitation and emission time if the instrument’s gain cannot be further adjusted). Calculate the background-adjusted fluorescences and standard curves Subtract the mean fluorescence of the two wells containing the 0 μg / mL TE-1 / 2 diluted standards from the mean fluorescences of the two wells containing each of the TE-1 / 2 diluted standards and separately from the mean fluorescences of the three wells containing each of the 1 / 2-diluted TE samples, thereby obtaining background-adjusted mean fluorescences for each of the TE-1 / 2 diluted standards and background-adjusted mean fluorescences for each of the TE-1 / 2 diluted samples respectively. Perform a linear standard curve fit of each of the background-adjusted mean fluorescences of the TE-1 / 2 diluted standards (y-axis) versus the μg / mL value of the respective standard (3 μg / mL, 1.5 μg / mL, 0.75 μg / mL, 0.38 μg / mL, 0.19 μg / mL, and 0 μg / mL), thereby obtaining a TE-standard curve. Subtract the mean fluorescence of the two wells containing the 0 μg / mL Triton X-100 TE-1 / 2 diluted standards from the mean fluorescences of the two wells containing each of the Triton X-100 TE-1 / 2 diluted standards and separately from the mean fluorescences of the three wells containing each of the Triton X-100 TE-1 / 2 diluted samples thereby obtaining background-adjusted mean fluorescences for each of the Triton X-100 TE-1 / 2 diluted standards and background-adjusted mean fluorescences for each of the Triton X-100 TE-1 / 2 diluted samples respectively. Perform a linear standard curve fit of each of the background-adjusted mean fluorescences of the Triton X-100 TE-1 / 2 diluted standards (y-axis) versus the μg / mL value of the respective standard (3 μg / mL, 1.5 μg / mL, 0.75 μg / mL, 0.38 μg / mL, 0.19 μg / mL, and 0 μg / mL), thereby obtaining a Triton X-100 TE- standard curve. Determine the μg of RNA per mL of solution for each of the means of the TE-1 / 2 diluted samples and Triton X-100 TE-1 / 2 diluted samples. With the background-adjusted mean fluorescences of the Triton X-100 TE-1 / 2 diluted samples and with the Triton X-100 TE-standard curve, determine the μg per mL of each of the Triton X-100 TE-1 / 2 diluted samples, thereby obtaining a total μg of mRNA per mL of the sample for each of the samples. With the background-adjusted mean fluorescences of the TE-1 / 2 diluted samples and with the TE-standard curve, determine the μg per mL of each of the TE-1 / 2 diluted samples, thereby obtaining the μg of mRNA that is outside the LNP per mL of the sample for each of the samples. For each sample, subtract the μg of mRNA that is outside the LNP per mL of the sample from the total μg of mRNA per mL of the sample, thereby obtaining the μg of mRNA that is inside the LNP per mL of the sample for each sample. For each sample, divide the μg of mRNA that is inside the LNP per mL of the sample by the total μg of mRNA per mL of the sample, thereby obtaining a fraction of the mRNA that is inside the LNP for each sample. For each sample, convert the fraction of the mRNA Attorney Docket No: 70488WO01 that is inside the LNP for each sample to mass percent of encapsulation for the sample by multiplying the fraction of the mRNA that is inside the LNP for each sample by 100. LIPID NANOPARTICLES AND LIPIDS THEREOF CONTINUED In the diameters below, they are hydrodynamic diameters through the Stokes-Einstein relationship as measured by dynamic light scattering, and more specifically multiangle dynamic light scattering. In some embodiments, the LNPs have a diameter from 20nm to 220nm; from 35nm to 180nm; or from 60nm to 150nm. In some embodiments, LNP has a pKa of at least: 5.0, 5.1, 5.2, 5.3, 5.4, 5.5, 5.6, 5.7, 5.8, 5.9, 6.0, 6.1, 6.2, 6.3, 6.4, 6.5, 6.6, 6.7, 6.8, 6.9, 7.0, 7.1, 7.2, 7.3, 7.4, 7.5, 7.6, 7.7, 7.8, 7.9, 8.0, 8.1, 8.2, 8.3, 8.4, 8.5, 8.6, 8.7, 8.8, 8.9, 9.0, 9.1, 9.2, 9.3, 9.4, 9.5, 9.6, 9.7, 9.8, 9.9, or 10. In embodiments, the LNP has a pKa of no more than: 10, 9.9, 9.8, 9.7, 9.6, 9.5, 9.4, 9.3, 9.2, 9.1, 9.0, 8.9, 8.8, 8.7, 8.6, 8.5, 8.4, 8.3, 8.2, 8.1, 8.0, 7.9, 7.8, 7.7, 7.6, 7.5, 7.4, 7.3, 7.2, 7.1, 7.0, 6.9, 6.8, 6.7, 6.6, 6.5, 6.4, 6.3, 6.2, 6.1, 6.0, 5.9, 5.8, 5.7, 5.6, 5.5, 5.4, 5.3, 5.2, 5.1, or 5.0. In some embodiments, LNP has a pKa from 5.0 to: 7.0, 7.5, 8.0, 8.5, 9.0, 9.5, or 10; from 5.3 to: 6.8, 6.9, 7.0, 7.5, 8.0, 8.5, 9.0, or 9.5; from 5.6 to: 6.6, 6.7, 6.8, 6.9, 7.0, 7.5, 8.0, 8.5, or 9.0; from 5.9 to: 6.4, 6.5, 6.6, 6.7, 6.8, 6.9, 7.0, 7.5, 8.0, or 8.5 from: 6.2 to: 6.5, 6.6, 6.7, 6.8, 6.9, 7.0, 7.1, 7.2, 7.3, 7.4, or 7.5; from 6.3 to: 6.4, 6.5, 6.6, 6.7, 6.8, 6.9, or 7.0; from 6.4 to: 6.5, 6.6, 6.7, 6.8, or 6.9; or from 6.5 to: 6.6, 6.7, 6.8, or 6.9. In this regard, “the ionizable cationic lipid having a pKa” and “the LNP having a pKa” (a.k.a. “the lipids having a pKa” and “the lipids of LNP having a pKa”) are distinguishable. The pKa of the lipids of the LNP (a.k.a. “the pKa of the lipids” and “the pKa of the LNP”) is influenced by the selection of a ionizable cationic lipid and the mole percentages of the individual lipids in the overall formulation (I.e. the mole percentage of sterol, the mole percentage of a particular anionic lipid, neutral lipid, or zwitterionic lipid, the mole percentage of the particular ionizable cationic lipid) but to be clear the pKa of the lipids of the LNP excludes the influence of the EBV antigen-encoding mRNA constructs (and non-EBV antigen-encoding mRNA constructs). That is, the term “the pKa of the lipids of the LNP ” is defined to be measured from a liposome (i.e. an LNP that does not encapsulate or further comprise any ribonucleic acids) consisting of the lipids of the LNP (i.e. excluding the EBV antigen-encoding mRNA constructs (and non-EBV antigen-encoding mRNA constructs, i.e. a blank LNP wherein “blank” excludes EBV antigen-encoding mRNA constructs (and non-EBV antigen-encoding mRNA constructs) and any other molecules that would be delivered by the LNP). The “the pKa of the lipids of the LNP ” is measured by the following 6-(p-toluidino)-2-naphthalenesulfonic acid (TNS) assay. TNS Assay: TNS was suspended at 300 µM in DMSO. Following Zhang et al. “Ionization behavior of amino lipids for siRNA delivery: determination of ionization constants, SAR, and the impact of lipid pKa on cationic lipid-biomembrane interactions, LANGMUIR 27: 1907-1914 (2001), the LNPs were admixed with the 300 µM TNS in DMSO and buffered solutions containing 20 mM boric acid, 10 mM imidazole, 10 mM sodium acetate, 10 mM glycylglycine, and 25 mM NaCl and an individual pH from Attorney Docket No: 70488WO01 3 to 10, such that each final admixture had 75 µM of a ionizable cationic lipid and 6 µM of TNS and the series of admixtures provided at least one admixture within each of one pH unit within the range of pH from 3 to 10 (i.e. an admixture with said buffer having a pH within 3 (i.e. from 3.0 to 3.99), an admixture with said buffer having a pH within 4 (i.e. from 4.0 to 4.99), an admixture with said buffer having a pH within 5 (i.e. from 5.0 to 5.99), an admixture with said buffer having a pH within 6 (i.e. from 6.0 to 6.99), an admixture with said buffer having a pH within 7 (i.e. from 7.0 to 7.99), an admixture with said buffer having a pH within 8 (i.e. from 8.0 to 8.99), and an admixture with said buffer having a pH within 9 (i.e. from 9.0 to 9.99)). The fluorescence of said mixtures are then determined with an excitation wavelength of 321 nm and an emission wavelength of 445 nm. The blank-subtracted fluorescence of each admixture is then determined by subtracting a blank solution’s fluorescence from each admixture’s emission fluorescence. The relative fluorescence is then determined by dividing the blank-subtracted fluorescence of each admixture from the relative fluorescence of the admixture that has the highest relative fluorescence. The relative fluorescence’s for all the admixtures versus the pHs of the respective buffers were then regressed following the Henderson-Hasselbalch equation to obtain a line of best fit. The pKa of the lipids of the LNP was determined from the pH value that has a relative fluorescence of 0.5 on the line of best fit. Ionizable Cationic Lipid In some embodiments, the lipids of the LNP comprise: a ionizable cationic lipid, an optional sterol (e.g. cholesterol), an optional polymer-conjugated lipid, an optional anionic lipid, an optional neutral lipid, or an optional zwitterionic lipid (i.e. net neutral lipid). In some embodiments, the optional neutral lipid comprises, consists of, or is a zwitterionic lipid. In some embodiments, the polymer-conjugated lipid comprises, consists of, or is a poly(ethylene glycol)-conjugated lipid. In some embodiments, the lipids of the LNP comprise a lipid from WO2012 / 006376, WO2012 / 030901, WO2012 / 031046, WO2012 / 031043, WO2012 / 006378, WO2011 / 076807, WO2013 / 033563, WO2013 / 006825, WO2014 / 136086, WO2015 / 095340, WO2015 / 095346, WO2016 / 037053, WO2017 / 075531, WO2018 / 081480, WO2015 / 074085, WO2018 / 1703322, U.S. Patent Application Publication Nos.: 20220081392, 20220072155, 20220040285, 20210395188, 20210251898, 20210128488, 20210122703, 20210122702, 20210107861, 20200283372, 20200172472, 20200163878, 20200121809, 20200046838, 20190359556, 20190314524, 20190274968, 20190270697, 20190022247, 20180185516, 20170283367, 20170157268, 20170119904, 20160376224, 20160317676, or 20150376115, U.S. Application Nos.61 / 905,724 or 15 / 614,499, or U.S. Patent Nos.8,802,863, 9,458,090, 9,593,077, 9,567,296, 9,604,908, 9,643,916, 9,669,097, 9,670,487, 9,737,619, 9,738,593, 9,725,720, 9,796,977,10,106,490, 10,166,298, 10,221,127, 10,723,692, 11,040,112, 11,168,051, or 11,285,222 (including ionizable and PEG-lipids, as referred to therein). In some embodiments, the ionizable cationic lipid has a pKa of at least: 5.0, 5.1, 5.2, 5.3, 5.4, 5.5, 5.6, 5.7, 5.8, 5.9, 6.0, 6.1, 6.2, 6.3, 6.4, 6.5, 6.6, 6.7, 6.8, 6.9, 7.0, 7.1, 7.2, 7.3, 7.4, 7.5, 7.6, 7.7, 7.8, 7.9, 8.0, 8.1, 8.2, 8.3, 8.4, 8.5, 8.6, 8.7, 8.8, 8.9, 9.0, 9.1, 9.2, 9.3, 9.4, 9.5, 9.6, 9.7, 9.8, 9.9, or 10. In embodiments, the cationic-ionizable lipid has a pKa of no more than: 10, 9.9, 9.8, 9.7, 9.6, 9.5, Attorney Docket No: 70488WO01 9.4, 9.3, 9.2, 9.1, 9.0, 8.9, 8.8, 8.7, 8.6, 8.5, 8.4, 8.3, 8.2, 8.1, 8.0, 7.9, 7.8, 7.7, 7.6, 7.5, 7.4, 7.3, 7.2, 7.1, 7.0, 6.9, 6.8, 6.7, 6.6, 6.5, 6.4, 6.3, 6.2, 6.1, 6.0, 5.9, 5.8, 5.7, 5.6, 5.5, 5.4, 5.3, 5.2, 5.1, or 5.0. In some embodiments, the ionizable cationic lipid has a pKa from 5.0 to: 7.0, 7.5, 8.0, 8.5, 9.0, 9.5, or 10; from 5.3 to: 6.8, 6.9, 7.0, 7.5, 8.0, 8.5, 9.0, or 9.5; from 5.6 to: 6.6, 6.7, 6.8, 6.9, 7.0, 7.5, 8.0, 8.5, or 9.0; from 5.9 to: 6.4, 6.5, 6.6, 6.7, 6.8, 6.9, 7.0, 7.5, 8.0, or 8.5 from: 6.2 to: 6.5, 6.6, 6.7, 6.8, 6.9, 7.0, 7.1, 7.2, 7.3, 7.4, or 7.5; from 6.3 to: 6.4, 6.5, 6.6, 6.7, 6.8, 6.9, or 7.0; from 6.4 to: 6.5, 6.6, 6.7, 6.8, or 6.9; or from 6.5 to: 6.6, 6.7, 6.8, or 6.9. Within the meaning of “the ionizable cationic lipid having a pKa,” the pKa of the ionizable cationic lipid is determined by: 1) admixing 400 μL of 2 mM of the ionizable cationic lipid that are in 100 volume % ethanol and 800 μL of 0.3 mM of fluorescent probe fluorescent probe 6-(p-toluidino)-2-naphthalenesulfonic acid (TNS), which is in 90 volume % ethanol and 10 volume % methanol, thereby obtaining a lipid / TNS mixture; 2) admixing 7.5 μL of the lipid / TNS mixture and 242.5 μL of a first buffer comprising a sodium salt buffer comprising 20 mM sodium phosphate, 25 mM sodium citrate, 20 mM sodium acetate, and 150 mM sodium chloride, wherein the first buffer has a first pH from 4.44 to 4.52, thereby obtaining a first mixture, and dispensing 100 μL of the first mixture in a first well of a 96-well plate, which has a clear bottom; 3) admixing 7.5 μL of the lipid / TNS mixture and 242.5 μL of a second buffer comprising the sodium salt buffer, wherein the second buffer has a second pH of 5.27, thereby obtaining a second mixture, and dispensing 100 μL of the second mixture in a second well of the 96-well plate; 4) admixing 7.5 μL of the lipid / TNS mixture and 242.5 μL of a third buffer comprising the sodium salt buffer, wherein the third buffer has a third pH of from 6.15 to 6.21, thereby obtaining a third mixture, and dispensing 100 μL of the third mixture in a third well of the 96-well plate; 5) admixing 7.5 μL of the lipid / TNS mixture and 242.5 μL of a fourth buffer comprising the sodium salt buffer, wherein the fourth buffer has a fourth pH of 6.57, thereby obtaining a fourth mixture, and dispensing 100 μL of the fourth mixture in a fourth well of the 96-well plate; 6) admixing 7.5 μL of the lipid / TNS mixture and 242.5 μL of a fifth buffer comprising the sodium salt buffer, wherein the fifth buffer has a fifth pH of from 7.10 to 7.20, thereby obtaining a fifth mixture, and dispensing 100 μL of the fifth mixture in a fifth well of the 96-well plate; 7) admixing 7.5 μL of the lipid / TNS mixture and 242.5 μL of a sixth comprising the sodium salt buffer, wherein the sixth buffer has a sixth pH of from 7.72 to 7.80, thereby obtaining a sixth mixture, and dispensing 100 μL of the sixth mixture in a sixth well of the 96-well plate; 8) admixing 7.5 μL of the lipid / TNS mixture and 242.5 μL of a seventh buffer comprising the sodium salt buffer, wherein the seventh buffer has a seventh pH of from 8.27 to 8.33, thereby obtaining a seventh mixture, and dispensing 100 μL of the seventh mixture in a seventh well of the 96-well plate; 9) admixing 7.5 μL of the lipid / TNS mixture and 242.5 μL of an eighth buffer comprising the sodium salt buffer, wherein the eighth buffer has a eighth pH of from 10.47 to 11.12, thereby Attorney Docket No: 70488WO01 obtaining an eighth mixture, and dispensing 100 μL of the eighth mixture in an eighth well of the 96- well plate; 10) measuring the absolute fluorescence at a wavelength of 431 nm with an excitation wavelength of 322 nm and a cut-off below 420 nm of each of the first through eighth wells and an empty well of the 96-well plate; 11) subtracting the absolute fluorescence of the empty well from each of the absolute fluorescences of the first through the eighth wells, thereby obtaining a blank-subtracted fluorescence for each of the first through eighth mixtures; 12) normalizing each of the blank-subtracted fluorescences of the first through eighth mixtures to the blank-subtracted fluorescence of the first mixture, thereby obtaining a relative fluorescence for each of the first through eighth mixtures, the relative fluorescence of the first mixture being 1; 13) regressing by the Henderson-Hasselbalch equation, the first through eighth pHs versus the respective relative fluorescences of the first through eighth mixtures thereby obtaining a line of best fit; and 14) determining the pKa as the pH at which a relative fluorescence of 0.5 is obtained on the line of best fit. In some embodiments, the ionizable cationic lipid comprises an amine that can be a tertiary amine, which can become charged depending upon the pH of the solution that the ionizable cationic lipid is in when compared to the pKa of the ionizable cationic lipid. In some embodiments, at least half of the ionizable cationic lipids are neutrally charged when the pH of the solvent that the ionizable cationic lipids are in is above the pKa; and at least half of the ionizable cationic lipids are positively charged when the pH of the solvent that the ionizable cationic lipids are in is below the pKa. In this regard, in some embodiments, but without being limited to a particular theory, it is considered that the positive charge of the ionizable lipid is distributed at least partially onto the tertiary amine, and thereby at least a portion of the tertiary amines in the moles of ionizable cationic lipids are positively charged when the pH of the solvent that the ionizable cationic lipids are in is below the pKa. Since the tertiary amine can vary between neutrally and positively charged depending upon the pH of the solution relative to the pKa of the ionizable cationic lipid and since, without being bound a particular theory, the tertiary amine is an ionizable amine. “Cationic” in “ionizable cationic lipid” is understood to be a not permanently cationic, but rather when ionized, the molecule of the ionizable cationic lipid is positively charged (i.e. a cation) and when not ionized, the molecule of the ionizable cationic lipid is neutrally charged. That is, “ionizable cationic” is used in “ionizable cationic lipid” to distinguish from molecules that are ionizable but become negatively charged when ionized (i.e. an ionizable anionic molecule). The ionizable cationic lipid will be further described when the amine is tertiary and when the ionizable cationic lipid is neutrally charged, but such descriptions shall not limit the ionizable cationic lipid to lacking the ability to transition to having being positively charged. That is, the lipid being in a tertiary amine state and having a neutral charged is hereby described, without having to describe the Attorney Docket No: 70488WO01 ionizable cationic lipid when the tertiary amine becomes charged. In some embodiments, the ionizable cationic lipid is one of the generic formulae or specifically named cationic lipid described in WO2023 / 242817, which is hereby incorporated by reference in its entirety. In some embodiments, the ionizable cationic lipid is: In some embodiments, the cationic lipid has the structure of lipid RV28, RV31, RV33, RV37, RV39 RV42, RV44, RV73, RV75, RV81, RV84, RV85, RV86, RV88, RV91, RV92, RV93, RV94, RV95, RV96, RV97, RV99 or RV101, as disclosed in WO 2021 / 038508, which is hereby incorporated by reference. In an embodiment, the ionizable cationic lipid comprises, consists of, consists essentially of, or is RV39, i.e., 2,5-bis((9Z,12Z)-octadeca-9,12-dien-1-yloxy)benzyl 4-(dimethylamino)butanoate):

[0003] Attorney Docket No: 70488WO01 In or is 2-(5-((4-((1,4-dimethylpiperidine-4-carbonyl)oxy)hexadecyl)oxy)-5-oxopentyl)propane-1,3-diyl dioctanoate (RV94), having the following structure: In some or is a ionizable cationic lipid from WO2012 / 006376, WO2012 / 030901, WO2012 / 031046, WO2012 / 031043, WO2012 / 006378, WO2011 / 076807, WO2013 / 033563, WO2013 / 006825, WO2014 / 136086, WO2015 / 095340, WO2015 / 095346, WO2016 / 037053, WO2017 / 075531, WO2018 / 081480, WO2015 / 074085, WO2018 / 1703322, U.S. Patent Application Publication Nos.: 20220081392, 20220072155, 20220040285, 20210395188, 20210251898, 20210128488, 20210122703, 20210122702, 20210107861, 20200283372, 20200172472, 20200163878, 20200121809, 20200046838, 20190359556, 20190314524, 20190274968, 20190270697, 20190022247, 20180185516, 20170283367, 20170157268, 20170119904, 20160376224, 20160317676, or 20150376115, U.S. Application Nos.61 / 905,724 or 15 / 614,499, or U.S. Patent Nos.8,802,863, 9,458,090, 9,593,077, 9,567,296, 9,604,908, 9,643,916, 9,669,097, 9,670,487, 9,737,619, 9,738,593, 9,725,720, 9,796,977,10,106,490, 10,166,298, 10,221,127, 10,723,692, 11,040,112, 11,168,051, 11,246,933, or 11,285,222 (called ionizable lipids therein). Anionic lipid, Neutral Lipid, or Zwitterionic lipid In some embodiments, the lipids of the LNP further comprises an anionic lipid, a neutral lipid, or a zwitterionic lipid (i.e. a net neutral lipid). In some embodiments, the neutral lipid comprises, consists of, or is a neutral zwitterionic lipid. In some embodiments, the anionic lipid, a neutral lipid, or the zwitterionic lipid comprises a phospho-group (i.e. is a phospholipid), a choline, or a sphingolipid. Attorney Docket No: 70488WO01 In some embodiments, the anionic lipid, a neutral lipid, or the zwitterionic lipid is described in WO2023 / 242817, which is hereby incorporated by reference in its entirety. In some embodiments, the anionic lipid, neutral lipid, or zwitterionic lipid (i.e. net neutral lipid) comprises, consists of, or is 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE), 1,2-distearoyl- sn-glycero-3-phosphocholine (DSPC), 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), or sphingomyelin. Sterols In some embodiments, the lipid nanoparticles further comprise a sterol. In some embodiments, the sterol comprises, consists of, or is cholesterol, cholesterol sulfate, desmosterol, stigmasterol, lanosterol, 7-dehydrocholesterol, dihydrolanosterol, symosterol, lathosteriol, 14-demethyl-lanosterol, 8(9)-dehydrocholesterol, 8(14)-dehydrocholesterol, 14-demethyl-14-dehydrolanosterol (FF-MAS), diosgenin, dehydroepiandrosterone sulfate (DHEA sulfate), dehydroepiandrosterone, sitosterol, lanosterol-95, 4,4-dimethyl(d6)-cholest-8(9), 14-dien-3β-ol (dihydro-FF-MAS-d6), 4,4-dimethyl(d6)- cholest-8(9)-en-3β-ol (dihydro T-MAS-d6), zymostenol, sitostanol, campestanol, camperstanol, 7- dehydrodesmosterol, pregnenolone, 4,4-dimethyl-cholest-8(9)-en-3β-ol (dihyrdro T-MAS), Δ5- avensterol, brassicasterol, dihydro FF-MAS, 24-methylene cholesterol, oxysterols, deuterated sterols, fluorinated sterols, sulfonated sterols, phosphorylated sterols, A-ring substituted sterols, cholest-5-ene-3ß,4ß-diol, 5α-cholestan-3ß-ol, 4-cholesten-3-one, cholesta-8(9),24-dien-3-one, cholesta-8(9),24-dien-3-one, 2,2,3,4,4-pentadeuterio-5a-cholestan-3ß-ol, cholesteryl phosphocholine, cholesteryl-d7 pentadecanoate, cholesteryl-d7 palmitate, B-ring substituted sterols, cholestanol, 5ß,6ß-epoxy-d7, 3ß-hydroxy-5-cholestene-7-one, 6α-hydroxy-5α-cholestane, cholestanol, 5α,6α-epoxy, cholest-5-en-3ß,7α-diol, cholest-5-en-3ß,7ß-diol, cholestanol, 5α,6α- epoxy-d7, Δ5,7-cholesterol, cholesta-5,8(9)-dien-3ß-ol, cholesta-5,8(14)-dien-3ß-ol, 7α-hydroxy-4- cholesten-3-one, zymostenol-d7, zymostenol, 7-dehydrodesmosterol, 3b,5a-dihydroxy-cholestan-6- one, D-ring substituted sterols, 3ß-hydroxy-5α-cholest-8(14)-en-15-one, 3ß-hydroxy-5α-cholestane- 15-one, 5α-cholest-8(14)-ene-3ß,15α-diol, 5α-cholest-8(14)-ene-3ß,15ß,-diol, lanosterol-95, 5α-7,24- cholestadiene, 14-dehydro zymostenol, ergosta-5,7,9(11),22-tetraen-3ß-ol, cholest-5-ene-3ß,25-diol, cholest-(25R)-5-ene-3ß,27-diol, 24(R / S),25-epoxycholesterol, 24(S),25-epoxycholesterol, 24(R / S),25-epoxycholesterol-d6, cholest-5-ene-3ß,22(S)-diol, cholest-5-ene-3ß,22(R)-diol, cholest-5- ene-3ß,24(S)-diol, cholest-5-ene-3ß,24(R)-diol, 27-hydroxy-4-cholesten-3-one, campestanol, N,N- dimethyl-3ß-hydroxycholenamide, 25,27-dihydroxycholesterol, N,N-dimethyl-3ß- hydroxycholenamide, 25,27-dihydroxycholesterol, 5-cholestene-3β,20α-diol, 24S,25-epoxy-5α- cholest-8(9)-en-3β-ol, 24(S / R),25-epoxylanost-8(9)-en-3β-ol, 7-keto-27-hydroxycholesterol, 7α,27- dihydroxy-4-cholesten-3-one, 7α,27-dihydroxycholesterol, 7ß,27-dihydroxycholesterol, 5α,6ß- dihydroxycholestanol, 7α,25-dihydroxycholesterol, 7β,25-dihydroxycholesterol, 7α,24(S)- dihydroxycholesterol, 7α,24(S)-dihydroxy-4-cholesten-3-one, 7-keto-25-hydroxycholesterol, 7α,24S,27-trihydroxycholesterol, dihydrotestosterone, testosterone, estrone, estrogen, estradiol, corticosterone, cortisol, or 24S,27-dihydroxycholesterol. Attorney Docket No: 70488WO01 Polymer-conjugated lipids As noted above, the lipids of the LNP can comprise a polymer-conjugated lipid. Polymer- conjugated lipids can include those described in U.S. Patent No.11,759,442 including the those in Formula (X) found from Column 3, Line 53, to Column 4, line 28. In a preferred embodiment, the polymer-conjugated lipid comprises, consists of, or is a poly(ethylene glycol)-conjugated lipid (PEG- conjugated). Poly(ethylene glycol)-conjugated lipids In some embodiments, the polymer-conjugated lipid comprises, consists of, or is a poly(ethylene glycol)-conjugated (PEG-conjugated) lipid. In some embodiments, the PEG-conjugated lipid comprises a poly(ethylene glycol) (PEG) having various lengths and number-averaged molecular weights. In some embodiments, the PEGs in the PEG-conjugated lipids have a number-averaged molecular weight of at least: 0.9 kDa, 1.1 kDa, 1.3 kDa, 1.5 kDa, or 1.7 kDa. In some embodiments, the PEGs in the PEG-conjugated lipids have a number-averaged molecular weight of no more than: 8 kDa, 6 kDa, 4 kDa, 3.8 kDa, 3.6 kDa, 3.4 kDa, 3.2 kDa, 3 kDa, 2.8 kDa, or 2.6 kDa. In some embodiments, the PEGs in the PEG-conjugated lipids have a number-averaged molecular weight from 0.5 kDa to: 3.0 kDa, 3.1 kDa, 3.2 kDa, 3.3 kDa, or 3.4 kDa; from 0.7 kDa to: 2.5 kDa, 2.6 kDa, 2.7 kDa, 2.8 kDa, 2.9 kDa, 3.0 kDa, 3.1 kDa, or 3.2 kDa; from 0.9 kDa to: 2.3 kDa, 2.4 kDa, or 2.5 kDa; from 1.3 kDa to: 2.3 kDa, 2.4 kDa, 2.5 kDa, or 2.6 kDa; or from 1.5 kDa to: 2.0 kDa, 2.1 kDa, 2.2 kDa, 2.3 kDa, or 2.4 kDa. In some embodiments, the PEGs in the PEG-conjugated lipids have a number-average molecular weight of: 0.5 kDa, 1.0 kDa, 1.5 kDa, 1.6 kDa, 1.7 kDa, 1.8 kDa, 1.9 kDa, 2.0 kDa, 2.1 kDa, 2.2 kDa, 2.3 kDa, 2.4 kDa, 2.5 kDa, 3.0 kDa, 3.5 kDa, 4.0 kDa, 4.5 kDa, 5.0 kDa, 5.5 kDa, or 6.0 kDa. In some embodiments, the PEG-conjugated lipid comprises, consists of, or is 1,2-dimyristoyl-rac- glycero-3-methoxypolyethylene glycol-2000 or 1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N- [methoxy(polyethylene glycol)-2000]. In some embodiments, the PEG-conjugated lipid comprises, consists of, or is 1,2-dimyristoyl-rac-glycerol-3-methoxypolyethylene glycol. In some embodiments, the PEG-conjugated lipid comprises, consists of, or is N,N-ditetradecylacetamide PEG(2000) or the following molecule: Mole amounts of lipids in the LNP In some embodiments, the lipids in the LNP have, comprise, consist of, consist essentially of, or are from 20 mole% to 70 mole%; from 24 mole% to 65 mole%; from 28 mole% to 60 mole%; from 30 Attorney Docket No: 70488WO01 mole% to 55 mole%; from 32 mole% to 50 mole%; or from 34 mole% to 45 mole% of the ionizable cationic lipid. In some embodiments, the lipids in the LNP have, comprise, consist of, consist essentially of, or are from 30 mole% to 70 mole%; from 35 mole% to 65 mole%; from 40 mole% to 60 mole%; from 45 mole% to 55 mole%; from 47 mole% to 52 mole%; or from 49 mole% to 51 mole% of sterol (e.g. cholesterol). In some embodiments, the lipids in the LNP have, comprise, consist of, consist essentially of, or are from 0.7 mole% to 8.0 mole%; from 1.1 mole% to 7.4 mole%; from 1.5 mole% to 6.8 mole%; from 1.7 mole% to 5.4 mole%; from 1.9 mole% to 4.8 mole%; or from 2.1 mole% to: 2.6 mole%, 2.8 mole%, 3.0 mole%, 3.2 mole%, 3.4 mole%, 3.6 mole%, 3.8 mole%, 4.0 mole%, 4.2 mole%, or 4.4 mole% of polymer-conjugated lipid (e.g. PEG-conjugated lipid). In some embodiments, the lipids in the LNP have, comprise, consist of, consist essentially of, or are from 0.1 mole% to20.9 mole%; from 5 mole% to 20.0 mole%; from 7.5 mole% to 20.0 mole%; from 10 mole% to: 16.0 mole%, 16.5 mole%, 17.0 mole%, 17.5 mole%, 18.0 mole%, 18.5 mole%, 19.0 mole%, 19.5 mole%, or 20.0 mole% of anionic lipid, neutral lipid, zwitterionic lipid, or combinations thereof. In some embodiments, the formulations comprising the LNP and the EBV antigen-encoding and non-EBV antigen-encoding mRNA constructs have a ratio of the number of nitrogen in the lipids of the LNP to the phosphorous atoms in the recombinant RNA molecules in the “from”, “to”, and ranges described in WO2023 / 242817, which is hereby incorporated by reference in its entirety. In some embodiments, the lipids in the LNP have, comprise, consist of, consist essentially of, or are: (1) from 20 mole% to 70 mole%; from 24 mole% to 65 mole%; from 28 mole% to 60 mole%; from 30 mole% to 55 mole%; from 32 mole% to 50 mole%; or from 34 mole% to 45 mole% of the ionizable cationic lipid, such as RV94, the ALC-315, or the SM-102; from 30 mole% to 70 mole%; from 35 mole% to 65 mole%; from 40 mole% to 60 mole%; (2) from 45 mole% to 55 mole%; from 47 mole% to 52 mole%; or from 49 mole% to 51 mole% of the sterol, such as cholesterol; from 0.7 mole% to 8.0 mole%; from 1.1 mole% to 7.4 mole%; from 1.5 mole% to 6.8 mole%; from 0.1 mole% to20.9 mole%; from 5 mole% to 20.0 mole%; from 7.5 mole% to 20.0 mole%; from 10 mole% to: 16.0 mole%, 16.5 mole%, 17.0 mole%, 17.5 mole%, 18.0 mole%, 18.5 mole%, 19.0 mole%, 19.5 mole%, or 20.0 mole% of the zwitterionic lipid, such as DSPC or DOPC; and from 1.7 mole% to 5.4 mole%; from 1.9 mole% to 4.8 mole%; or from 2.1 mole% to: 2.6 mole%, 2.8 mole%, 3.0 mole%, 3.2 mole%, 3.4 mole%, 3.6 mole%, 3.8 mole%, 4.0 mole%, 4.2 mole%, or 4.4 mole% of the PEG-conjugated lipid, such as 1,2-dimyristoyl-rac-glycero-3-methoxypolyethylene glycol-2000, the 1,2-distearoyl-sn- glycero-3-phosphoethanolamine-N-[methoxy(polyethylene glycol)-2000], the N,N- ditetradecylacetamide PEG(2000), or the following molecule: Attorney Docket No: 70488WO01 . vehicles such as polymeric microparticles. Various polymers can form microparticles to encapsulate or adsorb the at least two EBV antigen- encoding mRNA constructs. The use of a substantially non-toxic polymer means that a recipient can safely receive the particles, and the use of a biodegradable polymer means that the particles can be metabolized after delivery to avoid long-term persistence. Useful polymers are also sterilizable, to assist in preparing pharmaceutical grade formulations. Suitable non-toxic and biodegradable polymers of the polymeric microparticles include, but are not limited to, poly(α-hydroxy acids), polyhydroxy butyric acids, polylactones (including polycaprolactones), polydioxanones, polyvalerolactone, polyorthoesters, polyanhydrides, polycyanoacrylates, tyrosine-derived polycarbonates, polyvinyl-pyrrolidinones or polyester-amides, and combinations thereof. In some embodiments, the polymeric microparticles are formed from poly(α-hydroxy acids), such as a poly(lactides) ("PLA"), copolymers of lactide and glycolide such as a poly(D,L-lactide-co- glycolide) ("PLG''), and copolymers of D,L-lactide and caprolactone. Useful PLG polymers include those having a lactide / glycolide molar ratio ranging, for example, from 20:80 to 80:20, e.g., 25:75, 40:60, 45:55, 50:50, 55:45, 60:40, 75:25. Useful PLG polymers include those having a molecular weight between, for example, 5,000-200,000 Da, e.g., between 10,000-100,000, 20,000-70,000, 30,000-40,000, 40,000-50,000 Da. The microparticles ideally have a diameter in the range of 0.02µm to 8µm. For a composition comprising a population of polymeric microparticles with different diameters at least 80% by number should have diameters in the range of 0.03-7µm. Techniques for preparing suitable polymeric microparticles are described in WO2012 / 006377, which is incorporated by reference in its entirety. To facilitate adsorption of RNA, a microparticle may include a cationic surfactant and / or lipid, e.g., as disclosed in WO2012 / 006377. In this regard, non- lipid delivery vehicles do not entirely lack lipids, but the presence of lipids may be there to facilitate the appropriate properties of the polymeric microparticles (e.g. avoid aggregation, etc.) An alternative way of making polymeric microparticles is by molding and curing, e.g., as disclosed in reference 11. The polymeric microparticles can have a zeta potential of between 40-100 mV. One advantage of microparticles is that they are readily lyophilized for stable storage. The EBV antigen-encoding mRNA constructs can be adsorbed to the microparticles, and adsorption is facilitated by including cationic materials (e.g., cationic lipids) in the microparticle. Self-replicating mRNA constructs Attorney Docket No: 70488WO01 In other embodiments, the at least two EBV antigen-encoding mRNA constructs are self- replicating. Accordingly, at least one, or each, of the EBV antigen-encoding mRNA constructs comprises a segment that encodes an RNA-dependent RNA polymerase and the at least one, or each, of the at least two EBV antigen-encoding mRNA constructs being a self-replicating mRNA construct. The RNA-dependent RNA polymerase can in certain embodiments be from, for example, a Sindbis virus, a Semliki forest virus, an eastern equine encephalitis virus (EEEV), or a Venezuelan equine encephalitis virus (VEEV). Mutant or wild-type virus sequences can be used e.g. the attenuated TC83 mutant of VEEV has been used for self-replicating RNA. Thus, in certain embodiments, the EBV antigen-encoding mRNA construct comprises a segment that encodes the RNA-dependent RNA polymerase and the segment that encodes the EBV antigen. In certain embodiments, the EBV antigen-encoding mRNA construct comprises a segment that encodes the RNA-dependent RNA polymerase and the segment that encodes the EBV antigen. In certain embodiments, the EBV antigen-encoding mRNA construct comprises a segment that encodes the RNA-dependent RNA polymerase and the segment that encodes the EBV antigen; the segment that encodes the RNA-dependent RNA polymerase is 5’ of the segment that encodes the EBV antigen. In some embodiments, an internal ribosomal entry site sits between the segment that encodes the RNA-dependent RNA polymerase and the segment that encodes the EBV antigen. In some embodiments at least one, or each, of the EBV antigen-encoding mRNA constructs comprises a segment that encodes replicase and the at least one, or each, of the at least two EBV antigen-encoding mRNA constructs being a self-replicating mRNA construct. In some embodiments at least one, or each, of the EBV antigen-encoding mRNA constructs comprises a segment that encodes replicase and the at least one, or each, of the at least two EBV antigen-encoding mRNA constructs being a self-replicating mRNA construct; and the replicase comprises alphavirus proteins nsP1, nsP2, nsP3 and nsP4. In some embodiments, alphavirus nsP4 comprises an RNA-dependent RNA polymerase. Such alphavirus-based self-replicating RNA can use a replicase from, for example, a Sindbis virus, a Semliki forest virus, an eastern equine encephalitis virus (EEEV), or a Venezuelan equine encephalitis virus (VEEV). Mutant or wild-type virus sequences can be used e.g. the attenuated TC83 mutant of VEEV has been used for self-replicating RNA. Thus, in certain embodiments, the EBV antigen-encoding mRNA construct comprises a segment that encodes the replicase and the segment that encodes the EBV antigen. In certain embodiments, the EBV antigen-encoding mRNA construct comprises a segment that encodes the replicase and the segment that encodes the EBV antigen. In certain embodiments, the EBV antigen-encoding mRNA construct comprises a segment that encodes the replicase and the segment that encodes the EBV antigen; the segment that encodes the replicase is 5’ of the segment that encodes the EBV antigen. In some embodiments, an internal ribosomal entry site sits between the segment that encodes the replicase and the segment that encodes the EBV antigen. Trans-amplifying mRNA Attorney Docket No: 70488WO01 In some embodiments, the pharmaceutical composition further comprises an RNA-dependent RNA polymerase-encoding mRNA construct comprising a segment that encodes the RNA-dependent RNA polymerase. In such embodiments, the RNA-dependent RNA polymerase-encoding mRNA construct and the at least two EBV antigen-encoding mRNA constructs are collectively trans- amplifying mRNA constructs, such that when the RNA-dependent RNA polymerase is expressed in a host cell, the EBV antigen-encoding mRNA constructs are amplified. The RNA-dependent RNA polymerase can in certain embodiments be from, for example, a Sindbis virus, a Semliki forest virus, an eastern equine encephalitis virus (EEEV), or a Venezuelan equine encephalitis virus (VEEV). Mutant or wild-type virus sequences can be used e.g. the attenuated TC83 mutant of VEEV has been used for self-replicating RNA. In some embodiments, the pharmaceutical composition further comprises an replicase-encoding mRNA construct comprising a segment that encodes the replicase. In such embodiments, the replicase-encoding mRNA construct and the at least two EBV antigen-encoding mRNA constructs are collectively trans-amplifying mRNA constructs, such that when the replicase is expressed in a host cell, the EBV antigen-encoding mRNA constructs are amplified. In some embodiments, alphavirus nsP4 comprises an RNA-dependent RNA polymerase. Such alphavirus-based self- replicating RNA can use a replicase from, for example, a Sindbis virus, a Semliki forest virus, an eastern equine encephalitis virus (EEEV), or a Venezuelan equine encephalitis virus (VEEV). Mutant or wild-type virus sequences can be used e.g. the attenuated TC83 mutant of VEEV has been used for self-replicating RNA. SUBUNIT / PROTEIN VACCINES In some aspects, a pharmaceutical composition is provided; the pharmaceutical composition comprises EBV antigens, the EBV antigens comprising at least two recombinant T cell module antigens, the at least two recombinant T cell module antigens comprise: (a) at least four of the EBV LMP1 protein fragments, (b) at least four of the EBV LMP2 protein fragments, (c) at least three of the EBNA1 protein fragments, and (d) at least seven of the EBNA3A protein fragments; the first of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 2; the second of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 3; the third of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 4; the fourth of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 5; the first of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 8; the second of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 9; the third of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 10; the fourth of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 11; the first of the EBNA1 protein Attorney Docket No: 70488WO01 fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 13; the second of the EBNA1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 14; the third of the EBNA1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 15; the first of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 17; the second of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 18; the third of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 19; the fourth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 20; the fifth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 21; the sixth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 22; and the seventh of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 23. In some embodiments, the at least two recombinant T cell module antigens comprise: (a) at least four of the EBV LMP1 protein fragments, (b) at least four of the EBV LMP2 protein fragments, (c) at least three of the EBNA1 protein fragments, and (d) at least seven of the EBNA3A protein fragments; the first of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 2; the second of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 3; the third of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 4; the fourth of the EBV LMP1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 5; the first of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 8; the second of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 9; the third of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 10; the fourth of the EBV LMP2 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 11; the first of the EBNA1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 13; the second of the EBNA1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 14; the third of the EBNA1 protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 15; the first of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 17; the second of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 18; the third of the EBNA3A protein fragments has at least 80%, at least 85%, at least Attorney Docket No: 70488WO01 90%, at least 95%, or at least 99% identity to SEQ ID NO: 19; the fourth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 20; the fifth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 21; the sixth of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 22; the seventh of the EBNA3A protein fragments has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 23; at least two of, or at least three of, the first, second, third, and fourth of the EBV LMP1 protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens; at least two of, or at least three of, the first, second, third, and fourth of the EBV LMP2 protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens; at least two of the first, second, and third of the EBNA1 protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens; and at least two of, at least three of, at least four of, at least five of, or at least six of the first, second, third, fourth, fifth, sixth, and seventh of the EBNA3A protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens. In some embodiments therein; the first, second, third, and fourth of the EBV LMP1 protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens; the first, second, third, and fourth of the EBV LMP2 protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens; the first, second, and third of the EBNA1 protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens; and the first, second, third, fourth, fifth, sixth, and seventh of the EBNA3A protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens. In some embodiments therein, the at least two recombinant T cell module antigens further comprise a first of the ZEBRA protein fragments, which has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 25, and a second of the ZEBRA protein fragments, which has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO:26. In some embodiments therein, the at least two recombinant T cell module antigens further comprise a first of the ZEBRA protein fragments, which has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 25, and a second of the ZEBRA protein fragments, which has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO:26; the first of the recombinant T cell module antigens comprises, from N-terminus to C-terminus, the second of the EBNA1 protein fragments, the seventh of the EBNA3A protein fragments, the fourth of the EBV LMP2 protein fragments, the second of the ZEBRA protein fragments, the first of the EBNA3A protein fragments, the second of the EBV LMP1 protein fragments, the sixth of the EBNA3A protein fragments, the third of the EBV LMP2 protein fragments, the third of the EBV LMP1 protein fragments, and the fifth of the EBNA3A protein fragments. In some embodiments therein, the segment that encodes the first of the recombinant T cell module antigens Attorney Docket No: 70488WO01 comprising a sequence having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 30 or SEQ ID NO: 120. In some embodiments of the last paragraph, the second of the recombinant T cell module antigens comprises, from N-terminus to C-terminus, the second of the EBV LMP2 protein fragments, the fourth of the EBV LMP1 protein fragments, the fourth of the EBNA3A protein fragments, the first of the EBV LMP1 protein fragments, the first of the EBNA1 protein fragments, the third of the EBNA3A protein fragments, the first of the EBV LMP2 protein fragments, the second of the EBNA3A protein fragments, the first of the ZEBRA protein fragments, and the third of the EBNA1 protein fragments. In some embodiments therein, the segment that encodes the second of the recombinant T cell module antigens comprising a sequence having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 32 or SEQ ID NO: 121. Accordingly, in some embodiments, the first of the recombinant T cell module antigens has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 29; and the second of the recombinant T cell module antigens has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 31 In some embodiments, the pharmaceutical composition comprises at least three of the at least two EBV recombinant T cell module antigens; the at least three recombinant T cell module antigens further comprise a first ZEBRA protein fragment, which has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 25, and a second ZEBRA protein fragment, which has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO:26; the first of the recombinant T cell module antigens comprises, from N-terminus to C-terminus, the second of the EBNA1 protein fragments, the seventh of the EBNA3A protein fragments, the fourth of the EBV LMP2 protein fragments, the second of the ZEBRA protein fragments, the first of the EBNA3A protein fragments, the second of the EBV LMP1 protein fragments, and the sixth of the EBNA3A protein fragments. In some embodiments, the second of the recombinant T cell module antigens comprises, from N- terminus to C-terminus, the third of the EBV LMP2 protein fragments, the third of the EBV LMP1 protein fragments, the fifth of the EBNA3A protein fragments, the second of the EBV LMP2 protein fragments, the fourth of the EBV LMP1 protein fragments, the fourth of the EBNA3A protein fragments, and the first of the EBV LMP1 protein fragments. In some embodiments, the third of the recombinant T cell module antigens comprises, from N- terminus to C-terminus, the first of the EBNA1 protein fragments, the third of the EBNA3A protein fragments, the first of the EBV LMP2 protein fragments, the second of the EBNA3A protein fragments, the first of the ZEBRA protein fragments, and the third of the EBNA1 protein fragments. In some embodiments, the pharmaceutical composition further comprises: i. a EBV gp42 antigen comprising an EBV gp42 protein or an EBV gp42 protein fragment, the EBV gp42 protein comprising a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 43; Attorney Docket No: 70488WO01 ii. a EBV gH antigen comprising an EBV gH protein or an EBV gH protein fragment; the EBV gH protein comprising a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 39; iii. a EBV gL antigen comprising an EBV gL protein or an EBV gL protein fragment, the EBV gL protein comprising a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 41; or iv. a EBV gp220 antigen comprising an EBV gp220 protein or an EBV gp220 protein fragment, the EBV gp220 protein comprising a sequence that has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 45. In some embodiments, the pharmaceutical composition comprises the EBV gp42 protein, the EBV gH protein, the EBV gL protein, and the EBV gp220 protein. In some embodiments, the pharmaceutical composition further comprises an adjuvant. In some embodiments, the adjuvant optionally comprises, consists of, or is a saponin. An “adjuvant” as used herein refers to a composition that enhances the immune response to an immunogen, which in the above-noted embodiments is provided as a protein within the pharmaceutical composition. The adjuvant accelerates, prolongs and / or enhances the quality and / or strength of an immune response to an antigen / immunogen in comparison to the administration of the antigen alone, or in comparison to the administration of an EBV antigen-encoding mRNA construct comprising a segment that encodes the EBV antigen. In some embodiments, the adjuvant reduces the quantity of EBV antigen, or the quantity of the EBV antigen-encoding mRNA construct comprising a segment that encodes the EBV antigen, necessary in any given vaccine, and / or the frequency of injection necessary to generate an adequate immune response to the EBV antigen. In some embodiments, the adjuvants may comprise inorganic adjuvants (e.g. inorganic metal salts such as aluminum phosphate or aluminum hydroxide), gel-like precipitates of aluminum hydroxide (alum); AlPO4; alhydrogel; bacterial products from the outer membrane of Gram-negative bacteria, in particular monophosphoryl lipid A (MPLA), lipopolysaccharides (LPS), muramyl dipeptides and derivatives thereof; Freund’s incomplete adjuvant; liposomes, in particular neutral liposomes, liposomes containing the composition and optionally cytokines; AS01B, AS01E, AS02; non-ionic block copolymers; ISCOMATRIX adjuvant; unmethylated DNA comprising CpG dinucleotides (CpG motif), in particular CpG ODN with a phosphorothioate (PTO) backbone (CpG PTO ODN) or phosphodiester (PO) backbone (CpG PO ODN); synthetic lipopeptide derivatives, in particular Pam3Cys; lipoarabinomannan; peptidoglycan; zymosan; heat shock proteins (HSP), in particular HSP 70; dsRNA and synthetic derivatives thereof, in particular Poly I:poly C; polycationic peptides, in particular poly-L-arginine; taxol; fibronectin; flagellin; imidazoquinoline; cytokines with adjuvant activity, in particular GM-CSF, interleukin- (IL-2, IL-6, IL-7, IL-18, type I and II interferons, in particular interferon-gamma, TNF-alpha; 25-dihydroxyvitamin D3 (calcitriol); synthetic oligopeptides, in particular MHCII-presented peptides; and non-ionic block polymers containing polyoxyethylene (POE) and polyoxypropylene (POP), such as POE-POP-POE block copolymers. Attorney Docket No: 70488WO01 In some embodiments, the adjuvants may comprise inorganic adjuvants (e.g. inorganic metal salts such as aluminium phosphate or aluminium hydroxide), organic adjuvants (e.g. saponins, such as QS21, or squalene), oil-based adjuvants (e.g. Freund's complete adjuvant and Freund's incomplete adjuvant), cytokines (e.g. IL-1β, IL-2, IL-7, IL-12, IL-18, GM-CFS, and INF-g) particulate adjuvants (e.g. immuno-stimulatory complexes (ISCOMS), liposomes, biodegradable microspheres, virosomes, bacterial adjuvants (e.g. monophosphoryl lipid A, such as 3-de-O-acylated monophosphoryl lipid A (3D-MPL), or muramyl peptides), synthetic adjuvants (e.g. monophosphoryl lipid A (MPL), in particular 3-de-O-acylated monophosphoryl lipid A (3D-MPL and muramyl peptide analogues, or synthetic lipid A, and synthetic polynucleotides adjuvants, e.g., polyarginine or polylysine. In some embodiments, the adjuvants may comprise saponins, for example, the saponin Quil A, derived from the bark of the South American tree Quillaja Saponaria Molina, and fractions thereof. In some embodiments, said fractions comprise, and thereby the adjuvant comprises: squalene, QS21, QS17 and QS7, a non-haemolytic fraction of Quil-A. Combinations of QS21 and polysorbate or cyclodextrin are also suitable. Another example of an adjuvant is an immunostimulatory oligonucleotide containing unmethylated cytosine-guanosine dinucleotide motifs present in DNA ("CpG"). CpG is known as an adjuvant when administered by both systemic and mucosal routes. When formulated into vaccines, it may be administered in free solution together with free antigen or covalently conjugated to an antigen or formulated with a carrier such as aluminium hydroxide. Activation of specific receptors can stimulate an immune response. Such receptors are known to the skilled artisan and comprise, for example, cytokine receptors, in particular type I cytokine receptors, type II cytokine receptors, TNF receptors; and a vitamin D receptor acting as transcription factor; and the Toll-like receptors 1 (TLR1), TLR-2, TLR 3, TLR4, TLR5, TLR-6, TLR7, and TLR9. Agonists to such receptors have adjuvant activity, i.e., are immunostimulatory. Other suitable adjuvants include alkyl glucosaminide phosphates (AGPs) or pharmaceutically acceptable salts of AGPs. Some AGPs are TLR4 agonists, and some are TLR4 antagonists. In certain embodiments, an adjuvant of the composition may be one or more Toll-like receptor agonists. In some aspects, the adjuvant is a Toll-like receptor 4 agonist. In some embodiments, the adjuvant is a Toll-like receptor 9 agonist. Adjuvants such as those described above may be formulated together with carriers, such as liposomes, oil in water emulsions, and / or metallic salts (including aluminum salts such as aluminum hydroxide). For example, 3D-MPL may be formulated with aluminum hydroxide or oil in water emulsions; QS21 may be formulated with cholesterol containing liposomes, oil in water emulsions or alum; CpG may be formulated with alum or with other cationic carriers. Combinations of adjuvants may be utilized in some embodiments, for example, a combination of a monophosphoryl lipid A and a saponin derivative, more particularly the combination of QS21 and 3D-MPL or a composition where the QS21 is quenched in cholesterol-containing liposomes (DQ). Attorney Docket No: 70488WO01 Alternatively, a combination of CpG plus a saponin such as QS21 is an adjuvant, as is a potent adjuvant formulation involving QS21, 3D-MPL and tocopherol in an oil in water emulsion. Saponin adjuvants may be formulated in a liposome and combined with an immunostimulatory polynucleotide. Thus, suitable adjuvants include, for example, a combination of monophosphoryl lipid A, preferably 3D-MPL, together with an aluminium salt. A further exemplary adjuvant comprises, consists of, or is QS21 and / or MPL and / or CpG. QS21 may be quenched in cholesterol-containing liposomes. METHODS OF TREATMENTS WITH THE PHARMACEUTICAL COMPOSITIONS In one aspect, a method of eliciting an immune response in a subject to the EBV antigens is provided, the method comprises administering to the subject a unit dose of the pharmaceutical compositions above (including those comprising the at least two EBV antigen-encoding mRNA constructs (each comprising a segment that encodes the EBV antigen) and those comprising the at least two recombinant T cell module antigens). In another aspect, a method of eliciting an immune response in a subject to the EBV antigens is provided, the method comprises administering to the subject a biologically effective amount of the pharmaceutical compositions above (including those comprising the at least two EBV antigen-encoding mRNA constructs (each comprising a segment that encodes the EBV antigen) and those comprising the at least two recombinant T cell module antigens).In some embodiments, the subject is human. In some embodiments in both aspects, the immune response is a protective immune response, which reduces the likelihood of the subject of being infected with EBV or the likelihood of a symptom of initial EBV infection). In some embodiments in both aspects, the immune response or the protective immune response comprises a cell-mediated immune response, an antibody-response (e.g. humoral immune response), a TH1immune response, or a TH2immune response. In some embodiments, the immune response is a therapeutic immune response. In some embodiments in both aspects, the therapeutic immune response is to treat multiple sclerosis (a therapeutic immune response against multiple sclerosis). In some embodiments in both aspects, the therapeutic immune response is to treat relapsing-remitting multiple sclerosis (a therapeutic immune response against relapsing-remitting multiple sclerosis). In some embodiments in both aspects, the therapeutic immune response to treat multiple sclerosis is an immune response that: reduces the likelihood of multiple sclerosis relapse, reduces the number of relapses of multiple sclerosis, and / or increases the time between relapses of multiple sclerosis (i.e. increases the time of remission of multiple sclerosis relapses). In some embodiments in both aspects, the therapeutic immune response is to treat cancers, such as gastric carcinoma, nasopharyngeal carcinoma, and lymphoma. In some embodiments, the therapeutic immune response is to treat post-transplant lymphoproliferative disorder (which is a lymphoma). Accordingly, in some embodiments, the subject has been diagnosed with multiple sclerosis, post- transplant lymphoproliferative disorder, gastric carcinoma, nasopharyngeal carcinoma, and / or lymphoma. Attorney Docket No: 70488WO01 In some embodiments, the subject has been diagnosed with multiple sclerosis. In some embodiments, the administering reduces the loss of myelinating cells in the subject who has been diagnosed with multiple sclerosis, when compared to a subject who has not been administered the pharmaceutical composition and who has been diagnosed with multiple sclerosis. In some embodiments, the administering reduces the concentration of myelinating basic protein in cerebrospinal fluid of the subject who has been diagnosed with multiple sclerosis, when compared to concentration of myelinating basic protein in cerebrospinal fluid of a subject who has not been administered the pharmaceutical composition and who has been diagnosed with multiple sclerosis. In some embodiments, the administering reduces the titers of antibodies against myelinating basic protein in cerebrospinal fluid of the subject who has been diagnosed with multiple sclerosis, when compared to titers of antibodies against myelinating basic protein in cerebrospinal fluid of a subject who has not been administered the pharmaceutical composition and who has been diagnosed with multiple sclerosis. In some embodiments, the administering reduces the titers of cytotoxic T cells against myelinating basic protein in cerebrospinal fluid of the subject who has been diagnosed with multiple sclerosis, when compared to titers of cytotoxic T cells against myelinating basic protein in cerebrospinal fluid of a subject who has not been administered the pharmaceutical composition and who has been diagnosed with multiple sclerosis. In some embodiments, the administering reduces the titers of Epstein-Barr virions in saliva of the subject who has been diagnosed with multiple sclerosis, when compared titers of Epstein-Barr virions in saliva of the subject of a subject who has not been administered the pharmaceutical composition and who has been diagnosed with multiple sclerosis. In some embodiments, the administering reduces the concentration of EBV antigens in saliva of the subject who has been diagnosed with multiple sclerosis, when compared to concentration of EBV antigens in saliva of a subject who has not been administered the pharmaceutical composition and who has been diagnosed with multiple sclerosis. In some embodiments, the administering increases the number of Th1 positive cells in serum or cerebrospinal fluid of the subject who has been diagnosed with multiple sclerosis, when compared to number of Th1 positive cells in serum or cerebrospinal fluid of a subject who has not been administered the pharmaceutical composition and who has been diagnosed with multiple sclerosis. In some embodiments, the administering increases the percent of Th1 positive cells in serum or cerebrospinal fluid of the subject who has been diagnosed with multiple sclerosis, when compared to percent of Th1 positive cells in serum or cerebrospinal fluid of a subject who has not been administered the pharmaceutical composition and who has been diagnosed with multiple sclerosis. In some embodiments, the subject is a mammal, such as a human or a large veterinary mammal (e.g. horses, cattle, deer, goats, pigs). Where the pharmaceutical composition is for eliciting a protective immune response, the subject is preferably a human, such as a child or a teenager. Where the pharmaceutical composition is used as a treatment or for therapeutic use, the human is Attorney Docket No: 70488WO01 preferably a teenager or an adult. In some embodiments, the human is preferably a teenager or an adult A vaccine intended for children may also be administered to adults, with the proviso that the amount of pharmaceutical composition may be scaled up to provide an unit dose consistent with the state of the immune system of the subject (i.e. the elderly having more difficulty eliciting certain immune responses) and the average body weight of a subject of that age or the actual body weight of the subject. In some embodiments, the pharmaceutical composition is administered to the subject intramuscularly, intradermally, subcutaneously, transcutaneously, topically, intraperitoneally, intrathecally, pulmonarily (i.e. inhaled), intracerebroventricularly, intravenously, intra-arterially, onto a mucosa (i.e. vaginally), buccally, sublingually, intranasally, optically, to the cornea, or into the eyeball. In some embodiments, the administering comprises contacting skeletal muscle of the subject with the pharmaceutical composition. In some embodiments, the unit dose (e.g. administered to the human) comprises, or is, at least: 5 μg, 10 μg, 20 μg, 25 μg, 30 μg, 35 μg, 40 μg, 45 μg, 50 μg, 55 μg, 60 μg, 65 μg, 70 μg, 75 μg, 80 μg, 85 μg, 90 μg, 95 μg, 100 μg, 105 μg, 110 μg, 115 μg, 120 μg, 125 μg, 130 μg, 135 μg, 140 μg, 145 μg, 150 μg, 155 μg, 160 μg, 165 μg, 170 μg, 175 μg, 180 μg, 185 μg, 190 μg, 195 μg, 200 μg, 205 μg, 210 μg, 215 μg, 220 μg, 225 μg, 230 μg, 235 μg, 240 μg, 245 μg, 250 μg, 255 μg, 260 μg of the at least two, at least three, at least four, at least five, at least six, at least seven of the EBV antigen-encoding mRNA constructs. In some embodiments, the unit dose (e.g. administered to the human) comprises or is no more than: 260 μg, 255 μg, 250 μg, 245 μg, 240 μg, 235 μg, 230 μg, 225 μg, 220 μg, 215 μg, 210 μg, 205 μg, 200 μg, 195 μg, 190 μg, 185 μg, 180 μg, 175 μg, 170 μg, 165 μg, 160 μg, 155 μg, 150 μg, 145 μg, 140 μg, 135 μg, 130 μg, 125 μg, 120 μg, 115 μg, 110 μg, 105 μg, 100 μg, 95 μg, 90 μg, 85 μg, 80 μg, 75 μg, 70 μg, 65 μg, 60 μg, 55 μg, 50 μg, 45 μg, 40 μg, 35 μg, 30 μg, 25 μg, 20 μg, or 15 μg of the at least two, at least three, at least four, at least five, at least six, at least seven of the EBV antigen-encoding mRNA constructs. In some embodiments, the unit dose (e.g. administered to the human) comprises or is from 5 μg to 259 μg; from 25 μg to 255 μg; from 50 μg to 250 μg; from 80 μg to 245 μg; from 85 μg to 240 μg; from 90 μg to 230 μg; from 95 μg to 220 μg; from 100 μg to 210 μg; from 105 μg to 200 μg; or from 110 μg to 195 μg of the at least two, at least three, at least four, at least five, at least six, at least seven of the EBV antigen-encoding mRNA constructs. In some embodiments, the unit dose comprises or is from 5 μg to 50μg; from 7.5 μg to 45μg; from 10 μg to 40 μg; from 12.5 μg to 35 μg; from 15 μg to 30 μg; from 17.5 μg to 25 μg; or from 20 μg to 25 μg of each of the at least two, at least three, at least four, at least five, at least six, or at least seven of the EBV antigen-encoding mRNA constructs. In some embodiments, the unit dose comprises or is from 0.1 μg of each of the at least two, at least three, at least four, at least five, at least six, or at least seven of the EBV antigen-encoding mRNA constructs per kg body weight of the subject (e.g. human) to 1.5 μg of each of the at least two, at least three, at least four, at least five, at least six, or at least seven of the EBV antigen- Attorney Docket No: 70488WO01 encoding mRNA constructs per kg body weight of the subject (e.g. human). In some embodiments, the unit dose comprises or is from 0.5 μg of each of the at least two, at least three, at least four, at least five, at least six, or at least seven of the EBV antigen-encoding mRNA constructs per kg body weight of the subject (e.g. human) to 1.2 μg of each of the at least two, at least three, at least four, at least five, at least six, or at least seven of the EBV antigen-encoding mRNA constructs per kg body weight of the subject (e.g. human). In some embodiments, the unit dose comprises or is from 0.75 μg of each of the at least two, at least three, at least four, at least five, at least six, or at least seven of the EBV antigen-encoding mRNA constructs per kg body weight of the subject (e.g. human) to 1.0 μg of each of the at least two, at least three, at least four, at least five, at least six, or at least seven of the EBV antigen-encoding mRNA constructs per kg body weight of the subject (e.g. human). In some embodiments, at least one, at least two, at least three, at least four, at least five administerings of biologically effective amount or the unit dose of the pharmaceutical composition to the subject is provided. In some embodiments, a primary administration is provided; the primary administration comprising at least one, at least two, at least three, at least four, at least five administerings of biologically effective amount or the unit dose of the pharmaceutical composition to the subject. In some embodiments, a booster administration is provided; the booster administration comprising at least one, at least two, at least three, at least four, at least five administerings of biologically effective amount or the unit dose of the pharmaceutical composition to the subject. In some embodiments, both a primary administration and a booster administration is provided; the primary administration comprising at least one, at least two, at least three, at least four, at least five administerings of biologically effective amount or the unit dose of the pharmaceutical composition to the subject; the booster administration comprising at least one, at least two, at least three, at least four, at least five administerings of biologically effective amount or the unit dose of the pharmaceutical composition to the subject. In the above-noted embodiments of this paragraph, the primary administerings, the booster administerings, and the biologically effective amounts of the pharmaceutical composition can optionally encompass the unit doses described in above in this section. In some embodiments, the methods of eliciting an immune response, of treating the above-noted diseases, include the unit doses, conditions, formulations, and embodiments described in WO2023 / 242817, which is hereby incorporated by reference in its entirety. METHOD OF MAKING THE PHARMACEUTICAL COMPOSITIONS Methods of manufacturing protein and subunit vaccines known elsewhere can be relied upon for making the aspects of the pharmaceutical compositions comprising the EBV antigens and the EBV antigens comprising at least two recombinant T cell module antigens. That is, in view of this specification’s disclosure regarding the aspects of the pharmaceutical compositions comprising the EBV antigens and the EBV antigens comprising at least two recombinant T cell module antigens, the methods of manufacturing such aspects, and embodiments therein, can now be achieved with known processes. Attorney Docket No: 70488WO01 Methods of manufacturing pharmaceutical compositions comprising mRNA constructs and delivery vehicles are also known. That is, in view of this specification’s disclosure regarding the aspects of the pharmaceutical compositions comprising at least two EBV antigen-encoding mRNA constructs, each of the EBV antigen-encoding mRNA constructs comprising a segment that encodes an EBV antigen, the methods of manufacturing such aspects and embodiments therein can now be achieved with known processes. Such processes are described in WO2012 / 006376; WO2012 / 030901; WO2012 / 031046; WO2012 / 031043; WO2012 / 006378; WO2011 / 076807; WO2013 / 033563; WO2013 / 006825; WO2014 / 136086; WO2015 / 095340; WO2015 / 095346; WO2016 / 037053; WO2017 / 075531; WO2018 / 081480; WO2015 / 074085; WO2018 / 170332; WO2010 / 053572; WO2012 / 170930; WO2014 / 197651; WO2015 / 123767; WO2019 / 064115; WO2023 / 242817; each of which are incorporated by reference in their entireties. In such aspects of methods of manufacturing pharmaceutical compositions, as described in the aspects above (i.e. pharmaceutical compositions comprising lipids and at least two EBV antigen- encoding mRNA constructs, each of the EBV antigen-encoding mRNA constructs comprising a segment that encodes an EBV antigen, the lipids encapsulating the at least two EBV antigen- encoding mRNA constructs), the method generally comprises: a. admixing the at least two EBV antigen-encoding mRNA constructs with an aqueous buffer, thereby obtaining an aqueous EBV antigen-encoding mRNA construct solution; b. admixing the lipids in an organic solvent, thereby obtaining a lipid solution; c. admixing the lipid solution and the aqueous EBV antigen-encoding mRNA construct solution with at least a T-mixer, a microfluidics mixer, or an impinging jet mixer, thereby obtaining a first admixture, wherein the first admixture comprises the LNPs, wherein at least some of at least two EBV antigen-encoding mRNA constructs are encapsulated in the LNPs; and d. purifying the LNPs to obtain the encapsulation by the lipids of the at least 50 mass %, at least 75 mole% of, at least 80 mole%, at least 85 mole%, at least 90 mole%, or at least 95 mole% of the at least two EBV antigen-encoding mRNA constructs. In some embodiments, the pharmaceutical composition is obtained from (d) purifying the LNPs. In other embodiments, dialysis, cross-flow filtration, tangential flow filtration, and ultra filtration provide for a change of solution components to obtain the pharmaceutical composition. In some embodiments, the aqueous buffer comprises, consists of, or is citrate buffer (e.g. sodium citrate) or acetate buffer (e.g. sodium acetate). In some embodiments, the organic solvent comprises, consists of, or is chloroform, dichloromethane, diethylether, cyclohexane, cyclopentane, benzene, toluene, methanol, benzyl alcohol, and aliphatic alcohols (e.g. C1 to C8 alcohols). In some embodiments, the aliphatic alcohols comprise ethanol, propanol, isopropanol, butanol, tert-buranol, isobutanol, pentanol, benzyl alcohol, and hexanol. In some embodiments, the organic solvent comprises, consists of, or is an alcohol solution. In some embodiments, the organic alcohol solution comprises, consists of, or is from 70 volume % to 100 volume % ethanol. Attorney Docket No: 70488WO01 In some embodiments, the EBV antigen-encoding mRNA constructs and lipids of the LNP are admixed in an organic solvent. In some embodiments, the organic solvent comprises, consists of, or is chloroform, dichloromethane, diethylether, cyclohexane, cyclopentane, benzene, toluene, methanol, benzyl alcohol, and aliphatic alcohols (e.g. C1 to C8 alcohols). In some embodiments, the aliphatic alcohols comprise ethanol, propanol, isopropanol, butanol, tert-buranol, isobutanol, pentanol, benzyl alcohol, and hexanol. In some embodiments, the organic solvent comprises, consists of, or is an alcohol solution. In some embodiments, the organic alcohol solution comprises, consists of, or is from 70 volume % to 100 volume % ethanol. In some embodiments, the organic alcohol solution comprises, consists of, or is from 70 volume % to 100 volume % ethanol and 30 volume % to 0 volume % benzyl alcohol. In some embodiments, the aqueous solution comprises, consists of, or is a citrate buffer (e.g. sodium citrate) or an acetate buffer (e.g. sodium acetate). In some embodiments, the aqueous EBV antigen-encoding mRNA construct solution and lipid solution ar...

Claims

Attorney Docket No: 70488WO01 CLAIMS We claim:

1. A pharmaceutical composition comprising lipids and at least two EBV antigen-encoding mRNA constructs; the lipids encapsulating the at least two EBV antigen-encoding mRNA constructs, thereby forming LNPs; each of the EBV antigen-encoding mRNA constructs comprising a segment that encodes an EBV antigen; the EBV antigens comprising an EBV B cell module antigen and an EBV T cell module antigen; the EBV B cell module antigen comprising an EBV gp220 antigen; and the EBV T cell module antigen comprising at least two, at least three, or at least four of: (a) an EBV LMP1 antigen; (b) an EBV LMP2 antigen; (c) an EBNA1 antigen; (d) EBNA3A antigen; and (e) a ZEBRA antigen.

2. The pharmaceutical composition of claim 1, the lipids encapsulating at least 50 mass %, at least 75 mass% of, at least 80 mass%, at least 85 mass%, at least 90 mass%, or at least 95 mass% of the at least two immunogen-encoding mRNA constructs (e.g. the lipids encapsulating at least 50 mass %, at least 75 mass% of, at least 80 mass%, at least 85 mass%, at least 90 mass%, or at least 95 mass% of the at least two EBV antigen-encoding mRNA constructs).

3. The pharmaceutical composition of claim 1 or claim 2, the EBV B cell module antigen further comprising an EBV glycoprotein-42 (gp42) antigen, an EBV glycoprotein-H (gH) antigen, and / or an EBV glycoprotein-L (gL) antigen.

4. The pharmaceutical composition of any of the preceding claims: i. the EBV LMP1 antigen comprising an EBV LMP1 protein or an EBV LMP1 protein fragment; the EBV LMP1 protein having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 1; and the EBV LMP1 protein fragment having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, or SEQ ID NO: 5; ii. the EBV LMP2 antigen comprising an EBV LMP2 protein or an EBV LMP2 protein fragment; the EBV LMP2 protein having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 6 or SEQ ID NO: 7; and the EBV LMP2 protein fragment having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, or SEQ ID NO: 11; iii. the EBNA1 antigen comprising an EBNA1 protein or an EBNA1 protein fragment; the EBNA1 protein having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 12; and the EBNA1 protein fragment having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 13, SEQ ID NO: 14, or SEQ ID NO: 15;Attorney Docket No: 70488WO01 iv. the EBNA3A antigen comprising an EBNA3A protein or an EBNA3A protein fragment; the EBNA3A protein having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 16; and the EBNA3A protein fragment having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 22, or SEQ ID NO: 23; and / or v. the ZEBRA antigen comprising the ZEBRA protein or a ZEBRA protein fragment; the ZEBRA protein having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 24; and the ZEBRA protein fragment having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 25 or SEQ ID NO:

26.

5. The pharmaceutical composition of claim 4, the T cell module antigen comprising the EBV LMP2 protein and the EBNA3A protein.

6. The pharmaceutical composition of claim 5, the T cell module antigen comprising the EBV LMP1 protein, the EBNA1 protein, and / or the ZEBRA protein.

7. The pharmaceutical composition of claim 4, the EBV T cell module antigen being a recombinant T cell module antigen; the recombinant T cell module antigen comprising: i. at least two EBV LMP1 protein fragments, which are not adjacent to each other on the recombinant T cell module antigen; ii. at least two EBV LMP2 protein fragments, which are not adjacent to each other on the recombinant T cell module antigen; iii. at least two EBNA1 protein fragments, which are not adjacent to each other on the recombinant T cell module antigen; iv. at least two EBNA3A protein fragments, which are not adjacent to each other on the recombinant T cell module antigen; and / or v. at least two ZEBRA protein fragments, which are not adjacent to each other on the recombinant T cell module antigen.

8. The pharmaceutical composition of claim 7 comprising at least three of the EBV antigen- encoding mRNA constructs; the EBV antigens comprising at least two of the recombinant T cell module antigens; the first of the EBV antigen-encoding mRNA constructs comprising the segment that encodes the first of the recombinant T cell module antigens; the second of the EBV antigen-encoding mRNA constructs comprising the segment that encodes the second of the recombinant T cell module antigens; the at least two of the recombinant T cell module antigens comprising: (a) at least four of the EBV LMP1 protein fragments, (b) at least four ofAttorney Docket No: 70488WO01 the EBV LMP2 protein fragments, (c) at least three of the EBNA1 protein fragments, and (d) at least seven of the EBNA3A protein fragments; the first of the EBV LMP1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 2; the second of the EBV LMP1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 3; the third of the EBV LMP1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 4; the fourth of the EBV LMP1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 5; the first of the EBV LMP2 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 8; the second of the EBV LMP2 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 9; the third of the EBV LMP2 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 10; the fourth of the EBV LMP2 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 11; the first of the EBNA1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 13; the second of the EBNA1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 14; the third of the EBNA1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 15; the first of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 17; the second of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 18; the third of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 19; the fourth of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 20; the fifth of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 21; the sixth of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 22; the seventh of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 23; at least two of, or at least three of, the first, second, third, and fourth of the EBV LMP1 protein fragments not being adjacent to each other on the at least two recombinant T cell module antigens; at least two of, or at least three of, the first, second, third, and fourth of the EBV LMP2 protein fragments not being adjacent to each other on the at least two recombinant T cell module antigens; at least two of the first, second, and third of the EBNA1 protein fragments not being adjacent to each other on the at least two recombinant T cell module antigens; and at least two of, at least three of, at least four of, at least five of, or at least six of the first, second, third, fourth, fifth, sixth, and seventh of theAttorney Docket No: 70488WO01 EBNA3A protein fragments not being adjacent to each other on the at least two recombinant T cell module antigens; wherein optionally: the first, second, third, and fourth of the EBV LMP1 protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens; the first, second, third, and fourth of the EBV LMP2 protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens; the first, second, and third of the EBNA1 protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens; and the first, second, third, fourth, fifth, sixth, and seventh of the EBNA3A protein fragments are not adjacent to each other on the at least two recombinant T cell module antigens.

9. The pharmaceutical composition of claim 8, the at least two recombinant T cell module antigens comprising a first of the ZEBRA protein fragments, which has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 25, and a second of the ZEBRA protein fragments, which has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO:26; the first of the recombinant T cell module antigens comprising, from N-terminus to C-terminus, the second of the EBNA1 protein fragments, the seventh of the EBNA3A protein fragments, the fourth of the EBV LMP2 protein fragments, the second of the ZEBRA protein fragments, the first of the EBNA3A protein fragments, the second of the EBV LMP1 protein fragments, the sixth of the EBNA3A protein fragments, the third of the EBV LMP2 protein fragments, the third of the EBV LMP1 protein fragments, and the fifth of the EBNA3A protein fragments; wherein, optionally, the segment that encodes the first of the recombinant T cell module antigens comprises a sequence having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 30 or SEQ ID NO:

120.

10. The pharmaceutical composition of claim 9, the second of the recombinant T cell module antigens comprising, from N-terminus to C-terminus, the second of the EBV LMP2 protein fragments, the fourth of the EBV LMP1 protein fragments, the fourth of the EBNA3A protein fragments, the first of the EBV LMP1 protein fragments, the first of the EBNA1 protein fragments, the third of the EBNA3A protein fragments, the first of the EBV LMP2 protein fragments, the second of the EBNA3A protein fragments, the first of the ZEBRA protein fragments, and the third of the EBNA1 protein fragments; wherein, optionally: (a) the segment that encodes the second of the recombinant T cell module antigens comprises a sequence having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 32 or SEQ ID NO: 121; or (b) the first of the recombinant T cell module antigens has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 29; and theAttorney Docket No: 70488WO01 second of the recombinant T cell module antigens has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO:

31.

11. The pharmaceutical composition of any of claims 8-10 comprising at least six of the EBV antigen-encoding mRNA constructs; the third of the EBV antigen-encoding mRNA constructs comprising the segment that encodes an or the EBV gp42 antigen; the fourth of the EBV antigen-encoding mRNA constructs comprising the segment that encodes an or the EBV gH antigen; the fifth of the EBV antigen-encoding mRNA constructs comprising the segment that encodes an or the EBV gL antigen; and the sixth of the EBV antigen-encoding mRNA constructs comprising the segment that encodes an or the EBV gp220 antigen.

12. The pharmaceutical composition of claim 7 comprising at least four of the EBV antigen- encoding mRNA constructs; the EBV antigens comprising at least three of the recombinant T cell module antigens; the first of the EBV antigen-encoding mRNA constructs comprising the segment that encodes the first of the recombinant T cell module antigens; the second of the EBV antigen-encoding mRNA constructs comprising the segment that encodes the second of the recombinant T cell module antigens; the third of the EBV antigen-encoding mRNA constructs comprising the segment that encodes the third of the recombinant T cell module antigens; the at least three of the recombinant T cell module antigens comprising: (a) at least four of the EBV LMP1 protein fragments, (b) at least four of the EBV LMP2 protein fragments, (c) at least three of the EBNA1 protein fragments, and (d) at least seven of the EBNA3A protein fragments; the first of the EBV LMP1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 2; the second of the EBV LMP1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 3; the third of the EBV LMP1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 4; the fourth of the EBV LMP1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 5; the first of the EBV LMP2 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 8; the second of the EBV LMP2 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 9; the third of the EBV LMP2 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 10; the fourth of the EBV LMP2 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 11; the first of the EBNA1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 13; the second of the EBNA1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 14; the third of the EBNA1 protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 15; the first of theAttorney Docket No: 70488WO01 EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 17; the second of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 18; the third of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 19; the fourth of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 20; the fifth of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 21; the sixth of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 22; the seventh of the EBNA3A protein fragments having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 23; at least two of, or at least three of, the first, second, third, and fourth of the EBV LMP1 protein fragments not being adjacent to each other on the at least three recombinant T cell module antigens; at least two of, or at least three of, the first, second, third, and fourth of the EBV LMP2 protein fragments not being adjacent to each other on the at least three recombinant T cell module antigens; at least two of the first, second, and third of the EBNA1 protein fragments not being adjacent to each other on the at least three recombinant T cell module antigens; and at least two of, at least three of, at least four of, at least five of, or at least six of the first, second, third, fourth, fifth, sixth, and seventh of the EBNA3A protein fragments not being adjacent to each other on the at least three recombinant T cell module antigens; wherein, optionally: the first, second, third, and fourth of the EBV LMP1 protein fragments are not adjacent to each other on the at least three recombinant T cell module antigens; the first, second, third, and fourth of the EBV LMP2 protein fragments are not adjacent to each other on the at least three recombinant T cell module antigens; the first, second, and third of the EBNA1 protein fragments are not adjacent to each other on the at least three recombinant T cell module antigens; and the first, second, third, fourth, fifth, sixth, and seventh of the EBNA3A protein fragments are not adjacent to each other on the at least three recombinant T cell module antigens 13. The pharmaceutical composition of claim 12, the at least three recombinant T cell module antigens comprising a first of the ZEBRA protein fragments, which has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 25, and a second of the ZEBRA protein fragments, which has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO:26; the first of the recombinant T cell module antigens comprising, from N-terminus to C-terminus, the second of the EBNA1 protein fragments, the seventh of the EBNA3A protein fragments, the fourth of the EBV LMP2 protein fragments, the second of the ZEBRA protein fragments, the first of the EBNA3A proteinAttorney Docket No: 70488WO01 fragments, the second of the EBV LMP1 protein fragments, and the sixth of the EBNA3A protein fragments; wherein, optionally, the segment that encodes the first of the recombinant T cell module antigens comprises a sequence having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 34 or SEQ ID NO:

122.

14. The pharmaceutical composition of claim 13, the second of the recombinant T cell module antigens comprising, from N-terminus to C-terminus, the third of the EBV LMP2 protein fragments, the third of the EBV LMP1 protein fragments, the fifth of the EBNA3A protein fragments, the second of the EBV LMP2 protein fragments, the fourth of the EBV LMP1 protein fragments, the fourth of the EBNA3A protein fragments, and the first of the EBV LMP1 protein fragments; wherein, optionally, the segment that encodes the second of the recombinant T cell module antigens comprises a sequence having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 36 or SEQ ID NO:

123.

15. The pharmaceutical composition of claim 13 or claim 14, the third of the recombinant T cell module antigens comprising, from N-terminus to C-terminus, the first of the EBNA1 protein fragments, the third of the EBNA3A protein fragments, the first of the EBV LMP2 protein fragments, the second of the EBNA3A protein fragments, the first of the ZEBRA protein fragments, and the third of the EBNA1 protein fragments; wherein, optionally: (a) the segment that encodes the third of the recombinant T cell module antigens comprises a sequence having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 38 or SEQ ID NO: 124; or (b) the first of the recombinant T cell module antigens has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 33; the second of the recombinant T cell module antigens has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO: 35; and the third of the recombinant T cell module antigens has at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to SEQ ID NO:

37.

16. The pharmaceutical composition of any of claims 12-15 comprising at least seven of the EBV antigen-encoding mRNA constructs; the fourth of the EBV antigen-encoding mRNA constructs comprising the segment that encodes an or the EBV gp42 antigen; the fifth of the EBV antigen- encoding mRNA constructs comprising the segment that encodes an or the EBV gH antigen; the sixth of the EBV antigen-encoding mRNA constructs comprising the segment that encodes an or the EBV gL antigen; and the seventh of the EBV antigen-encoding mRNA constructs comprising the segment that encodes an or the EBV gp220 antigen.Attorney Docket No: 70488WO01 17. The pharmaceutical composition of any of the preceding claims, each of the EBV antigen- encoding mRNA constructs further comprising a 5’ cap nucleoside, a first 5’ ribonucleoside, and a triphosphate bridge; and the 5’ cap nucleoside being linked 5’-to-5’ to the first 5’ ribonucleoside by the triphosphate bridge.

18. The pharmaceutical composition of claim 17, the first 5’ ribonucleoside comprising a 2’ methylated ribose.

19. The pharmaceutical composition of claim 17 or claim 18, the ‘5 cap nucleoside being a 7- methylguanosine, a 7-methyl-, 3’-O-methylguanosine, or a 7-methyl-, 2’-O-methylguanosine.

20. The pharmaceutical composition of any of the preceding claims, each of the EBV antigen- encoding mRNA constructs further comprising a 5’ untranslated region (UTR), a 3’ UTR, and a 3’ poly(adenosine monophosphate) (poly(A)) tail; the 5’ UTR being 5’ of the segment that encodes the EBV antigen; the 3’ UTR being 3’ of the segment that encodes the EBV antigen; and the 3’ poly(A) tail being 3’ of the 3’ UTR.

21. The pharmaceutical composition of claim 20, at least one, or each, of the 5’ UTRs having at least 95% sequence identity to SEQ ID NO: 48, SEQ ID NO: 50, or SEQ ID NO:

52.

22. The pharmaceutical composition of claim 20 or claim 21, at least one, or each, of the 3’ UTRs having at least 95% sequence identity to SEQ ID NO: 49, SEQ ID NO: 51, or SEQ ID NO:

53.

23. The pharmaceutical composition of claim 22, the first of the EBV antigen-encoding mRNA constructs of claim 15 having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 74, 75, 76, 138, 139, or 140; the second of the EBV antigen- encoding mRNA constructs of claim 15 having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 78, 79, 80, 141, 142, or 143; the third of the EBV antigen-encoding mRNA constructs of claim 15 having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 82, 83, 84, 144, 145, or 146.

24. The pharmaceutical composition of claim 22 or claim 23, the fourth of the EBV antigen- encoding mRNA constructs of claim 16 having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 66, 67, 68, 153, 154, or 155; the fifth of the EBV antigen-encoding mRNA constructs of claim 16 having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 58, 59, 60, 147, 148, or 149; the sixth of the EBV antigen-encoding mRNA constructs of claim 16 having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 62, 63, 64, 150, 151, or 152; and / or the seventh of the EBV antigen-encoding mRNA constructs of claim 16 having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 70, 71, 72, 156, 157, or 158.Attorney Docket No: 70488WO01 25. The pharmaceutical composition of claim 22, the first of the EBV antigen-encoding mRNA constructs of claim 10 having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 89, 90, 91, 132, 133, or 134; the second of the EBV antigen- encoding mRNA constructs of claim 10 having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 92, 93, 94, 135, 136, or 137.

26. The pharmaceutical composition of claim 22 or claim 25, the third of the EBV antigen-encoding mRNA constructs of claim 11 having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 66, 67, 68, 153, 154, or 155; the fourth of the EBV antigen-encoding mRNA constructs of claim 11 having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 58, 59, 60, 147, 148, or 149; the fifth of the EBV antigen-encoding mRNA constructs of claim 11 having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 62, 63, 64, 150, 151, or 152; and / or the sixth of the EBV antigen-encoding mRNA constructs of claim 11 having at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity to: SEQ ID NO: 70, 71, 72, 156, 157, or 158.

27. The pharmaceutical composition of any of the preceding claims, at least one, or each, of the at least two EBV antigen-encoding mRNA constructs comprising a modified nucleotide; wherein, optionally, the modified nucleotide includes a N1-methylpseudouridine.

28. The pharmaceutical composition of any of the preceding claims, the lipids comprising an ionizable cationic lipid, a sterol (e.g. cholesterol), and a polymer-conjugated lipid.

29. The pharmaceutical composition of claim 28, the polymer-conjugated lipid being a poly(ethylene glycol)-conjugated (PEG-conjugated) lipid.

30. The pharmaceutical composition of any of the preceding claims, the lipids comprising a zwitterionic lipid or a neutral lipid.

31. The pharmaceutical composition of any of claims 28-30, the ionizable cationic lipid comprising a tertiary amine.

32. The pharmaceutical composition of any of claims 28-31, the ionizable cationic lipid having a pKa from 6.1 to 7.0; from 6.1 to 6.5; from 6.5 to 7.0; from 6.2 to 6.4; and from 6.6 to 6.

9.

33. The pharmaceutical composition of any of claims 28-32, the lipids having a pKa from 5.8 to 7.0; from 5.9 to 6.2; and from 6.6 to 6.

9.

34. The pharmaceutical composition of any of claims 28-33, the lipids comprising from 35 mole% to 50 mole% sterol (e.g. cholesterol).

35. The pharmaceutical composition of any of claims 29-34, the lipids comprising from 0.5 mole% to 5 mole% PEG-conjugated lipid, from 0.6 mole% to 4 mole% PEG-conjugated lipid, from 0.7Attorney Docket No: 70488WO01 mole% to 3 mole% PEG-conjugated lipid, or from 0.8 mole% to 2.6 mole% PEG-conjugated lipid.

36. The pharmaceutical composition of any of claims 28-35, the lipids comprising from 5 mole% to 20 mole% zwitterionic lipid, from 8 mole% to 15 mole% zwitterionic lipid, or from 9 mole% to 12 mole% zwitterionic lipid.

37. The pharmaceutical composition of any of claims 1-36 for use as a medicament.

38. The pharmaceutical composition of any of claims 1-36 for use in the treatment of a disease caused by EBV infection.

39. The pharmaceutical composition of any of claims 1-36 for use in the treatment of multiple sclerosis.

40. The pharmaceutical composition of any of claims 1-36 for use in the treatment of post- transplant lymphoproliferative disorder.

41. The pharmaceutical composition of any of claims 1-36 for use in the treatment of cancers, such as gastric carcinoma, nasopharyngeal carcinoma, and lymphoma.

42. A method of manufacturing the pharmaceutical composition of any of claims 1-36, the method comprising: a. admixing the at least two EBV antigen-encoding mRNA constructs with an aqueous buffer, thereby obtaining an aqueous EBV antigen-encoding mRNA construct solution; b. admixing the lipids in an organic solvent, thereby obtaining a lipid solution; c. admixing the lipid solution and the aqueous EBV antigen-encoding mRNA construct solution with at least a T-mixer, a microfluidics mixer, or an impinging jet mixer, thereby obtaining a first admixture, wherein the first admixture comprises the LNPs, wherein at least some of at least two EBV antigen-encoding mRNA constructs are encapsulated in the LNPs; and d. purifying the LNPs to obtain the encapsulation by the lipids of the at least 50 mass %, at least 75 mass% of, at least 80 mass%, at least 85 mass%, at least 90 mass%, or at least 95 mass% of the at least two EBV antigen-encoding mRNA constructs.

43. A method of manufacturing the pharmaceutical composition of any of claims 1-36, the method comprising: a. admixing at least a first of the at least two EBV antigen-encoding mRNA constructs with an aqueous buffer, thereby obtaining a first aqueous EBV antigen-encoding mRNA construct solution; b. admixing the lipids in an organic solvent, thereby obtaining a first lipid solution;Attorney Docket No: 70488WO01 c. admixing the first lipid solution and the first aqueous EBV antigen-encoding mRNA construct solution with at least a T-mixer, a microfluidics mixer, or an impinging jet mixer, thereby obtaining a first admixture, wherein the first admixture comprises a first LNPs of the LNPs, wherein the at least the first of the at least two EBV antigen-encoding mRNA constructs are encapsulated in the first LNPs of the LNPs; d. admixing at least a second of the at least two EBV antigen-encoding mRNA constructs with the aqueous buffer, thereby obtaining a second aqueous EBV antigen-encoding mRNA construct solution; e. admixing the lipids in the organic solvent, thereby obtaining a second lipid solution; f. admixing the second lipid solution and the second aqueous EBV antigen-encoding mRNA construct solution with at least a T-mixer, a microfluidics mixer, or an impinging jet mixer, thereby obtaining a second admixture, wherein the second admixture comprises a second LNPs of the LNPs, wherein the at least the second of the at least two EBV antigen- encoding mRNA constructs are encapsulated in the second LNPs of the LNPs; g. admixing the first admixture and the second admixture and purifying the first LNPs and second LNPs to obtain the encapsulation by the lipids of the at least 50 mass %, at least 75 mass% of, at least 80 mass%, at least 85 mass%, at least 90 mass%, or at least 95 mass% of the at least two EBV antigen-encoding mRNA constructs.

44. The method of claim 42 or claim 43, the purifying comprising a dialysis, a cross-flow filtration, a tangential flow filtration, or an ultra filtration.

45. The method of any of claims 45-47, the aqueous buffer comprising a citrate buffer or an acetate buffer and / or the organic solvent comprising an alcohol solution, such as from 70 volume % to 99 volume % ethanol.

46. The method of claim 43, in (g), the admixing of the first admixture and the second admixture being before the purifying.

47. The method of claim 43, in (g), the purifying being before the admixing of the first admixture and the second admixture.

48. The method of claims 42-47, the first of the at least two EBV antigen-encoding mRNA constructs encoding the B cell module antigen, and thereby the first of the at least two EBV antigen-encoding mRNA constructs comprising the segment that encodes the B cell module antigen; the second of the at least two EBV antigen-encoding mRNA constructs encoding the T cell module antigens, and thereby the second of the at least two EBV antigen-encoding mRNA constructs comprising the segment that encodes the T cell module antigens.

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