Methods and reagents for treating or preventing ebv

Abstract

The present disclosure relates to Epstein-Barr Virus (EBV) (human herpesvirus 4) antigens. Specifically, proteins and uses thereof, and self-amplifying mRNA (sa-mRNA) encoding an EBV antigen and uses thereof. The present disclosure relates to vaccines and therapeutic agents, and production and uses thereof.

Description

[0001]METHODS AND REAGENTS FOR TREATING OR PREVENTING EBV RELATED APPLICATIONS This application claims priority from US Patent Application No. 63 / 633,224 entitled “Methods and reagents for treating or preventing EBV (I)” filed on 12 April 2024, and US Patent Application No. 63 / 633,215 entitled “Methods and reagents for treating or preventing EBV (II)” filed on 12 April 2024, the entire contents of which are hereby incorporated by reference. SEQUENCE LISTING The present application is filed together with a Sequence Listing in electronic form. The entire contents of the Sequence Listing are hereby incorporated by reference. FIELD The present disclosure relates to Epstein-Barr Virus (EBV) (human herpesvirus 4) antigens. Specifically, proteins and uses thereof, and self-amplifying mRNA (sa- mRNA) encoding an EBV antigen and uses thereof. The present disclosure relates to vaccines and therapeutic agents, and production and uses thereof. BACKGROUND Epstein-Barr virus (EBV), also known as human (gamma)herpesvirus 4, is a member of the herpes virus family and one of the most common human viruses worldwide. EBV is an oncogenic, double-stranded DNA virus, EBV spreads most commonly through bodily fluids, primarily saliva, and infects EBV infects B cells of the immune system and epithelial cells. Once EBV’s initial lytic infection is brought under control, EBV latency persists in the individual's memory B cells for the rest of their life. EBV can cause infectious mononucleosis (glandular fever), illnesses of the nervous system and haematological system, and other conditions, including cancers and malignant diseases. Many people become infected with EBV in childhood. After EBV infection, the virus becomes latent, and can reactivate. EBV causes infectious mononucleosis and is also tightly linked to many malignant diseases. There is currently no approved vaccine for EBV. Consequently, there is a pressing need for new approaches to EBV vaccines, suitable for administration in early childhood, for preventing, treating, and delaying onset of EBV infection, and for reducing EBV viral load in an infected individual. SUMMARY The present disclosure is based on the inventors’ identification of protein sub- units of Epstein-Barr virus (EBV (human (gamma)herpes 4) that are suitable as a vaccine for the prevention and treatment of an EBV infection, including for administration to children or infants, as well as on the inventors’ identification of a self-amplifying RNA (sa-mRNA) comprising an antigen from an Epstein-Barr virus (EBV (human (gamma)herpes 4) that is suitable as a vaccine for the prevention and treatment of an EBV infection. The findings by the inventors provide the basis for reagents and methods useful for immunising subjects against EBV infections, e.g., vaccines. The findings also provide the basis for a sa-mRNA against an EBV antigen, and monovalent, bivalent and trivalent recombinant protein subunit vaccines, with one, two, or three antigenic epitopes against EBV, respectively. The findings also provide the basis for a monocistronic sa- mRNA against an EBV antigen, and a bicistronic sa-mRNA against two EBV antigens, and a multicistronic sa-mRNA against three or more EBV antigens. Furthermore, the findings by the inventors provide the basis for methods of treating or preventing or delaying progression of an EBV infection in a subject, including in a child or infant. Accordingly, the present disclosure provides a recombinant protein antigen or composition comprising the antigen, wherein the antigen is from an Epstein-Barr virus (EBV) and comprises at least one antigen selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220, or an antigenic fragment thereof. In one example, the recombinant protein antigen is gP350, or an antigenic fragment thereof. In one example, the antigen is gP42, or an antigenic fragment thereof. In one example, the antigen is gL, or an antigenic fragment thereof. In one example, the antigen is gH, or an antigenic fragment thereof. In one example, the antigen is gB, or an antigenic fragment thereof. In one example, the antigen is gP220, or an antigenic fragment thereof. In one example, the recombinant protein antigen or composition further comprises a second antigen selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220, or antigenic fragments thereof. For example, the second antigen is different to the first antigen, or antigenic fragment thereof. When discussing a recombinant protein antigen comprising two or more antigens, the recombinant protein antigen may be a fusion protein comprising the two or more antigens or may be a complex of the two or more proteins or may be a mixture of a fusion protein and a protein complex. In one example, the recombinant protein antigen is a fusion protein. In one example, the recombinant protein antigen is a protein complex. In one example, the first and second antigens, or antigenic fragments thereof, are pooled in one antigenic combination, e.g., in a composition. In one example, the first and second antigens, or antigenic fragments thereof, are joined by a linker. In one example, the recombinant protein antigen or composition comprises SEQ ID NO: 5 and SEQ ID NO: 6 or 44, or antigenic fragments thereof. In one example, the recombinant protein antigen or composition further comprises a third antigen selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220, or antigenic fragments thereof. For example, the first and second and third antigens are all different antigens, or antigenic fragments thereof. In one example, the first, second, and third antigens, or antigenic fragments thereof, are pooled in one antigenic combination. In one example, the second and third antigens, or antigenic fragments thereof, are pooled in one antigenic combination. In one example, the second and third antigens, or antigenic fragments thereof, are joined by a linker. In one example, the recombinant protein antigen or composition comprises one or more sequences as set forth in SEQ ID NOs: 1 to 7 or 40 to 45, or antigenic fragments thereof. In one example, the recombinant protein antigen or composition comprises two or more of the antigens set forth in SEQ ID NOs: 1 to 7 or 40 to 45, or an antigenic fragment thereof. In one example, the recombinant protein antigen or composition comprises three or more of the antigens set forth in SEQ ID NOs: 1 to 7 or 40 to 45, or antigenic fragments thereof. In one example, the recombinant protein antigen comprises SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41, or antigenic fragments thereof. In one example, the recombinant protein antigen or composition comprises SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41 and SEQ ID NO: 3 or 42, or antigenic fragments thereof. In one example, the recombinant protein antigen or composition comprises SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41 and SEQ ID NO: 4, or antigenic fragments thereof. In one example, the recombinant protein antigen or composition comprises SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41 and SEQ ID NO: 7, 43, or 45, or antigenic fragments thereof. In one example, the recombinant protein antigen or composition comprises SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41 and SEQ ID NO: 3 or 42 and SEQ ID NO: 7, 43, or 45, or antigenic fragments thereof. The present disclosure provides a protein subunit vaccine comprising any one of the recombinant protein antigens or antigenic fragments thereof disclosed herein. In one example, the protein subunit vaccine antigen comprises the amino acid sequences set forth in SEQ ID NO: 6 or 44, or an antigenic fragment thereof. In one example, the protein subunit vaccine antigen comprises the amino acid sequences set forth in SEQ ID NO: 7, 43, or 45, or an antigenic fragment thereof. In one example, the protein subunit vaccine antigen comprises the amino acid sequences set forth in SEQ ID NO: 1 or 40, or an antigenic fragment thereof. In one example, the protein subunit vaccine antigen comprises the amino acid sequences set forth in SEQ ID NO: 2 or 41, or an antigenic fragment thereof. In one example, the protein subunit vaccine antigen comprises the amino acid sequences set forth in SEQ ID NO: 4 or 5, or an antigenic fragment thereof. In one example, the protein subunit vaccine antigen comprises the amino acid sequences set forth in SEQ ID NO: 3 or 42, or an antigenic fragment thereof. The present disclosure also provides a sa-mRNA comprising a nucleotide sequence encoding an antigen operably linked to a subgenomic (SG) promoter, wherein the antigen is from an Epstein-Barr virus (EBV). In one example, the EBV antigen is selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220. The present disclosure also provides a monocistronic sa-mRNA comprising a nucleotide sequence encoding an antigen operably linked to a subgenomic promoter, wherein the antigen is from an EBV. In one example, the antigen is gP350. In one example, the antigen is gP42. In one example, the antigen is gL. In one example, the antigen is gH. In one example, the antigen is gB. In one example, the antigen is gP220. In one example, the SG promoter is a minimal or an extended promoter. In one example the SG promoter is a minimal promoter. In one example the SG promoter is anextended promoter. For example, the extended SG promoter is extended at the 5 endwith nucleotides occurring in a sequence encoding a non-structural protein (e.g., NSP4) of the RNA virus (e.g., an alphavirus). In one example, the extended SG promoter isextended at the 5 end with nucleotides occurring in a sequence encoding an alphavirusNSP4. The addition of nucleotides to the 5 end of the SG promoter sequence did notinterfere with expression of the non-structural protein and viral replicase, e.g., alphavirusNSP4. In one example, the SG promoter is extended with 12 bases at the 5 end.In one example, the SG promoter is encoded by a sequence comprising set forth in SEQ ID NOs: 25, 26, and / or 35. The present disclosure also provides a bicistronic sa-mRNA comprising a first nucleotide sequence encoding a first antigen operably linked to a subgenomic (SG) promoter; and a second nucleotide sequence encoding a second antigen operably linked to a second SG promoter, wherein the first and second antigens are from an Epstein-Barr virus. In one example, the first and second EBV antigens are selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220. In one example, the first and second antigens are selected from the pair of gL and gH, for example, the first and second antigens are gl and gH or gH and gL. In one example, the first and second antigens are selected from the pair of gB and gP220. In one example, the SG promoter is a minimal or an extended promoter or a combination of both a minimal and an extended SG promoter. For example, the first SG promoter is a minimal SG promoter and the second SG promoter is an extended SG promoter. In one example, the bicistronic sa-mRNA comprises, in order from 5 to 3 : a firstnucleotide sequence encoding a first antigen operably linked to a minimal SG promoter; and a second nucleotide sequence encoding a second antigen operably linked to a minimal SG promoter; or a first nucleotide sequence encoding a first antigen operably linked to a minimal SG promoter; and a second nucleotide sequence encoding a second antigen operably linked to an extended SG promoter; or a first nucleotide sequence encoding a first antigen operably linked to an extended SG promoter; and a second nucleotide sequence encoding a second antigen operably linked to an extended SG promoter. In one example, the bicistronic sa-mRNA comprises, in order from 5 to 3 : a firstnucleotide sequence encoding gL operably linked to a SG promoter; and a second nucleotide sequence encoding gH operably linked to a SG promoter; or a first nucleotide sequence encoding gB operably linked to a SG promoter; and a second nucleotide sequence encoding gP220 operably linked to a SG promoter; or a first nucleotide sequence encoding gP220 operably linked to a SG promoter, and a second nucleotide sequence encoding gB operably linked to a SG promoter. The present disclosure also provides a multicistronic sa-mRNA comprising a first nucleotide sequence encoding a first antigen operably linked to a subgenomic (SG) promoter; and a second nucleotide sequence encoding a second antigen operably linked to a second SG promoter; and a third nucleotide sequence encoding a third antigen operatively linked to a third SG promoter, wherein the first and second and third antigens are from an Epstein-Barr virus. In one example, the first and second and third EBV antigens are selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220. In one example, the first and second and third antigens are selected from gL, gH and gP42. For example, the first antigen is gL, the second antigen is gH and the third antigen is gP42. In one example, the first and second and third antigens are selected from gL, gH, and gB. For example, the first antigen is gL, the second antigen is gH and the third antigen is gB. In one example, the first and second and third antigens are selected from gL, gH, and gP220. . For example, the first antigen is gL, the second antigen is gH and the third antigen is gP220. The present disclosure also provides a multicistronic sa-mRNA comprising a first nucleotide sequence encoding a first antigen operably linked to a subgenomic (SG) promoter; and a second nucleotide sequence encoding a second antigen operably linked to a second SG promoter; and a third nucleotide sequence encoding a third antigen operatively linked to a third SG promoter; and a fourth nucleotide sequence encoding a fourth antigen operatively linked to a fourth SG promoter, wherein the first and second and third and fourth antigens are from an Epstein-Barr virus. In one example, the first and second and third and fourth EBV antigens are selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220. In one example, the first and second and third and fourth antigens are selected from gL, gH, gP42 and gP220. For example, the first antigen is gL, the second antigen is gH, the third antigen is gP42, and the fourth antigen is gP220. In one example, the SG promoter is a minimal or an extended promoter or a combination of both minimal and extended SG promoters. For example, the first SG promoter is a minimal SG promoter and the second SG promoter is an extended SG promoter and the third SG promoter is an extended SG promoter. In one example, the SG promoter is a minimal or an extended promoter or a combination of both minimal and extended SG promoters. For example, the first SG promoter is a minimal SG promoter and the second SG promoter is an extended SG promoter and the third SG promoter is an extended SG promoter and the fourth SG promoter is an extended SG promoter. In one example, the multicistronic sa-mRNA comprises one or more additional nucleotide sequences, wherein each sequence encodes an additional EBV antigen operably linked to a SG promoter, and wherein the one or more nucleotide sequences arelocated 3 of the third nucleotide sequence.In one example, the multicistronic sa-mRNA comprises, in order from 5 to 3 : afirst nucleotide sequence encoding gL operably linked to a SG promoter; a second nucleotide sequence encoding gH operably linked to a SG promoter; and a third nucleotide sequence encoding gP42 operably linked to a SG promoter. In one example, the multicistronic sa-mRNA comprises, in order from 5 to 3 : afirst nucleotide sequence encoding gL operably linked to a SG promoter; a second nucleotide sequence encoding gH operably linked to a SG promoter; and a third nucleotide sequence encoding gB operably linked to a SG promoter. In one example, the multicistronic sa-mRNA comprises, in order from 5 to 3 : afirst nucleotide sequence encoding gL operably linked to a SG promoter; a second nucleotide sequence encoding gH operably linked to a SG promoter; and a third nucleotide sequence encoding gP220 operably linked to a SG promoter. In one example, the multicistronic sa-mRNA comprises, in order from 5 to 3 : afirst nucleotide sequence encoding gL operably linked to a SG promoter; a second nucleotide sequence encoding gH operably linked to a SG promoter; and a third nucleotide sequence encoding gP42 operably linked to a SG promoter; and a fourth nucleotide sequence encoding g220 operably linked to a SG promoter. In some examples, the EBV antigen is encoded by a sequence set forth in any one of SEQ ID NOs: 9 to 14. In one example, the antigen from an EBV comprises a polynucleotide sequence having at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 90% at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99% or 100% identity to any one of SEQ ID NOs: 9 to 14. In one example, the antigen from an EBV is encoded by a polynucleotide sequence having at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 90% at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99% or 100% identity to any one of SEQ ID NOs: 15 to 20. In some examples, the nucleotide sequence encoding the antigen is codon optimised. In some examples, the nucleotide sequence encoding the antigen is a wild- type sequence. In some examples, gB furin cleavage site in aa 427–434 LRRRRDA (SEQ ID NO: 37) is stabilised, for example, the sequence is mutated such that it cannot be cleaved by furin or is deleted in whole or in part. For example, the gB antigen is fusion stabilised. In some examples, the antigen is a subunit antigen. For example, the EBV antigen is a subunit of gP220. In some examples, the sa-mRNA comprises native non-structural proteins (NSPs)1–4. For example, the NSPs1–4 are native to the RNA virus from which it is derived and / or based on (e.g., an alphavirus). In one example, the NSP1–4 are native alphavirus NSP1–4. In one example, the nucleotide sequences encoding non-structural proteins (NSPs) comprise a sequence set forth in any one of SEQ ID NOs: 21 to 26. In one example, the nucleotide sequence encoding a NSP1 comprises or consists of a sequence set forth in SEQ ID NO: 21. In one example, the nucleotide sequence encoding a NSP2 comprises or consists of a sequence set forth in SEQ ID NO: 22. In one example, the nucleotide sequence encoding a NSP3 comprises or consists of a sequence set forth in SEQ ID NO: 23. In one example, the nucleotide sequence encoding a NSP4 comprises or consists of a sequence set forth in SEQ ID NO: 24. In one example, the sa-mRNA comprises, or consists, of NSP1–4 wherein the NSP1–4 are encoded by a nucleotide sequence comprising or consisting of SEQ ID NOs: 21 to 26. In some examples, the SG promoter is a native SG promoter. For example, a native SG promoter is a promoter that is native to the RNA virus from which it is derived and / or based on (e.g., an alphavirus). In one example, the native SG promoter is a native alphavirus SG promoter. In one example, the native SG promoter is a minimal SG promoter. For example, the minimal SG promoter is the minimal sequence required for initiation of transcription. In one example, the minimal native SG promoter comprises or consists of a sequence set forth in SEQ ID NO: 35. In one example, the 5 UTR is a 5 UTR of a Venezuelan equine encephalitis virus(VEEV) or modified forms thereof. For example, the 5 UTR comprises a sequence setforth in SEQ ID NO: 38. In one example, the 5 -UTR, the fragment and / or the variant thereof is between30 and 200 nucleotides in length. For example, the 5 UTR, the fragment, and / or thevariant thereof is between 30 and 50 nucleotides in length. For example, the 5 UTR, thefragment, and / or the variant thereof is between 40 and 50 nucleotides in length. Forexample, the 5 UTR, the fragment, and / or the variant thereof is between 40 and 60nucleotides in length. For example, the 5 UTR, the fragment, and / or the variant thereofis between 50 and 75 nucleotides in length. For example, the 5 UTR, the fragment, and / orthe variant thereof is between 75 and 100 nucleotides in length. For example, the 5 UTR,the fragment, and / or the variant thereof is between 100 and 125 nucleotides in length.For example, the 5 UTR, the fragment and / or the variant thereof is between 125 and 150nucleotides in length. For example, the 5 -UTR, the fragment, and / or the variant thereofis between 150 and 175 nucleotides in length. For example, the 5 -UTR, the fragment,and / or the variant thereof is between 175 and 200 nucleotides in length. In one example, the 5 UTR, the fragment and / or the variant thereof comprises anucleotide sequence at least 90% identical to a nucleotide sequence set forth in SEQ IDNO: 38. For example, the 5 UTR, the fragment and / or the variant thereof comprises anucleotide sequence 90%, or 91%, or 92%, or 93%, or 94%, or 95%, or 96%, or 97%, or 98%, or 99% identical to a nucleotide sequence set forth in SEQ ID NO: 38. In one example, the 3 UTR is a 3 UTR of a Sindbis virus (SINV) or modifiedforms thereof. For example, the 3 UTR comprises a sequence set forth in SEQ ID NO:39. In one example, the 3 UTR, the fragment and / or the variant thereof is between 40and 400 nucleotides in length. For example, the 3 UTR is between 40 and 50, or 50 and60, or 60 and 70, or 70 and 80, or 80 and 90, or 90 and 100, or 100 and 125, or 125 and 150, or 150 and 175, or 175 and 200, or 200 and 225, or 225 and 250, or 250 and 275, or 275 and 300, or 300 and 325, or 325 and 350, or 350 and 375, or 375 and 400 nucleotidesin length. For example, the 3 UTR, the fragment, and / or the variant thereof is between40 and 50 nucleotides in length. For example, the 3 UTR, the fragment, and / or the variantthereof is between 50 and 60 nucleotides in length. For example, the 3 UTR, thefragment, and / or the variant thereof is between 60 and 70 nucleotides in length. Forexample, the 3 UTR, the fragment, and / or the variant thereof is between 70 and 80nucleotides in length. For example, the 3 UTR, the fragment, and / or the variant thereofis between 80 and 90 nucleotides in length. For example, the 3 UTR, the fragment, and / orthe variant thereof is between 90 and 100 nucleotides in length. For example, the 3 UTR,the fragment, and / or the variant thereof is between 100 and 125 nucleotides in length.For example, the 3 UTR, the fragment, and / or the variant thereof is between 125 and 150nucleotides in length. For example, the 3 UTR, the fragment, and / or the variant thereofis between 150 and 175 nucleotides in length. For example, the 3 UTR, the fragmentand / or the variant thereof is between 175 and 200 nucleotides in length. For example, the3 UTR, the fragment, and / or the variant thereof is between 200 and 225 nucleotides inlength. For example, the 3 UTR, the fragment, and / or the variant thereof is between 225and 250 nucleotides in length. For example, the 3 UTR, the fragment, and / or the variantthereof is between 250 and 275 nucleotides in length. For example, the 3 -UTR, thefragment, and / or the variant thereof is between 275 and 300 nucleotides in length. Forexample, the 3 UTR, the fragment, and / or the variant thereof is between 300 and 325nucleotides in length. For example, the 3 UTR, the fragment and / or the variant thereof isbetween 325 and 350 nucleotides in length. For example, the 3 UTR, the fragment, and / orthe variant thereof is between 350 and 375 nucleotides in length. For example, the 3 UTR,the fragment, and / or the variant thereof is between 375 and 400 nucleotides in length. In one example, the polynucleotide comprises a nucleotide sequence comprisingone or more 3 tailing sequences located at the 3 end of the nucleotide sequencecomprising the 3 UTR. In one example, the one or more 3 tailing sequences are selectedfrom the group consisting of a poly-A sequence, polyadenylation signal, a G-quadruplex,a poly-C sequence, a stem loop and combinations thereof. For example, the 3 tailingsequence comprises a poly-A sequence. In one example, the 3 tailing sequencecomprises a polyadenylation signal. In one example, the 3 tailing sequence comprises aG-quadruplex. In one example, the 3 tailing sequence comprises a poly-C sequence. Inone example, the 3 tailing sequence comprises a stem loop. For example, the stem loopis a histone stem loop. In one example, the 3 tailing sequence comprises a poly-Asequence and a G-quadruplex. In one example, the 3 tailing sequence comprises a stemloop (e.g., a histone stem loop) and a poly-A sequence. In one example, the one or more 3 tailing sequences comprises one or more poly-A sequences each comprising between 10 and 300 consecutive adenosine nucleotides. For example, the poly-A sequences each comprises between 10 and 20, or 20 and 30, or 30 and 40, or 40 and 50, or 50 and 60, or 60 and 70, or 70 and 80, or 80 and 90, or 90 and 100, or 100 and 125, or 125 and 150, or 150 and 175, or 175 and 200, or 200 and 225, or 225 and 250, or 250 and 275, or 275 and 300 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprises between 10 and 20 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprises between 20 and 30 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprises between 30 and 40 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprise 36 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprises between 40 and 50 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprises between 50 and 60 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprises between 60 and 70 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprises between 70 and 80 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprises between 80 and 90 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprises between 90 and 100 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprises between 100 and 125 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprises between 125 and 150 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprises between 150 and 175 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprises between 175 and 200 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprises between 200 and 225 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprises between 225 and 250 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprises between 250 and 275 consecutive adenosine nucleotides. For example, the one or more poly-A sequences each comprises between 275 and 300 consecutive adenosine nucleotides. In one example, the poly-A sequence comprises 36 consecutive adenosine nucleotides. In one example, the poly-A sequence comprises 37 consecutive adenosine nucleotides. In one example, the sa-mRNA comprises a 5-UTR, fragment, and / or variant thereof; a SG promoter; a nucleotide sequence encoding an antigen from an EBV; a3 UTR, fragment, and / or variant thereof; and one or more 3 tailing sequences.In one example, the sa-mRNA comprises, from 5 to 3 , a 5 UTR, fragment, and / orvariant thereof; a SG promoter; a nucleotide sequence encoding an antigen from an EBV;a 3 UTR, fragment, and / or variant thereof; and one or more 3 tailing sequences.In one example, the sa-mRNA further comprises a 5 terminal cap structure.In one example, the 5 terminal cap structure is an endogenous cap or analoguethereof. For example, the 5 terminal cap structure is an endogenous cap. For example,the 5 terminal cap structure is an analogue of an endogenous cap.In one example, the 5 terminal cap structure comprise a guanine or guanineanalogue thereof. For example, the 5 terminal cap structure comprise a guanine. Forexample, the 5 terminal cap structure comprise a guanine analogue of a guanine.In one example, the 5 terminal cap structure is selected from a group consistingof anti-reverse cap analogue (ARCA), N7,2’-0-dimethyl-guanosine (mCAP), inosine,N1-methyl-guanosine, 2 fluoro-guanosine, 7-deaza-guanosine, 8-oxo-guanosine, 2-amino-guanosine, LNA-guanosine, 2-azido-guanosine, N6,2’-O-dimethyladenosine, 7-methylguanosine (m7G), Cap1, and Cap2. For example, the 5 terminal cap structure isCap1. For example, the 5 terminal cap structure is Cap2.In one example, the 5 terminal cap structure is linked to the 5 end of the sa-mRNA by a 5 -5 -triphosphate linkage or a 5 -5 phosphorothioate linkage. For example,the 5 terminal cap structure is linked to the 5 end of the sa-mRNA by a 5 -5 -triphosphatelinkage. For example, the 5 terminal cap structure is linked to the 5 end of the sa-mRNAby a 5 -5 phosphorothioate linkage.In one example, the sa-mRNA is from an alphavirus. For example, the alphavirus is selected from the group consisting of Semliki Forest virus (SFV), Sindbis virus (SIN), and Venezuelan equine encephalitis virus (VEEV) and combinations thereof. In one example, the sa-mRNA is from a Semliki Forest virus (SFV). In one example, the sa-mRNA is from a Sindbis virus (SIN). In one example, the sa-mRNA is from a Venezuelan equine encephalitis virus (VEEV). In one example, the present disclosure provides a sa-mRNA comprising a sequence set forth in any one or more of SEQ ID NOs: 15 to 20. For example, the sa- mRNA comprises a sequence set forth in SEQ ID NO 15. For example, the sa-mRNA comprises a sequence set forth in SEQ ID NO 16. For example, the sa-mRNA comprises a sequence set forth in SEQ ID NO 17. For example, the sa-mRNA comprises a sequence set forth in SEQ ID NO 18. For example, the sa-mRNA comprises a sequence set forth in SEQ ID NO 19. For example, the sa-mRNA comprises a sequence set forth in SEQ ID NO 20. In one example, the present disclosure provides a sa-mRNA encoded by a sequence set forth in any one of to 34. For example, the sa-mRNA is encoded by a sequence set forth For example, the sa-mRNA is encoded by a sequence set forth For example, the sa-mRNA is encoded by a sequence set forth 29. For example, the sa-mRNA is encoded by a sequence set forth For example, the sa-mRNA is encoded by a sequence set forth 31. For example, the sa-mRNA is encoded by a sequence set forth 32, For example, the sa-mRNA is encoded by a sequence set forth 33. For example, the sa-mRNA is encoded by a sequence set forth in In one example, the present disclosure provides a polynucleotide encoding the sa- mRNA of the disclosure. In one example, the polynucleotide is RNA. In one example, the polynucleotide is a recombinant DNA, for example a plasmid. In one example, the plasmid comprises a sequence set forth in any one of SEQ ID NOs: 27 to 34. For example, the plasmid comprises a sequence set forth in SEQ ID NO: 27. For example, the plasmid comprises a sequence set forth in SEQ ID NO: 28. For example, the plasmid comprises a sequence set forth in SEQ ID NO: 29. For example, the plasmid comprises a sequence set forth in SEQ ID NO: 30. For example, the plasmid comprises a sequence set forth in SEQ ID NO: 31. For example, the plasmid comprises a sequence set forth in SEQ ID NO: 32. For example, the plasmid comprises a sequence set forth in SEQ ID NO: 33. For example, the plasmid comprises a sequence set forth in SEQ ID NO: 34. The present disclosure also provides a nanoparticle comprising the sa-mRNA or the polynucleotide of the disclosure. The present disclosure provides a monovalent protein subunit vaccine comprising any one of recombinant EBV antigens selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220, or antigenic fragments thereof. In one example, the monovalent protein subunit vaccine comprises recombinant antigen gP350, or an antigenic fragment thereof. In one example, the monovalent protein subunit vaccine comprises recombinant antigen gB, or an antigenic fragment thereof. In one example, the monovalent protein subunit vaccine comprises recombinant antigen P42, or an antigenic fragment thereof. In one example, the monovalent protein subunit vaccine comprises recombinant antigen gH, or an antigenic fragment thereof. In one example, the monovalent protein subunit vaccine comprises recombinant antigen gL, or an antigenic fragment thereof. In one example, the monovalent protein subunit vaccine comprises recombinant antigen gP220, or an antigenic fragment thereof. In one example, the monovalent protein subunit vaccine antigen comprises one of the amino acid sequences set forth in SEQ ID NOs: 1 to 7 or 40 to 45, or antigenic fragments thereof. The present disclosure provides a bivalent protein subunit vaccine comprising any two of recombinant EBV antigens, or antigenic fragments thereof, selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220, or antigenic fragments thereof. In one example, the bivalent protein subunit vaccine comprises recombinant antigens gH and gL, or antigenic fragments thereof. In one example, the bivalent protein subunit vaccine comprises recombinant antigens gB and gP220, or antigenic fragments thereof. In one example, the bivalent protein subunit vaccine comprises a first EBV antigen selected from the group comprising gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments thereof, and a second EBV antigen selected from the group comprising gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments thereof, wherein the individual antigens are mixed together in a single antigenic combination. For example, the bivalent protein antigenic combination comprises pooled gH and gL, or antigenic fragments thereof. For example, the bivalent protein antigenic combination comprises pooled gB and gP220, or antigenic fragments thereof. In one example, the bivalent protein subunit vaccine comprises a first EBV antigen selected from the group comprising gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments tehreof, a linker, and a second EBV antigen selected from the group comprising gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments thereof, wherein the linker joins the first and second EBV antigen or antigenic fragment thereof. For example, the bivalent protein subunit vaccine antigen comprises gH, or an antigenic fragment thereof, joined to gL, or an antigenic fragment thereof, by a linker. For example, the bivalent protein antigen comprises gB, or an antigenic fragment thereof, joined to gP220, or an antigenic fragment thereof, by a linker. In one example, the bivalent protein subunit vaccine antigen comprises two of the amino acid sequences set forth in SEQ ID NOs: 1 to 7 or 40 to 45, or antigenic fragments thereof. In one example, the bivalent protein subunit vaccine antigen comprises antigens gH and gL, or antigenic fragments thereof. In one example, bivalent protein subunit vaccine antigen comprises the amino acid sequences SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41, or antigenic fragments thereof. In one example, the bivalent protein subunit vaccine antigen comprises antigens gB and gp220, or antigenic fragments thereof. In one example, bivalent protein subunit vaccine antigen comprises the amino acid sequences SEQ ID NO: 4 or 5 and SEQ ID NO: 7, 43, or 45, or antigenic fragments thereof. The present disclosure provides a trivalent protein subunit vaccine comprising any three of recombinant EBV antigens selected from the group comprising: gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments thereof. In one example, the trivalent protein subunit vaccine comprises recombinant antigens gH, gL, and gP42, or antigenic fragments thereof. In one example, the trivalent protein subunit vaccine comprises recombinant antigens gH, gL, and gP220, or antigenic fragments thereof. In one example, the trivalent protein subunit vaccine antigen comprises three of the amino acid sequences set forth in SEQ ID NOs: 1 to 7 or 40 to 45, or antigenic fragments thereof. In one example, the trivalent protein subunit vaccine comprises a first EBV antigen selected from the group comprising gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments thereof, and a second EBV antigen selected from the group comprising gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments thereof, and a third EBV antigen selected from the group comprising gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments thereof, wherein the individual antigens are mixed together in a single antigenic combination. For example, the trivalent protein antigenic combination comprises pooled gL, gH, and gB, or antigenic fragments thereof. For example, the trivalent protein antigenic combination comprises pooled gL, gH, and gP220, or antigenic fragments thereof. For example, the trivalent protein antigenic combination comprises pooled gL, gH, and gP220, or antigenic fragments thereof. In one example, the trivalent protein antigen comprises a first EBV antigen, or antigenic fragment thereof, selected from the group comprising gP350; gP42; gL; gH; gB; and gP220, or antigenic fragments thereof, a linker, and a second EBV antigen, or antigenic fragment thereof, selected from the group comprising gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments thereof, wherein the linker joins the first and second EBV antigen, or antigenic fragments thereof, and further comprises a third EBV antigen, selected from the group comprising gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments thereof, and conjugated to the second EBV antigen, or antigenic fragment thereof, for example by a linker. In one example, the first and second and third antigens are selected from gL, gH and gB, or antigenic fragments thereof. For example, the first antigen is gL, or antigenic fragment thereof, the second antigen is gH, or antigenic fragment thereof, and the third antigen is gB, or antigenic fragment thereof. In one example, the trivalent protein subunit vaccine comprises recombinant antigens gL, gH, and gP42, or antigenic fragments thereof. For example, the first antigen is gL, or antigenic fragment thereof, the second antigen is gH, or antigenic fragment thereof, and the third antigen is gP42, or antigenic fragment thereof. In one example, the first and second and third antigens are selected from gL, gH and gP220, or antigenic fragments thereof. For example, the first antigen is gL, or antigenic fragment thereof, the second antigen is gH, or antigenic fragment thereof, and the third antigen is gP220, or antigenic fragment thereof. In one example, the trivalent protein subunit vaccine comprises recombinant antigens gL, gH, and gP220, or antigenic fragments thereof. In one example, the first and second and third antigens are selected from gL, gH and gP42, or antigenic fragments thereof. For example, the first antigen is gL, or antigenic fragment thereof, the second antigen is gH, or antigenic fragment thereof, and the third antigen is gP42, or antigenic fragment thereof. In one example, the trivalent protein subunit vaccine comprises recombinant antigens gL, gH, and gP42, or antigenic fragments thereof. The present disclosure provides a multivalent protein subunit vaccine comprising any four of recombinant EBV antigens selected from the group comprising: gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments thereof. In one example, the multivalent protein subunit vaccine comprises recombinant antigens gH, gL, gP42, and gP220, or antigenic fragments thereof. In one example, the multivalent protein subunit vaccine antigen comprises four of the amino acid sequences set forth in SEQ ID NOs: 1 to 7 or 40 to 45, or antigenic fragments thereof. In one example, the trivalent protein subunit vaccine comprises a first EBV antigen selected from the group comprising gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments thereof, and a second EBV antigen selected from the group comprising gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments thereof, and a third EBV antigen selected from the group comprising gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments thereof, and a fourth EBV antigen selected from the group comprising gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments thereof, wherein the individual antigens are mixed together in a single antigenic combination. For example, the multivalent protein antigenic combination comprises pooled gL, gH, gP42, and gP220, or antigenic fragments thereof. In one example, the multivalent protein antigen comprises a first EBV antigen, or antigenic fragment thereof, selected from the group comprising gP350; gP42; gL; gH; gB; and gP220, or antigenic fragments thereof, a linker, and a second EBV antigen, or antigenic fragment thereof, selected from the group comprising gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments thereof, wherein the linker joins the first and second EBV antigen, or antigenic fragments thereof, and further comprises a third EBV antigen, selected from the group comprising gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments thereof, and conjugated to the second EBV antigen, or antigenic fragment thereof, for example by a linker, and further comprises a fourth EBV antigen, selected from the group comprising gP350, gP42, gL, gH, gB, and gP220, or antigenic fragments thereof, and conjugated to the third EBV antigen, or antigenic fragment thereof, for example by a linker. In one example, the first and second and third and fourth antigens are selected from gL, gH and gB, or antigenic fragments thereof. For example, the first antigen is gL, or antigenic fragment thereof, the second antigen is gH, or antigenic fragment thereof, the third antigen is gp42, or antigenic fragment thereof, and the fourth antigen is gP220, or antigenic fragment thereof. In one example, the multivalent protein subunit vaccine comprises recombinant antigens gL, gH, gP42, and gP220, or antigenic fragments thereof. In some examples, the protein subunit vaccine comprises a protein subunit as set forth in any one of SEQ ID NOs: 1 to 7 or 40 to 45, or antigenic fragments thereof. In some examples, the protein subunit vaccine comprises a protein subunit as set forth in any two of SEQ ID NOs: 1 to 7 or 40 to 45, or antigenic fragments thereof. In some examples, the protein subunit vaccine comprises a protein subunit as set forth in any three of SEQ ID NOs: 1 to 7 or 40 to 45, or antigenic fragments thereof. In some examples, the protein subunit vaccine comprises a protein subunit as set forth in any four of SEQ ID NOs: 1 to 7 or 40 to 45, or antigenic fragments thereof. In one example, the protein subunit vaccine comprises a sequence having at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 90% at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99% or 100% identity to any one of SEQ ID NOs: 1 to 7 or 40 to 45. In one example, the protein subunit vaccine comprises a protein subunit encoded by a polynucleotide sequence. In some examples, the nucleotide sequence encoding the antigen is codon optimised. In some examples, the nucleotide sequence encoding the antigen is a wild- type sequence. In some examples, gB furin cleavage site in aa 427–434 LRRRRDA (SEQ ID NO: 8) is stabilised, for example, the sequence is mutated such that it cannot be cleaved by furin or is deleted in whole or in part. For example, the gB antigen is fusion stabilised. In some examples the gB antigen of the protein subunit vaccine is a recombinant gB mutant. For example, the gB antigen is the recombinant gB mutant as set forth in SEQ ID NO: 5. In some examples, the gB mutant exchanges amino acids 112 (W) and 113 (Y) for H and R respectively. In some examples, the gB mutant exchanges amino acids 193–196 (WLIW) for RVEA. In some examples, the gB mutant exchanges amino acids 469 (R) and 470 (R) for P and P respectively. In some examples, the antigen is a subunit antigen. For example, the EBV antigen is a subunit of gP220. The present disclosure also provides an immunogenic composition comprising the sa-mRNA or the polynucleotide or the nanoparticle or the recombinant protein antigen or the protein subunit vaccine of the present disclosure. For example, the composition of the present disclosure, when administered, is capable of inducing an immune response in the subject. For example, administration of the composition induces a humoral immune response in the subject. For example, the humoral immune response is an antibody-mediated immune response. For example, administration of the composition induces a humoral and / or a cell-mediated immune response. For example, the humoral immune response is an antibody-mediated immune response. In another example, the composition induces a cell-mediated immune response. For example, the cell-mediated immune response includes activation of antigen-specific cytotoxic T cells. In one example, the immunogenic composition comprises a plurality of recombinant protein antigens and / or sa-mRNAs of the disclosure of the disclosure. For example, a plurality of different polypeptide antigen sequences. For example, each sa- mRNA encodes a different polypeptide antigen sequence. For example, the different polypeptide antigen sequences are from the same strain of the virus (e.g., encode antigens from the same EBV strain). In one example, the different polypeptide antigen sequences are from different strains of the same virus (e.g., encode an antigen from different strains of EBV). In one example, the polypeptide antigen sequences are from different strains of the virus (e.g., encode the same antigens from different EBV strains). In one example, the immunogenic composition further comprises an adjuvant. For example, the adjuvant is MF59. The skilled person will be aware of other suitable adjuvants, all of which are contemplated by the present disclosure. The present disclosure also provides a pharmaceutical composition comprising an immunogenic composition of the disclosure and a pharmaceutically acceptable carrier. Pharmaceutically acceptable carriers suitable for use in the present disclosure will be apparent to the skilled person and / or are described herein. In one example, the pharmaceutical composition further comprises a lipid-based carrier, a polymeric microparticle and / or an oil-in-water emulsion. For example, the sa- mRNA is contained in, or otherwise associated with a lipid-based carrier, a polymeric microparticle and / or an oil-in-water emulsion. In one example, the pharmaceutical composition comprises an adjuvant. In one example, the sa-mRNA is contained in, or otherwise associated with a lipid-based carrier. For example, the lipid-based carrier is, or comprises, a lipid nanoparticle (LNP). In one example, the pharmaceutical composition further comprises a LNP. For example, sa-mRNA is encapsulated in a LNP. In another example, the sa- mRNA is bound to a LNP. In a further example, the sa-mRNA is adsorbed on to a LNP. In another example, each sa-mRNA is formulated together in the LNP. In another example, each sa-mRNA is formulated separately in the LNP. The present disclosure also provides the immunogenic composition or the pharmaceutical composition of the disclosure for use as a vaccine. The present disclosure also provides the recombinant protein antigen, the immunogenic composition, the pharmaceutical composition, or the vaccine of the disclosure, for use in the treatment or prevention or delaying progression of an EBV infection or disease or condition caused by an EBV infection in a subject. The present disclosure also provides the nanoparticle, the immunogenic composition, the pharmaceutical composition, or the vaccine of the disclosure, for use in the treatment or prevention or delaying progression of an EBV infection or disease or condition caused by an EBV infection, or for inducing an immune response in a subject. The present disclosure provides the recombinant protein antigen, the immunogenic composition, the pharmaceutical composition, or the vaccine of the disclosure, for use in the treatment or prevention or delaying progression of an EBV infection or a disease or condition caused by EBV in a subject. The present disclosure further provides the recombinant protein antigen, the immunogenic composition, the pharmaceutical composition, or the vaccine of the disclosure, for use in inducing an immune response in a subject. The present disclosure provides the nanoparticle, the immunogenic composition, the pharmaceutical composition, or the vaccine of the disclosure, for use in the treatment or prevention or delaying progression of an EBV infection or a disease or condition caused by EBV in a subject. The present disclosure further provides the nanoparticle, the immunogenic composition, the pharmaceutical composition, or the vaccine of the disclosure, for use in inducing an immune response in a subject. The present disclosure also provides a method of treating or preventing or delaying progression of an EBV infection or a disease or condition caused by EBV infection in a subject or for inducing an immune response in a subject, the method comprising administering the recombinant protein antigen, the immunogenic composition, the pharmaceutical composition, or the vaccine of the disclosure to a subject in need thereof. The present disclosure further provides use of the recombinant protein antigen, the immunogenic composition, or the pharmaceutical composition of the present disclosure in the manufacture of a medicament for treating or preventing or delaying progression of a disease in a subject in need thereof, for example, an EBV infection or a disease or condition caused by an EBV infection, or for inducing an immune response in a subject in need thereof. In one example, the recombinant protein antigen, the immunogenic composition, the pharmaceutical composition, or the vaccine induces a humoral immune response in the subject. For example, the humoral immune response is an antibody-mediated immune response. For example, production of neutralising antibodies. The present disclosure also provides a method of treating or preventing or delaying progression of an EBV infection or a disease or condition caused by EBV infection in a subject or for inducing an immune response in a subject, the method comprising administering the nanoparticle, the immunogenic composition, the pharmaceutical composition, or the vaccine of the disclosure to a subject in need thereof. The present disclosure also provides a method of treating or preventing or delaying progression of an EBV infection, or disease or condition caused by EBV infection in a subject, the method comprising administering the nanoparticle, the immunogenic composition, the pharmaceutical composition, or the vaccine of the disclosure to a subject in need thereof. The present disclosure also provides a method of inducing an immune response in a subject, the method comprising administering the nanoparticle, the immunogenic composition, the pharmaceutical composition, or the vaccine of the disclosure to a subject in need thereof. The present disclosure further provides use of the sa-mRNA, the polynucleotide, the nanoparticle, the immunogenic composition, or the pharmaceutical composition of the present disclosure in the manufacture of a medicament for treating or preventing or delaying progression of an EBV infection or a disease or condition caused by an EBV infection or for inducing an immune response in a subject in need thereof. The present disclosure further provides use of the sa-mRNA, the polynucleotide, the nanoparticle, the immunogenic composition, or the pharmaceutical composition of the present disclosure in the manufacture of a medicament for treating or preventing or delaying progression of an EBV infection or a disease or condition caused by an EBV infection in a subject in need thereof. The present disclosure further provides use of the sa-mRNA, the polynucleotide, the nanoparticle, the immunogenic composition, or the pharmaceutical composition of the present disclosure in the manufacture of a medicament for inducing an immune response in a subject in need thereof. In one example, the sa-mRNA, the polynucleotide, the immunogenic composition, the pharmaceutical composition, the nanoparticle or the vaccine induces a humoral immune response in the subject. For example, the humoral immune response is an antibody-mediated immune response. For example, production of neutralising antibodies. In another example, the sa-mRNA, the polynucleotide, the immunogenic composition, the pharmaceutical composition, the nanoparticle or the vaccine induces a cell-mediated immune response. For example, the cell-mediated immune response includes activation of antigen-specific cytotoxic T cells. For example, the T cells are CD4 T cells and / or CD8 T cells. In one example, the T cells are CD4 T cells. In another example, the T cells are CD8 T cells. In a further example, the T cells are CD4 and CD8 T cells. In one example, administration of a sa-mRNA, the polynucleotide, the immunogenic composition, the pharmaceutical composition, the nanoparticle or the vaccine of the present disclosure induces a CD4 T cell mediated immune response. In one example, administration of a sa-mRNA, the polynucleotide, the immunogenic composition, the pharmaceutical composition, the nanoparticle or the vaccine of the present disclosure induces a CD8 T cell mediated immune response. In one example, administration of a sa-mRNA, the polynucleotide, the immunogenic composition, the pharmaceutical composition, the nanoparticle or the vaccine of the present disclosure induces a CD4 and a CD8 T cell mediated immune response. In one example, the present disclosure provides a method for reducing viral load in a subject having a viral infection comprising administering the recombinant protein antigen, sa-mRNA, the polynucleotide, the immunogenic composition, the nanoparticle, the pharmaceutical composition, or the vaccine of the present disclosure to a subject having a viral infection. For example, an EBV viral infection. For example, an active EBV infection. For example, a latent EBV infection. In one example, the present disclosure provides use of the recombinant protein antigen, sa-mRNA, the polynucleotide, the immunogenic composition, the pharmaceutical composition, the nanoparticle, or the vaccine of the present disclosure in the preparation of a medicament for reducing viral load in a subject having a viral infection. For example, a EBV viral infection. For example, an active EBV infection. For example, a latent EBV infection. In one example, the present disclosure provides the recombinant protein antigen, sa-mRNA, the polynucleotide, the immunogenic composition, the pharmaceutical composition, the nanoparticle, or the vaccine of the present disclosure for use in reducing viral load in a subject having an EBV viral infection. For example, an active EBV infection. For example, a latent EBV infection. In one example, the subject is a human of 18 years of age or older. In another example, the subject is a human of 10 years or older. In one example, the subject is a human of any age, for example, from about 1 month to 100 years old, e.g., from about 2 months to about 80 years old, from about 6 months of age to about 3 years old, from about 3 years to about 18 years old, from about 12 years to about 18 years old, from about 18 years to about 55 years old, from about 50 years to about 75 years old, from about 40 years to about 65 years old. In another example, the subject is a human from 2 years of age. In another example, subject is a human from 18 years of age, a human from 30 years of age, a human from 40 years of age, a human from 50 years of age, a human from 60 years of age, a human from 70 years of age, a human from 80 years of age or a human from about 90 years of age. In another example, the subject is an infant, e.g., less than 2 years of age, less than 18 months of age, less than 12 months of age, less than 6 months of age or less than 3 months of age. In another example, the subject is elderly, e.g., a human from 60 years of age, a human from 70 years of age, a human from 80 years of age or a human from about 90 years of age. Thus, in one example, there is provided a method of treating, preventing or delaying progress of an EBV infection or a disease or condition caused by an EBV infection in a child or infant, comprising administering the recombinant protein antigen, sa-mRNA, the polynucleotide, the immunogenic composition, the pharmaceutical composition, the nanoparticle, or the vaccine of the present disclosure to the child or infant. In another example, there is provided use of the recombinant protein antigen, sa- mRNA, the polynucleotide, the immunogenic composition, the pharmaceutical composition, the nanoparticle, or the vaccine of the present disclosure in the manufacture of a medicament for treating, preventing or delaying progress of an EBV infection or a disease or condition caused by an EBV infection in a child or an infant. In another example, there is provided the recombinant protein antigen, sa-mRNA, the polynucleotide, the immunogenic composition, the pharmaceutical composition, the nanoparticle, or the vaccine of the present disclosure for use in treating, preventing or delaying progress of an EBV infection or a disease or condition caused by an EBV infection in a child or an infant. In another example, there is provided a method of inducing an immune response to an EBV infection or a disease or condition caused by an EBV infection in a child or an infant. comprising administering the recombinant protein antigen, sa-mRNA, the polynucleotide, the immunogenic composition, the pharmaceutical composition, the nanoparticle, or the vaccine of the present disclosure to the child or infant. In another example, there is provided use of the recombinant protein antigen, sa- mRNA, the polynucleotide, the immunogenic composition, the pharmaceutical composition, the nanoparticle, or the vaccine of the present disclosure in the preparation of a medicament for inducing an immune response to an EBV infection or a disease or condition caused by an EBV infection in a child or an infant. In another example, there is provided the recombinant protein antigen, sa-mRNA, the polynucleotide, the immunogenic composition, the pharmaceutical composition, the nanopraticle, or the vaccine of the present disclosure for use in inducing an immune response to an EBV infection or a disease or condition caused by an EBV infection in a child or an infant. Where treatment, prevention or delaying progression of an EBV infection or a disease or condition caused by an EBV infection in a child is contemplated, a skilled person will be aware of suitable immunogenic compositions described herein for administration to the child. For example, administration may be given in one dose, or in several sub-doses over time, for example, about 1, 2 or 3 months apart. The present disclosure also provides a kit comprising at least one recombinant protein antigen of the disclosure and / or at least one sa-mRNA of the disclosure, optionally with an adjuvant, optionally in a delivery system and / or a pharmaceutically acceptable carrier or diluent, packaged with instructions for use in treating or preventing or delaying progression of an EBV infection or a disease or condition caused by an EBV infection in a subject. The present disclosure also provides a kit comprising the recombinant protein antigen, sa-mRNA, the polynucleotide, nanoparticle, the immunogenic composition, the pharmaceutical composition, or the vaccine disclosed herein, optionally with an adjuvant, optionally in a delivery system, and / or a pharmaceutically acceptable carrier or diluent, packaged with instructions to administer the recombinant protein antigen, the immunogenic composition, the pharmaceutical composition, or the vaccine of the present disclosure to a subject who is suffering from or at risk of suffering from an EBV infection or disease or condition caused by EBV infection. In one example, the recombinant protein antigen, sa-mRNA, the polynucleotide, nanoparticle, the immunogenic composition, the pharmaceutical composition, or the vaccine of the present disclosure is supplied in a vial. In another example, the recombinant protein antigen, sa-mRNA, the polynucleotide, nanoparticle, the immunogenic composition, the pharmaceutical composition, or the vaccine of the present disclosure is supplied in a syringe. BRIEF DESCRIPTION OF THE DRAWINGS Figure 1 is a schematic representation of potential vaccine targets. Figure 2 is a schematic representation of the recombinant protein subunits of the disclosure. Figures 3 is a graphical representation showing antigen-specific IgG induced by EBV protein subunit vaccine.1 is recombinant gp350 at 0.1 μg; 2 is recombinant gp350 at μg; 3 is recombinant gHgL at 0.1 μg; 4 is recombinant gHgL at 1 μg; 5 is recombinant gHgL+gp42 at 0.1 μg; 6 is recombinant gHgL+gp42 at 1 μg; 7 is recombinant gB mutant (mutated in the furin cleavage site: Amino acids WY112–113 to HR; WLIW193–196 to RVEA; RR469–470 to PP) 0.1 μg; 8 is recombinant gB mutant 1 μg; C1 is control SEQ 80 group 1; C2 is PC (monoclonal pool); B is background (PBS-TBN). Figure 4 is a schematic representation of the sa-mRNA constructs of the disclosure. “c.o” is codon optimised. “wt” is wild type. “SGP” is subgenomic promoter. “SGPv2” is an extended subgenomic promoter. Figures 5 is a graphical representation showing antigen-specific IgG induced by EBV sa-mRNA vaccines. Figure 6 is a graphical representation showing EBV-neutralisation following immunisation with a sa-mRNA / vaccine of the present disclosure. Figure 7 is a schematic representation of three strategies for producing monomer, dimer, and trimer antigens and recombinant peptides comprising gH, gL, and gp42. TM (TM / CT) is transmembrane domain, CMV is CMV promoter. Figure 8 is a schematic representation of the gH / gL / gp42 trimer, indicating the transmembrane region. Figure 9 is a schematic representation of monomer and dimer production strategies for recombinant peptides comprising gp350 and gp220, indicating deleted regions, 6HB region, as well as the peptide structure. Figure 10 is a schematic representation of tri-cistronic sa-mRNA constructs of the disclosure. CRL-12 serology at day 41 and day 62 is depicted for monocistronic gB and gp220, di-cistronic gH / gL, and tri-cistronic gH / gL / gp42. Figure 11 is a graphical depiction of expression of gL-gH and gp42 or gB for four different sa-mRNA constructs, EB-17, EB-18, EB-14, and EB-16. Figure 12 is a graphical representation of the EBV microneutralisation assay at day 42 in both epithelial and B cells in vivo of four different sa-mRNA constructs. Figure 13 is a graphical representation comparing microneutralisation titres of different sa-mRNA constructs, as well as a dose comparison of CRL-12 B cell microneutralisation titres. Figure 14 is a graphical representation of the comparison of monocistronic, di- cistronic and tri-cistronic vaccines. Figure 15 is a graphical representation of epithelial cell microneutralisation assay comparing several sa-mRNA constructs. Figure 16 is a graphical representation of the comparison of monocistronic, di- cistronic and tri-cistronic vaccines on epithelial microneutralisation titre. Figure 17 is a heat-map representation of CRL-31 compared to CRL-12, comparing epithelial and B cell microneutralisation titres. Figure 18 is a graphical representation of sa-mRNA construct activity in HEK293 cells. Figure 19 is a graphical representation of the effect of co-transcriptional capping (EB-14) on activity and antigen expression. Figure 20 is a graphical representation of the mRNAid codon optimisation increased RNA expression. Figure 21 is a graphical representation of mRNAid codon optimisation improved activity. Figure 22 is a schematic representation of sa-mRNA constructs in ARCT platform. Figure 23 is a graphical representation of a comparison between sa-mRNA constructs in two different backbones, G-del and ARCT. Figure 24 is a graphical representation of the increased expression seen in constructs in the ARCT backbone. Figure 25 is a graphical representation of the in vitro activity of ARCT sa-mRNA. Figure 26 is a graphical representation of the improved RNA activity when gp42 is the first gene in the construct. Figure 27 is a graphical representation of the balanced antigen expression in ARCT constructs with gp42 as the first gene of interest. Figure 28 is a graphical representation of co-transcriptional capping enhancing gp220 potency. Figure 29 is a graphical representation of ARCT tri-cistronic constructs having improved potency with gp42 as the first gene of interest. Figure 30 is a graphical representation of co-transcriptional capping enhancing the potency of the CSL (G-del) backbone tri-cistronic construct, compared to constructs with the ARCT backbone. Figure 31 is a heat mat schematic representation of the CRL-31 constructs. Figure 32 is a schematic representation of antibody-dependent cellular cytotoxicity (ADCC). Figure 33 is a graphical representation of ADCC activity of different sa-mRNA constructs, showing gH-gL and gp42 constructs having highest ADCC. Figure 34 is a graphical representation of ADCC activity of different sa-mRNA constructs, showing gH-gL and gp42 constructs having highest ADCC. Figure 35 is a graphical representation showing that ADCC activity was similar for gH-gL and gH-gL-gp42 constructs in vivo in vaccinated animals. Figure 36 is a graphical representation of EBV pseudovirus (PV) titration in epithelial cells. Figure 37 is a graphical representation of EBV PV titration in B cells. Figure 38 is a schematic representation of sa-mRNA constructs in BoBw construct platform. Figure 39 is a heat map schematic of CRL-31 constructs, demonstrating that similar to CRL-12, gH-gL topped the epithelial-based microneutralisation titres, and gH- gL-gp42 topped the B cell-based microneutralisation titres. Figure 40 is a graphical representation of gp220 and gH-gL-gp42 targeting vaccine-induced antibodies that block epithelial EBV infection. Figure 41 is a graphical representation of gp220 and gH-gL-gp42 targeting vaccine-induced antibodies that block B cell EBV infection. Figure 42 is a graphical representation of the comparison between ARCT and capped CSL and uncapped CSL backbones, as well as a uridine depletion (EB-47) backbone in vivo. Figure 43 is a graphical representation of a comparison between different tri- cistronic constructs in vivo. KEY TO SEQUENCE LISTING DETAILED DESCRIPTION General Throughout this specification, unless specifically stated otherwise or the context requires otherwise, reference to a single step, composition of matter, group of steps or group of compositions of matter shall be taken to encompass one and a plurality (i.e. one or more) of those steps, compositions of matter, groups of steps or groups of compositions of matter. Thus, as used herein, the singular forms “a”, “an” and “the” include plural aspects unless the context clearly dictates otherwise. For example, reference to “a” includes a single as well as two or more; reference to "an" includes a single as well as two or more; reference to “the” includes a single as well as two or more and so forth. Those skilled in the art will appreciate that the present disclosure is susceptible to variations and modifications other than those specifically described. It is to be understood that the disclosure includes all such variations and modifications. The disclosure also includes all of the steps, features, compositions and compounds referred to or indicated in this specification, individually or collectively, and any and all combinations or any two or more of said steps or features. The present disclosure is not to be limited in scope by the specific examples described herein, which are intended for the purpose of exemplification only. Functionally equivalent products, compositions and methods are clearly within the scope of the present disclosure. Any example of the present disclosure herein shall be taken to apply mutatis mutandis to any other example of the disclosure unless specifically stated otherwise. Stated another way, any specific example of the present disclosure may be combined with any other specific example of the disclosure (except where mutually exclusive). Any example of the present disclosure disclosing a specific feature or group of features or method or method steps will be taken to provide explicit support for disclaiming the specific feature or group of features or method or method steps. Unless specifically defined otherwise, all technical and scientific terms used herein shall be taken to have the same meaning as commonly understood by one of ordinary skill in the art (for example, in cell culture, molecular genetics, immunology, immunohistochemistry, protein chemistry, and biochemistry). Unless otherwise indicated, the recombinant protein, cell culture, and immunological techniques utilised in the present disclosure are standard procedures, well known to those skilled in the art. Such techniques are described and explained throughout the literature in sources such as, J. Perbal, A Practical Guide to Molecular Cloning, John Wiley and Sons (1984), J. Sambrook et al. Molecular Cloning: A Laboratory Manual, Cold Spring Harbour Laboratory Press (1989), T.A. Brown (editor), Essential Molecular Biology: A Practical Approach, Volumes 1 and 2, IRL Press (1991), D.M. Glover and B.D. Hames (editors), DNA Cloning: A Practical Approach, Volumes 1-4, IRL Press (1995 and 1996), and F.M. Ausubel et al. (editors), Current Protocols in Molecular Biology, Greene Pub. Associates and Wiley-Interscience (1988, including all updates until present), Ed Harlow and David Lane (editors) Antibodies: A Laboratory Manual, Cold Spring Harbour Laboratory, (1988), and J.E. Coligan et al. (editors) Current Protocols in Immunology, John Wiley & Sons (including all updates until present). The term “and / or”, e.g., “X and / or Y” shall be understood to mean either “X and Y” or “X or Y” and shall be taken to provide explicit support for both meanings or for either meaning. Throughout this specification the word “comprise”, or variations such as “comprises” or “comprising”, will be understood to imply the inclusion of a stated element, integer or step, or group of elements, integers or steps, but not the exclusion of any other element, integer or step, or group of elements, integers or steps. As used herein the term “derived from” shall be taken to indicate that a specified integer may be obtained from a particular source albeit not necessarily directly from that source. Similarly, the term “based on” shall be taken to indicate that a specified integer may be developed or used from a particular source albeit not necessarily directly from that source. All publications cited herein are hereby incorporated by reference in their entirety. Where reference is made to a URL or other such identifier or address, it is understood that such identifiers can change and particular information on the internet can come and go, but equivalent information can be found by searching the internet. Reference thereto evidences the availability and public dissemination of such information. Any discussion of documents, acts, materials, devices, articles or the like that has been included in the present specification is solely for the purpose of providing a context for the present disclosure. It is not to be taken as an admission that any or all of these matters form part of the prior art base or were common general knowledge in the field relevant to the present disclosure as it existed before the priority date of each claim of this application. Selected Definitions As used herein, the term “monovalent” as used herein, refers to a single peptide having one distinct antigenic site derived from proteins of the same virus (e.g., an EBV). “Bivalent” as used herein, refers to a single peptide having two distinct antigenic sites derived from proteins of the same virus (e.g., EBV). Such antigenic sites may be derived from peptide sequences of the same, or different, proteins and / or strains and / or isolates. For example, a bivalent vaccine peptide or protein antigen may have a first antigenic site derived from a first viral protein (e.g., for example, a first EBV viral protein) and a second viral protein (e.g., a second EBV viral protein). refers to a RNA that encodes two polypeptides. The term “trivalent” as used herein, refers to a single peptide having three distinct antigenic sites derived from proteins of the same virus (e.g., EBV). Such antigenic sites may be derived from peptide sequences of the same, or different, proteins and / or strains and / or isolates. For example, a trivalent vaccine peptide may have a first antigenic site derived from a first EBV protein and a second antigenic site derived from a second EBV protein, and a third antigenic site derived from a third EBV protein. As used herein, the term “nucleotide sequence” or “nucleic acid sequence” will be understood to mean a series of contiguous nucleotides (or bases) covalently linked to a phosphodiester backbone. By convention, sequences are presented from the 5' end to the 3' end, unless otherwise specified. As used herein, the term “antigen” refers to a molecule or structure containing one or more epitopes that induce, elicit, augment or boost a cellular and / or humoral immune response. Antigens can include, for example, proteins and peptides from a pathogen such as a virus, bacteria, fungus, protozoan, plant or from a tumour. As used herein, the terms “protein antigen” or “protein subunit” in the context of a vaccine refers to an amino acid sequence comprising at least one antigenic region that is capable of inducing production of neutralising antibodies when used to immunise a mammal, for example a human, as described herein. As used herein, the term “antigenic epitope” or “antigen epitope” refers to a region of an amino acid sequence that is capable of inducing the production of neutralising antibodies in a mammal, for example in a human. As used herein, the term “antigenic fragment” refers to a portion of an antigen described herein that can stimulate an immune response the same or similar to an antigen as described herein. In some examples, that antigen fragment can bind an antibody bound by the parent antigen. For example, and antigen fragment is a portion of an EBV antigen, for example gH, gL, gP42, gB, gP350, or gP220, that is 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, or more amino acids in length. For example, the antigen fragment is a portion of the EBV antigen as set out in any one of SEQ ID NOs: 1 to 7 or 40 to 45, for example the portion is 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, or more amino acids in length. The skilled artisan will be aware that an the antigenic fragment of a protein comprises fewer amino acids than the entire protein, e.g., the antigenic fragment lacks 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, or more amino acids that are present in the entire protein. The skilled person will be aware of suitable methods for generating antigen fragments, and of routine methods for testing the antigenicity of fragments. For example, there are several rules that can be followed to determine what peptide fragments from a protein are likely to be antigenic, and which can increase the chances of an antibody recognising the native protein. These rules are known in the art and include the following examples. For example, antigenic peptides should be located in solvent accessible regions and contain both hydrophobic and hydrophilic residues. For proteins of known 3D structure solvent accessibility can be determined using a variety of programs such as DSSP, NACESS or WHATIF, among others. A web server to calculate solvent accessibility using Whatif is also available. If the 3D structure is not known, use any of the following web servers to predict accessibilities: PHD, JPRED, PredAcc (c), ACCpro. For example, it is preferable to select peptides lying in long loops connecting secondary structure (SS) motifs, avoiding peptides located in helical regions, to increase the odds that the antibody recognises the native protein. For protein with known 3D coordinates, SS can be obtained from the sequence link of the relevant entry at the Brookhaven data bank. The PDBsum server also offer SS analysis of pdb records. When no structure is available secondary structure predictions can be obtained from any of the following servers: PHD, JPRED, PSI-PRED, NNSP, etc. For example, when possible, peptides in the N- and C-terminal region of the protein should be chosen, because the N- and C- terminal regions of proteins are usually solvent accessible and unstructured. Antibodies against those regions are also likely to recognise the native protein. For example, for cell surface glycoproteins, eliminate peptides containing consensus sites for N-glycosylation. N-glycosylation sites can be detected using Scanprosite, or NetNGlyc. For example, there are several online prediction tools available. Scores for potential epitopes within the proteins are generated, based on likely antigenicity using different prediction models. Examples of well-known models include Emini Surface Accessibility Prediction (Emini et al., 1978), Parker Hydrophilicity Prediction (Parker et al., 1986), Kolaskar & Tongaonkar Antigenicity (Kolaskar and Tongaonkar 1990), Chou & Fasman Beta-Turn Prediction (Chou and Fasman 1978), Karplus & Schulz Flexibility Prediction (Karplus and Schulz 1985), and Bepipred Linear Epitope Prediction 2.0 (Jespersen et al., 1986). In some examples, an antigenic fragment is a portion of an isolated and / or recombinant protein defined herein capable of binding one or more antibody / antibodies and forming an antigen-antibody complex. For example, the portion of an isolated and / or recombinant protein is capable of binding one or more EBV antibody / antibodies and forming an antigen-antibody complex. Antigenic fragments can be any size as long as they maintain the defined activity. In some examples, the antigenic fragment has an immunogenic activity of about 20% to 100% of the activity of the full-length protein. In some examples, the antigenic fragment has an immunogenic activity of about 30% to 100% of the activity of the full- length protein. In some examples, the antigenic fragment has an immunogenic activity of about 40% to 100% of the activity of the full-length protein. In some examples, the antigenic fragment has an immunogenic activity of about 50% to 100% of the activity of the full-length protein. In some examples, the antigenic fragment has an immunogenic activity of about 60% to 100% of the activity of the full-length protein. In some examples, the antigenic fragment has an immunogenic activity of about 70% to 100% of the activity of the full-length protein. In some examples, the antigenic fragment has an immunogenic activity of about 80% to 100% of the activity of the full-length protein. In some examples, the antigenic fragment has an immunogenic activity of about 90% to 100% of the activity of the full-length protein. In some examples, the antigenic fragment has an immunogenic activity of at least 20% of the activity of the full-length protein. In some examples, the antigenic fragment has an immunogenic activity of at least 30% of the activity of the full- length protein. In some examples, the antigenic fragment has an immunogenic activity of at least 40% of the activity of the full-length protein. In some examples, the antigenic fragment has an immunogenic activity of at least 50% of the activity of the full-length protein. In some examples, the antigenic fragment has an immunogenic activity of at least 60% of the activity of the full-length protein. In some examples, the antigenic fragment has an immunogenic activity of at least 70% of the activity of the full-length protein. In some examples, the antigenic fragment has an immunogenic activity of at least 80% of the activity of the full-length protein. In some examples, the antigenic fragment has an immunogenic activity of at least 90% of the activity of the full-length protein. As used herein “immunogenic activity” refers to the immune response produced by an antigen in a subject. The term “linker” or “flexible linker” as used herein refers to a proteinaceous molecule containing at least one amino acid residue, usually at least two amino acids residues joined by peptide bond(s), which molecule permits two polypeptides linked thereby to move more freely relative to one another, as compared to their movement without the flexible linker. In certain examples, the flexible linker provides increased rotational freedom for two polypeptides linked thereby than the two linked polypeptides would have in the absence of the flexible linker. Such freedom of relative movement or rotational freedom allows polypeptides joined by the flexible linker to perform their individual functions or elicit their activities with less structural hindrance. A flexible linker may be characterised by the absence of secondary structures such as helices or - sheets or a maximal secondary structure content of 10%, 20% 30% or 40%. Non-limiting examples of flexible linkers include the amino acid sequences GS, GSG, GGS, GGSGG, (GGS)2, GGSG, GSGS, AS, GGGS, (GGS)2GG, ((GGS)2GG)2, G4S, (G4S)2, (G4S)3, (G4S)4, G4SG, GSGG and GSGGS. Additional flexible linker sequences are known in the art. In various examples, the flexible linker contains or consists of at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95 or 100 amino acid residues. In some examples, the flexible linker contains or consists of up to 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95 or 100 amino acid residues. In some examples, the flexible linker contains or consists of between about 1 to about 30 amino acid residues, between about 1 to about 25 amino acid residues, between about 1 to about 20 amino acid residues, between about 1 to about 15 amino acid residues, between about 1 to about 12 amino acid residues, between about 1 to about 10 amino acid residues, between about 1 to about 8 amino acid residues, between about 1 to about 6 amino acid residues, between about 1 to about 5 amino acid residues, between about 1 to about 4 amino acid residues, or between about 1 to about 3 amino acid residues. In some examples, the flexible linker contains or consists of between about 2 to about 30 amino acid residues, between about 2 to about 25 amino acid residues, between about 2 to about 20 amino acid residues, between about 2 to about 15 amino acid residues, between about 2 to about 12 amino acid residues, between about 2 to about 10 amino acid residues, between about 2 to about 8 amino acid residues, between about 2 to about 6 amino acid residues, between about 2 to about 5 amino acid residues, or between about 2 to about 4 amino acid residues. In some of the same and other embodiments, the flexible linker contains or consists of between about 3 to about 30 amino acid residues, between about 3 to about 25 amino acid residues, between about 3 to about 20 amino acid residues, between about 3 to about 15 amino acid residues, between about 3 to about 12 amino acid residues, between about 3 to about 10 amino acid residues, between about 3 to about 8 amino acid residues, between about 3 to about 6 amino acid residues, or between about 3 to about 5 amino acid residues. In certain embodiments, the flexible linker contains or consists of 1, 2, 3, 4, 5, 6, 7, 8, 9,10 or 16 amino acid residues. As used herein, the terms “furin cleavage site” and “furin-like cleavage site” are used interchangeably herein to refer to a scissile bond together with adjacent or non- adjacent recognition elements, or both, sufficient for detectable proteolysis at the scissile bond by furin under conditions suitable for furin protease activity. Furin cleavage sites are known in the art or can be defined by routine methods. See, e.g., Basak, A. et al., 2001. Biochem. J. 353: 537-545; Bader, O. et al., 2008. BMC Microbiol. 8: 116; Schilling, O. et al., 2008. Nat. Biotechnol. 26:685-694; Rawlings, N.D. et al., 2008. Nucleic Acids Res.36(Database issue): D320-D325; Rawlings, N.D. et al., 2010. Nucleic Acids Res. 38(Database issue): D227-D233 (2010); Seider, N.G. et al., 2012. Nat. Rev. Drug Discov. 10.1038 / nrd3699; Braun, E. et al., 2019. Clin. Transl. Immunol, 8:el073; Izaguirre. G., 2019. Viruses 11 (2019), 10.3390 / vll090837. As used herein, the term “encode”, “encodes” or “encoding” refers to a region of a RNA capable of undergoing translation into a polypeptide. The term “polypeptide” or “polypeptide chain” will be understood to mean a series of contiguous amino acids linked by peptide bonds. For example, a protein shall be taken to include a single polypeptide chain i.e., a series of contiguous amino acids linked by peptide bonds or a series of polypeptide chains covalently or non-covalently linked to one another (i.e., a polypeptide complex). The series of polypeptide chains can be covalently linked using a suitable chemical or a disulfide bond. Examples of non- covalent bonds include hydrogen bonds, ionic bonds, Van der Waals forces, and hydrophobic interactions. To facilitate a clear description of the nucleic acids and polypeptides, particular sequence components are referred to as e.g., a “first sequence” and a “second sequence”. It is to be understood that the first and second sequences can appear in any desired order or orientation, unless otherwise specified, and that no particular order or orientation is intended by the words “first”, “second” etc. The term “recombinant” shall be understood to mean the product of artificial genetic recombination. As used herein, the terms “self-amplifying mRNA”, “sa-mRNA” or “self- replicating RNA” refer to a construct based on an RNA virus that has been engineered to allow expression of heterologous RNA and proteins. sa-mRNA (e.g., in the form of naked RNA) can amplify in host cells leading to expression of the desired gene product in the host cell. As used herein, the term “monocistronic” in reference to the sa-mRNA, refers to a RNA that encodes one polypeptide. “bicistronic” refers to a RNA that encodes two polypeptides. “multicistronic” refers to a RNA that encodes two or more polypeptides, preferably three or more polypeptides. The term “naked” as used herein refers to nucleic acids that are substantially free of other macromolecules, such as lipids, polymers and proteins. A “naked” nucleic acid, such as a sa-mRNA, is not formulated with other macromolecules to improve cellular uptake. Accordingly, a naked nucleic acid is not encapsulated in, absorbed on, or bound to a LNP, a liposome, a polymeric microparticle or an oil-in-water emulsion. As used herein, the term “operably linked to” means positioning a subgenomic promoter relative to a nucleic acid such that expression of the nucleic acid is controlled or regulated by the element. As used herein, the term “subgenomic promoter” (SG; also known as ‘junction region’ promoter) refers to a promoter that directs the expression of a heterologous nucleotide sequence, regulating protein expression. As used herein, the term “encode”, “encodes” or “encoding” refers to a region of a RNA capable of undergoing translation into a polypeptide. As used herein, a subject “at risk” of developing a disease or condition may or may not have detectable disease or symptoms of disease, and may or may not have displayed detectable disease or symptoms of disease prior to the treatment according to the present disclosure. “At risk” denotes that a subject has one or more risk factors, which are measurable parameters that correlate with development of the disease or condition, as known in the art and / or described herein. As used herein, the terms “treating”, “treat” or “treatment” include administering a RNA or composition described herein to thereby reduce or eliminate at least one symptom of a specified disease or condition. As used herein, the term “preventing”, “prevent” or “prevention” includes providing prophylaxis with respect to occurrence or recurrence of a specified disease or condition in an individual. An individual may be predisposed to or at risk of developing the disease but has not yet been diagnosed with the disease. As used herein, the phrase “delaying progression of” includes reducing or slowing down the progression of the disease or condition in an individual and / or at least one symptom of a disease or condition. As used herein, the terms “disease”, “disorder” or “condition” refers to a disruption of or interference with normal function, and is not to be limited to any specific condition, and will include diseases or disorders. An “effective amount” refers to at least an amount effective, at dosages and for periods of time necessary, to achieve the desired result. For example, the desired result may be a therapeutic or prophylactic result. An effective amount can be provided in one or more administrations. In some examples of the present disclosure, the term “effective amount” is meant an amount necessary to effect treatment of a disease or condition as hereinbefore described. In some examples of the present disclosure, the term “effective amount” is meant an amount necessary to effect a change associated with a disease or condition as hereinbefore described. The effective amount may vary according to the disease or condition to be treated or factor to be altered and also according to the weight, age, racial background, sex, health and / or physical condition and other factors relevant to the mammal being treated. Typically, the effective amount will fall within a relatively broad range (e.g. a “dosage” range) that can be determined through routine trial and experimentation by a medical practitioner. Accordingly, this term is not to be construed to limit the disclosure to a specific quantity, e.g., weight or number of recombinant protein antigen. The effective amount can be administered in a single dose or in a dose repeated once or several times over a treatment period. A “therapeutically effective amount” is at least the minimum concentration required to effect a measurable improvement of a particular disease or condition. A therapeutically effective amount herein may vary according to factors such as the disease state, age, sex, and weight of the patient, and the ability of the recombinant protein antigen of the present disclosure to elicit a desired response in the individual. A therapeutically effective amount is also one in which any toxic or detrimental effects of the recombinant protein antigen are outweighed by the therapeutically beneficial effects. As used herein, the term “prophylactically effective amount” shall be taken to mean a sufficient quantity of the recombinant protein antigen of the disclosure to prevent or inhibit or delay the onset of one or more detectable symptoms of a disease or disorder as described herein. As used herein, the term “subject” shall be taken to mean any animal including humans, for example a mammal. Exemplary subjects include but are not limited to humans and non-human primates. For example, the subject is a human, which can be an infant, a child, an adult or an elderly adult. The term “adjuvant” as used herein refers to a compound that, when used in combination with a specific immunogen (e.g., a modified polypeptide, chimeric polypeptide, polypeptide complex, polynucleotide and nucleic acid construct of the present disclosure) in a composition, will augment the resultant immune response, including intensification or broadening the specificity of either or both antibody and cellular immune responses. In the context of the present disclosure, an adjuvant will preferably enhance the specific immunogenic effect of the active agents of the present disclosure. The term “adjuvant” is typically understood not to comprise agents which confer immunity by themselves. An adjuvant assists the immune system non-specifically to enhance the antigen-specific immune response by e.g., promoting presentation of an antigen to the immune system or induction of an unspecific innate immune response. Furthermore, an adjuvant may e.g., modulate the antigen-specific immune response by e.g., shifting the dominating Th2-based antigen specific response to a more Th1-based antigen specific response or vice versa. Accordingly, an adjuvant may favourably modulate cytokine expression / secretion, antigen presentation, type of immune response etc. As used herein, the term “lipid nanoparticle” or “LNP” shall be understood to refer to lipid-based particles having at least one dimension on the order of nanometers (e.g., 1–1,000 nm) and which comprises a compound of any formulae described herein. In examples, LNPs are formulated in a composition for delivery of a polynucleotide to a desired target such as a cell, tissue, organ, tumour, and the like. For example, the lipid nanoparticle or LNP any lipid composition, including, may be selected from, but not limited to, liposomes or vesicles, where an aqueous volume is encapsulated by amphipathic lipid bilayers (e.g., single; unilamellar or multiple; multilamellar), micelle- like lipid nanoparticles having a non-aqueous core and solid lipid nanoparticles, wherein solid lipid nanoparticles lack lipid bilayers. Epstein-Barr virus (EBV) Epstein-Barr virus (EBV) is a ubiquitous virus that belongs to the gamma herpesvirus subfamily. Primary EBV infection is usually asymptomatic, and sometimes may progress to infectious mononucleosis (IM), which typically has a good prognosis. The virus is rapidly cleared by the host immune response and then persists silently in the memory B lymphocyte pool. However, reactivation of EBV may occur in immunocompromised patients and rarely in immunocompetent patients. Epstein-Barr virus (EBV) can cause illnesses and complications aside from infectious mononucleosis. People with weakened immune systems may develop more severe symptoms and complications from EBV infection. They may also have more severe illness caused by EBV infection. EBV infection can affect a person’s brain, spinal cord, and nerves, and may cause conditions such as: viral meningitis, encephalitis, optic neuritis, transverse myelitis, facial nerve palsies, Guillain-Barré syndrome, acute cerebellar ataxia, hemiplegia, sleep disorders and psychoses. EBV infection can affect a person’s blood and bone marrow, and can cause lymphocytosis. EBV can also weaken the immune system, making it more difficult for the body to fight infection. Examples of some of these conditions include neutropenia with secondary infections, haemophagocytic syndrome (hemophagocytic lymphohistiocytosis), acquired hypogammaglobulinemia, X-linked lymphoproliferative disease. EBV infection can also cause pneumonia, interstitial lung disease, pancreatitis, myocarditis, and oral cavity-oral hairy leukoplakia. Cancers are also associated with EBV infection. EBV-associated cancers include Burkitt’s lymphoma, nasopharyngeal carcinoma, Hodgkin’s disease and non-Hodgkin’s lymphoma, post-transplant lymphoproliferative disorder, and other tumours, including leiomyosarcomas and T-cell lymphomas. Complications of EBV infection include peritonsillar abscesses, acute bacterial sinusitis, suppurative lymph nodes, mastoiditis, sialadenitis, and blockage of the air passages in the nose and throat. EBV is also associated with the childhood disorders of Alice in Wonderland syndrome and, by some evidence, higher risks of developing certain autoimmune diseases, especially dermatomyositis, systemic lupus erythematosus, rheumatoid arthritis, and Sjögren's syndrome. In 2022, a large study (population of 10 million over 20 years) suggested EBV as the leading cause of multiple sclerosis, with a recent EBV infection causing a 32-fold increase in the risk of developing multiple sclerosis. Infection with EBV occurs by the oral transfer of saliva and genital secretions. Most people become infected with EBV and gain adaptive immunity. In the United States, about half of all five-year-old children and about 90% of adults have evidence of previous infection. Infants become susceptible to EBV as soon as maternal antibody protection disappears. Many children who become infected with EBV display no symptoms or the symptoms are indistinguishable from the other mild, brief illnesses of childhood. EBV infects B cells of the immune system and epithelial cells. Once EBV's initial lytic infection is brought under control, EBV latency persists in the individual's memory B cells for the rest of their life. Self-amplifying RNA The present disclosure provides a self-amplifying RNA (sa-mRNA) (also known as a replicon). The skilled person will understand that the sa-mRNA of the present disclosure is based on the genomic RNA of RNA viruses. The RNA should be positive (+)-stranded so that it can be directly translated after delivery to a cell without the need for intervening replication steps (e.g., reverse transcription). Translation of the RNA results in the production of non-structural proteins (NSPs) which combine to form a replicase complex (i.e., an RNA-dependent RNA polymerase). The complex then amplifies the original RNA, producing both antisense and sense transcripts, resulting in production of multiple daughter RNAs which may subsequently be translated and transcribed, enhancing overall protein expression. In one example, the sa-mRNA of the present disclosure comprises the non-structural proteins of the RNA virus, the 5 and 3 untranslated regions (UTRs) and thenative subgenomic promoter. In one example, the sa-mRNA comprises one or more non-structural proteins of the RNA virus. For example, the RNA comprises at least one or more genes selected from the group consisting of a viral replicase (or viral polymerase), a viral protease, a viral helicase and other non-structural viral proteins. For example, the sa-mRNA comprises a viral replicase (or viral polymerase). In another example, the sa-mRNA comprises a 5 - and a 3 -end UTR of the RNAvirus. It will be apparent to the skilled person that the terms 5 and a 3 UTR alsoencompasses the terms 5 and 3 conserved sequence elements (CSE). In one example,the sa-mRNA comprises a 5 - and a 3-end CSE.The sa-mRNA of the present disclosure cannot induce production of infectious viral particles. For example, the sa-mRNA of the present disclosure does not comprise viral genes encoding structural proteins necessary for production of viral particles. In one example, the sa-mRNA is derived from or based on an alphavirus. Suitable alphaviruses will be apparent to the skilled person and / or described herein. In another example, the sa-mRNA is derived from or based on a virus other than an alphavirus, for example, a positive-stranded RNA virus. Suitable positive-stranded RNA viruses suitable for use in the present disclosure will be apparent to the skilled person and include, for example, a picornavirus, a flavivirus, a rubivirus, a pestivirus, a hepacivirus, a calicivirus, or a coronavirus. Alphavirus In one example, the sa-mRNA of the present disclosure is derived from (or based on) an alphavirus. Alphaviruses are the sole genus in the Togaviridae family and are an enveloped virus with a positive-sense, single-stranded RNA genome. The skilled person will understand that the alphavirus genome comprises two open reading frames (ORFs), non- structural and structural. The first ORF encodes four non-structural proteins (NSP1, NSP2, NSP3 and NSP4) necessary for transcription and replication of viral RNA. The second encodes three structural proteins: the core nucleocapsid protein C, and the envelope proteins P62 and E1, which associate as a heterodimer. The viral membrane- anchored surface glycoproteins are responsible for receptor recognition and entry into target cells through membrane fusion. In one example, the sa-mRNA of the present disclosure comprises a viral replicase (or viral polymerase). For example, the viral replicase is an alphavirus replicase, such as an alphavirus protein NSP4. In one example, the sa-mRNA of the present disclosure does not encode one or more alphavirus structural proteins (e.g., capsid and / or envelope glycoproteins). For example, the sa-mRNA is unable to produce RNA-containing alphavirus virions (i.e., infectious viral particles). In one example, the sa-mRNA comprises a native alphavirus SG promoter. For example, the native alphavirus SG promoter is a minimal SG promoter (i.e., the minimal sequence required for initiation of transcription) and comprises a sequence set forth in SEQ ID NO: 35. In one example, the alphavirus SG promoter is modified, for example is an extended SG promoter. For example, the extended SG promoter is extended at the5 end with nucleotides occurring in a sequence encoding a non-structural protein (e.g.,NSP4) of the RNA virus (e.g., an alphavirus). In one example, the extended SG promoteris extended at the 5 end with nucleotides occurring in a sequence encoding an alphavirusNSP4, for example, the nucleotides of SEQ ID NO: 25 and / or SEQ ID NO: 26. The skilled person will be aware of alphaviruses suitable for use in the present disclosure. Exemplary alphaviruses include, but are not limited to, Venezuelan equine encephalitis virus (VEE; e.g., Trinidad donkey, TC83CR), Semliki Forest virus (SFV), Sindbis virus (SIN), Ross River virus, Western equine encephalitis virus, Eastern equine encephalitis virus, Chikungunya virus, S.A. AR86 virus, Everglades virus, Mucambo virus, Barmah Forest virus, Middelburg virus, Pixuna virus, O'nyong-nyong virus, Getah virus, Sagiyama virus, Bebaru virus, Mayaro virus, Una virus, Aura virus, Whataroa virus, Banbanki virus, Kyzylagach virus, Highlands J virus, Fort Morgan virus, Ndumu virus, and Buggy Creek virus. The term alphavirus may also include chimeric alphaviruses (e.g., as described by Perri et al, (2003) J. Virol. 77(19): 10394-403) that contain genome sequences from more than one alphavirus. Subgenomic Promoters The present disclosure provides a sa-mRNA comprising a nucleotide sequence encoding an EBV antigen operably linked to a subgenomic (SG) promoter. The present disclosure also provides a polynucleotide comprising a nucleotide sequence encoding an EBV antigen operably linked to a subgenomic (SG) promoter. SG promoters (also known as ‘junction region’ promoters) suitable for use in the present disclosure will be apparent to the skilled person and / or are described herein. In one example, the SG promoter is derived from or based on an alphavirus SG promoter. For example, the SG promoter is a native alphavirus SG promoter. In one example, the native SG promoter is a minimal SG promoter. For example, the minimal SG promoter is the minimal sequence required for initiation of transcription. In one example, the native SG promoter is an extended SG promoter. For example, the extendedSG promoter is a minimal SG promoter extended at the 5 end with nucleotides occurringin a sequence encoding a non-structural protein (e.g., NSP4) of the RNA virus (e.g., an alphavirus). In one example, the extended SG promoter is a minimal SG promoterextended at the 5 end with nucleotides occurring in a sequence encoding an alphavirusNSP4. In one example, the polynucleotide of the disclosure comprises a SG promoter from any alphavirus. For example, the sa-mRNA of the comprises a SG promoter from any alphavirus. In one example, the sa-mRNA comprises a SG promoter from any alphavirus. In one example, the sa-mRNA and / or the polynucleotide of the present disclosure comprises two or more nucleotide sequences encoding two or more EBV antigens of interest. In one example, the two or more nucleotide sequences are each operably linked to SG promoters. When two or more SG promoters are present in the sa-mRNA and / or the polynucleotide of the present disclosure, the promoters can be the same or different. For example, the two or more SG promoters are derived from the same alphavirus. In another example, the two or more SG promoters are derived from different alphaviruses. Modifications In one example, the polynucleotide of the present disclosure comprises one or more modification(s). Typically, modifications are introduced into a polynucleotide (e.g. mRNA) to increase the translation efficiency and / or stability of the polynucleotide. Suitable modifications to the polynucleotide will be apparent to the skilled person and / or described herein. In one example, the first nucleotide sequence comprising the 5’-UTR and / or the fragment thereof is modified. Modification of the first nucleotide sequences comprisingthe 5 -UTR and / or the fragment thereof results in a variant of the 5 -UTR and / or thefragment thereof. In one example, one or more nucleotide sequence(s) of the polynucleotide are codon optimised. Method of codon optimisation will be apparent to the skilled person and / or described herein. For example, tools for codon optimisation of polynucleotide include, for example, GeneArt GeneOptimizer (Thermofisher®) or GenSmart® (GeneScript®). In one example, the polynucleotide is modified to increase the amount of Guanine (G) and / or Cytosine (C) in the polynucleotide. The amount of G / C in the polynucleotide (i.e. G / C content) can influence the stability of the polynucleotide. Accordingly, polynucleotide comprising an increased amount of G / C nucleotides can be functionally more stable than polynucleotides containing a large amount of Adenine (A) and Thymine (T) or Uracil (U) nucleotides. The G / C content is increased by substituting A or T nucleotides with G or C nucleotides. In one example, the G / C content is increased in the first and / or second nucleotide sequence encoding the first and / or second antigen of interest. In one example, the G / C content is increased in the first and / or second nucleotide sequence encoding the first and / or second antigen of interest and / or the one or more additional nucleotide sequences encoding the one or more antigens of interest. The modification(s) in the first and / or second and / or one or more nucleotide sequences takes advantage of the ability of substituting codons that contain less favourable combinations of nucleotides (in terms of mRNA stability) with alternative codons encoding the same amino acid, or encoding amino acid(s) of similar chemistry (e.g. conserved amino acid substitution). For example, the G / C content is increased by substituting codons containing A or T nucleotides with codons containing G or C nucleotides that encode for the same amino acid. For example, the G / C content is increased by substituting codons containing A or T nucleotides with codons containing G or C nucleotides that encode for an amino acid of similar chemistry. In one example, the G / C content is increased in one or more nucleotide sequences of the polynucleotide which do not encode the antigen of interest. For example, the G / Ccontent is increased in the 5 -UTR, the fragment and / or the variant thereof. For example,the G / C content is increased in the 3 -UTR, the fragment and / or the variant thereof.In one example, the polynucleotide comprises at least one chemically modified nucleotide. As used herein, the term “chemical modification” or “chemical modified” in the context of a nucleotide refers to a naturally occurring nucleotides (i.e. A, T, C, G, U) which are modified by replacement, insertion or removal of individual or several atoms or atomic groups compared to the naturally occurring nucleotides. In one example, at least one naturally occurring nucleotide of the polynucleotide is replaced with a chemically modified nucleotide. In one example, at least 10%, or 20%, or 30%, or 40%, or 50%, or 60%, or 70%, or 80%, or 90%, or 100% of naturally occurring nucleotides of the polynucleotide is replaced with a chemically modified nucleotide(s). Suitable chemical modified nucleotides for use in the present disclosure will be apparent to the skilled person and / or described herein. Exemplary chemically modified nucleotidesinclude, for example, N6,2 -O-dimethyl-adenosine (m6Am), 5-methyluridine (m5U),N4-acetylcytidine (ac4C), 2-thiocytidine (s2C), 2-thiouridine (s2U), 5-methylcytidine(m5C), N6-methyladenosine (m6a), pseudouridine ( ), and 1-methylpseudouridine(m1 ).Antigens The sa-mRNA of the present disclosure comprises a nucleotide sequence that encodes an EBV antigen of. For example, the EBV antigen an antigen polypeptide, a fragment and / or the variant thereof which can induce an immune response in the subject. The polynucleotide of the present disclosure comprises a nucleotide sequence that encodes an EBV antigen of. For example, the EBV antigen an antigen polypeptide, a fragment and / or the variant thereof which can induce an immune response in the subject. The recombinant protein antigen of the present disclosure comprises an amino acid sequence of an EBV antigen. For example, the EBV antigen is an antigen polypeptide, a fragment and / or the variant thereof which can induce an immune response in the subject. The terms “antigen,” “immunogenic,” “immunogen,” and “antigenic” refer to any substance capable of generating antibodies when introduced into an animal. By definition, an immunogen must contain at least one epitope (the specific biochemical unit capable of causing an immune response), and generally contain several. Proteins are most frequently used as immunogens, but lipid and nucleic acid moieties complexed with proteins may also act as immunogens, especially with smaller molecules with few epitopes that may only stimulate a weak immune response by themselves. Suitable EBV antigens will be apparent to the skilled person and include EBV envelope proteins, for example, glycoproteins and / or glycoprotein complexes. In one example, the antigen(s) is selected from the group consisting of: gP350, gP42, gL, gH, gB, and gP220. The skilled person will be aware of these EBV antigens. For example, EBV glycoprotein gP350 is the most abundant glycoprotein expressed on the EBV envelope, and is used to bind to the cell surface receptor 2 on human B cells. The 220 kd protein (gP220) is the result of RNA splicing. gP42 is a unique EBV glycoprotein which binds MHC / HLA class II molecules, and is required for viral entry and infection of B lymphocytes. EBV envelope proteins gH and gL form a glycoprotein complex which \ facilitates fusion of virus membrane with host cells. gB is the EBV fusion protein that mediates viral membrane fusion and participates in host recognition, making it critical for EBV infection in both B cells and epithelial cells. Additional antigenic polypeptides, fragments and / or variants thereof suitable for use in the polynucleotide described herein will be apparent to the skilled person and, for example, can include proteins and peptides derived from any pathogen in addition to an EBV antigen. For example, the antigen is a virus, bacteria, a fungus, or a protozoan. Methods of Production Suitable methods for the production of a sa-mRNA, polynucleotide, and / or a nanoparticle of the present disclosure will be apparent to the skilled person and / or described herein. In one example, the polynucleotide is DNA. For example, the polynucleotide is a plasmid DNA. In one example, the sa-mRNA is produced using a plasmid DNA. The skilled person will understand that plasmid DNA is relatively stable. Briefly, competent bacterial cells (e.g., Escherichia coli) cells are transformed with a DNA plasmid encoding a self-amplifying RNA of the present disclosure. Individual bacterial colonies are isolated and the resultant plasmid DNA amplified in E. coli cultures. In one example, the plasmid DNA is isolated following fermentation. For example, the plasmid DNA is isolated using a commercially available kit (e.g., Maxiprep DNA kit), or other routine methods known to the skilled person. Following isolation, plasmid DNA is linearised by restriction digest (i.e., using a restricting enzyme). Restriction enzymes are removed using methods known in the art, including for example phenol / chloroform extraction and ethanol precipitation. In one example, mRNA is made by in vitro transcription from a linearised DNA template using an RNA polymerase (e.g., T7 RNA polymerase). Following in vitro transcription, the DNA template is removed by DNase digestion. The skilled person will understand that synthetic mRNA capping is performed to correct mRNA processing andcontribute to stabilisation of the mRNA. In one example, the mRNA is enzymatically 5 -capped. For example, the 5 cap is a cap0 structure or a cap1 structure. In one example,the 5 cap is a cap0 structure, for example, the 5 -cap (i.e., cap0) consists of an inverted7-methylguanosine connected to the rest of the mRNA via a 5 –5 triphosphate bridge. Inone example, the 5 cap is a cap1 structure, for example, the 5 -cap (i.e., cap1) consistsof the cap0 with an additional methylation of the 2 O position of the initiating nucleotide.In some examples, capping sa-mRNA improves activity and / or antigen expression. For example, capping improves sa-mRNA activity. For example, capping improves sa-mRNA antigen expression. In some examples, capping improves sa-mRNA activity and / or antigen expression by between 5%–60%. In some examples, capping improves sa-mRNA activity and / or antigen expression by about 5%, about 10%, about 15% about 20%, about 25%, about 30%, about 40%, about 45%, about 50%. about 55%, or about 60% In one example, the mRNA is purified. Various methods for purifying mRNA will be apparent to the skilled person. For example, the mRNA is purified using lithium chloride (LiCl) precipitation. In another example, the mRNA is purified using tangential flow filtration (TFF). Following purification, the mRNA is resuspended in e.g., nuclease- free water. Suitable methods for selecting a sa-mRNA, polynucleotide and / or nanoparticle of the present disclosure are available to those skilled in the art. Assays may be conducted to assess the efficiency and efficacy of the sa-mRNA including, for example, serology and immune responses. Compositions The disclosure additionally provides compositions that comprise the sa-mRNA and / or recombinant protein antigens disclosed herein. The compositions are suitable for administration to a mammalian subject, such as a human, and may include one or more pharmaceutically acceptable carrier(s) and / or excipient(s), including adjuvants. A thorough discussion of such components is available in Gennaro (2000) Remington: The Science and Practice of Pharmacy. 20th edition, ISBN: 0683306472. Compositions will generally be in aqueous form. When the composition is an immunogenic composition or vaccine, it will elicit an immune response when administered to a mammal, such as a human. In some examples, in the case of a vaccine, the immune response is a neutralising immune response or a protective immune response. The compositions may include a single active ingredient e.g., a recombinant protein antigen, or sa-mRNA, or several active ingredients, e.g., several different recombinant protein antigen, or several different sa-mRNA, or a combination of a recombinant protein antigen and sa-mRNA, or a recombinant protein antigen in combination with any other active ingredient, or sa-mRNA in combination with any other active ingredient. For example, the composition comprises a recombinant protein antigen comprising one, two, three, or more an Epstein-Barr virus (EBV) antigens selected from the group consisting of gP350, gP42, gL, gH, gB; and gP220. In one example, the composition is a protein subunit vaccine. In one example, the protein subunit vaccine is monovalent, bivalent, or trivalent. For example, the composition comprises a sa-mRNA comprising a nucleotide sequence encoding an antigen operably linked to a subgenomic (SG) promoter, wherein the antigen is from an Epstein-Barr virus (EBV). In another example, the sa-mRNA comprises one, two, three, or more antigens selected from the group consisting of gP350, gP42, gL, gH, gB; and gP220. In one example, the one, two, three, or four, or more antigens are each operably linked to a subgenomic promoter. For example, the composition comprises a combination of a recombinant protein antigen comprising one, two, three, or more an Epstein-Barr virus (EBV) antigens selected from the group consisting of gP350, gP42, gL, gH, gB; and gP220 and a sa-mRNA comprising a nucleotide sequence encoding an antigen operably linked to a subgenomic (SG) promoter, wherein the antigen is from an Epstein-Barr virus (EBV). For example, the composition comprises a combination of a recombinant protein antigen comprising one, two, three, or more an Epstein-Barr virus (EBV) antigens selected from the group consisting of gP350, gP42, gL, gH, gB; and gP220 and a sa-mRNA comprising one, two, three, or more antigens selected from the group consisting of gP350, gP42, gL, gH, gB; and gP220. For example, the composition comprises a combination of a protein subunit vaccine and a sa-mRNA comprising a nucleotide sequence encoding an antigen operably linked to a subgenomic (SG) promoter, wherein the antigen is from an Epstein-Barr virus (EBV). For example, the composition comprises a combination of a protein subunit vaccine and a sa-mRNA comprising one, two, three, or more antigens selected from the group consisting of gP350, gP42, gL, gH, gB; and gP220. For example, the composition comprises a monovalent, bivalent, or trivalent protein subunit vaccine and a sa-mRNA comprising a nucleotide sequence encoding an antigen operably linked to a subgenomic (SG) promoter, wherein the antigen is from an Epstein-Barr virus (EBV). For example, the composition comprises a monovalent, bivalent, or trivalent protein subunit vaccine and a sa-mRNA comprising one, two, three, or more antigens selected from the group consisting of gP350, gP42, gL, gH, gB; and gP220. The composition may include preservatives such as thiomersal or 2- phenoxyethanol. To control tonicity, a composition can comprise a physiological salt, such as a sodium salt. Sodium chloride (NaCl) is exemplary, which may be present at between 1 and 20 mg / ml. Other salts that may be present include potassium chloride, potassium dihydrogen phosphate, disodium phosphate dehydrate, magnesium chloride, calcium chloride, and the like. Compositions will generally have an osmolality of between 200 mOsm / kg and 400 mOsm / kg, such as between 240–360 mOsm / kg, for example, within the range of 290–310mOsm / kg. Compositions may include one or more buffers. Typical buffers include: a phosphate buffer; a Tris buffer; a borate buffer; a succinate buffer; a histidine buffer (particularly with an aluminium hydroxide adjuvant); or a citrate buffer. Buffers will typically be included in the 5–20mM range. The pH of a composition will generally be between 5.0 and 8.1, and more typically between 6.0 and 8.0, e.g, between 6.5 and 7.5, or between 7.0 and 7.8. In one example, the composition is sterile. The composition is preferably non- pyrogenic, e.g., containing <1 EU (endotoxin unit, a standard measure) per dose, and preferably <0.1 EU per dose. The composition is preferably gluten free. Human vaccines are typically administered in a dosage volume of about 0.5ml, although a half dose (i.e., about 0.25ml) may be administered to children. In one example, the composition comprises an adjuvant. According to the disclosure adjuvants can be, but are not limited to, organic, inorganic, oil-based adjuvants or virosomes. Inorganic adjuvants include, but are not limited to mineral adjuvants, for example aluminium or calcium salts, such as aluminium phosphate, aluminium hydroxide (also referred to as Al(OH)3 herein), potassium aluminium sulphate (also referred to as alum) and calcium phosphate. Such adjuvants may be used with or without other adjuvants. Organic adjuvants include, but are not limited, to squalene. Further examples of adjuvants according to the disclosure include, but are not limited to, MPL (Monophosphoryl Lipid A), AS03 (developed by GSK, Prepandrix), AS04 (developed by GSK; combination of MPL and aluminum hydroxide; Fendrix; Cervarix), QS21 (Saponin purified plant extract from the Soap bark tree (Quillaia saponaria) containing triterpene glucoside), AS01 (developed by GSK; liposomes; QS21 and MPL), AS02 (developed by GSK; QS21 and MPL), LT (heat labile enterotoxin from E.coli), CpG (oligonucleotides containing unmethylated CpG sequences), and MF59 (from Novartis). MF59 is a sub-micron oil-in-water emulsion of a squalene, polyoxyethylene sorbitan monooleate and sorbitan trioleate compounds. Adjuvants suitable for the disclosure are for example mineral adjuvants or adjuvants containing squalene, e.g. emulsion of squalene, e.g. MF59. In one example, the composition of the disclosure comprises a fusion protein of the disclosure and either (i) MF59 or (ii) an aluminium salt (such as aluminium hydroxide). In one example, the composition of the disclosure comprises a fusion protein of the disclosure and MF59. The choice of adjuvant depends on the efficiency of adjuvant in promoting the immune response, the stability of the composition containing the adjuvant, e.g. the vaccine containing the adjuvant, the route of administration, the dosing regimen, the species to be vaccinated. Two or more adjuvants can be combined. For example, aluminium salts can be combined with MPL, QS21, and / or MF59. The present disclosure also provides an immunogenic composition comprising one or more recombinant protein antigens of the present disclosure. The present disclosure also provides an immunogenic composition comprising a sa-mRNA of the present disclosure. The present disclosure also provides an immunogenic composition comprising one or more recombinant protein antigens of the present disclosure and one or more sa- mRNA of the present disclosure. The present disclosure provides an immunogenic composition comprising a polynucleotide of the present disclosure. The present disclosure provides an immunogenic composition comprising a nanoparticle of the present disclosure. The present disclosure provides an immunogenic composition comprising a plurality of sa-mRNAs of the present disclosure. The present disclosure further provides an immunogenic composition comprising a plurality of sa-mRNAs of the present disclosure, wherein each sa-mRNA encodes different polypeptide antigen sequences. The present disclosure further provides an immunogenic composition comprising a plurality of sa-mRNAs of the present disclosure, wherein the plurality comprises at least two different sa-mRNA encoded polypeptide antigen sequences. The present disclosure also provides a pharmaceutical composition comprising an immunogenic composition of the present disclosure and a pharmaceutically acceptable carrier. For example, a protein carrier. It will be apparent to the skilled person and / or described herein, that the sa- mRNA, polynucleotide and / or nanoparticle of the present disclosure may be present as naked RNA or in combination with lipids, polymers or other delivery system that facilitates entry into the cells. In compositions or methods for administration of the recombinant protein antigen, or the sa-mRNA, or a protein subunit vaccine comprising the recombinant protein antigen of the disclosure, or a vaccine comprising the sa-mRNA of the disclosure to a subject, the recombinant protein antigen, or the sa-mRNA, or a protein subunit vaccine, or the vaccine comprising the sa-mRNA is combined with a suitable pharmaceutically acceptable carrier as is understood in the art. Accordingly, in some examples, the present disclosure provides a composition (e.g., a pharmaceutical composition) comprising the recombinant antigen of the disclosure (and any delivery system) combined with a pharmaceutically acceptable carrier. In some examples, the present disclosure provides a composition (e.g., a pharmaceutical composition) comprising the sa-mRNA of the disclosure (and any delivery system) combined with a pharmaceutically acceptable carrier. In general terms, a “carrier” is a solid or liquid filler, binder, diluent, encapsulating substance, emulsifier, wetting agent, solvent, suspending agent, coating or lubricant that may be safely administered to any subject, e.g., a human. Depending upon the particular route of administration, a variety of acceptable carriers, known in the art may be used, as for example described in Remington's Pharmaceutical Sciences (Mack Publishing Co. N.J. USA, 1991). Delivery systems In one example, the pharmaceutical composition of the present disclosure further comprises a LNP, a polymeric microparticle, an oil-in-water emulsion or other adjuvant. For example, the sa-mRNA, the polynucleotide, and / or the nanoparticle is encapsulated in, bound to or adsorbed on a LNP, a polymeric microparticle, or an oil-in-water emulsion. Lipid Nanoparticles In one example, the pharmaceutical composition of the present disclosure further comprises a LNP. It will be apparent that the term “lipid nanoparticle” or “LNP” refers to any lipid composition, including, but not limited to, liposomes or vesicles, where an aqueous volume is encapsulated by amphipathic lipid bilayers (e.g., single; unilamellar or multiple; multilamellar) micelle-like lipid nanoparticles having a non-aqueous core and solid lipid nanoparticles, wherein solid lipid nanoparticles lack lipid bilayers. Lipid nanoparticles suitable for use in the present disclosure will be apparent to the skilled person and / or are described herein. The lipids can have an anionic, cationic or zwitterionic hydrophilic head group. The present disclosure provides for an LNP for delivery of a nucleic acid, such as a RNA or sa-mRNA encoding a fusion protein of the disclosure. In examples, the LNPs have a mean diameter of from about 30 nm to about 160 nm, from about 40 nm to about 160 nm, from about 50 nm to about 160 nm, from about 60 nm to about 160 nm, from about 70 nm to about 160 nm, from about 50 nm to about 140 nm, from about 60 nm to about 130 nm, from about 70 nm to about 120 nm, from about 80 nm to about 120 nm, from about 90 nm to about 120 nm, from about 70 to about 110 nm, from about 80 nm to about 110 nm, or about 40 nm, 45 nm, 50 nm, 55 nm, 60 nm, 65 nm, 70 nm, 75 nm, 80 nm, 85 nm, 90 nm, 95 nm, 100 nm, 105 nm, 110 nm, 115 nm, 120 nm, 125 nm, 130 nm, 135 nm, 140 nm, 145 nm, 150 nm, 155 nm or 160 nm. The diameter of the LNP may be measured by dynamic light scattering (DLS), transmission electron microscopy (TEM), scanning electron microscopy (SEM), or other methods such as are known in the art. In some examples, the LNPs may be relatively homogenous. A polydispersity index may be used to indicate the homogeneity of the LNPs. A small, for example less than 0.3 or less than 0.2, polydispersity index generally indicates a narrow particle size distribution. A composition of the LNPs described herein may have a polydispersity index from about 0 to about 0.25, such as 0.01, 0.02, 0.03, 0.04, 0.05, 0.06, 0.07, 0.08, 0.09, 0.10, 0.11, 0.12, 0.13, 0.14, 0.15, 0.16, 0.17, 0.18, 0.19, 0.20, 0.21, 0.22, 0.23, 0.24, or 0.25. In some embodiments, the polydispersity index of the LNP composition may be from about 0 to about 0.20 or 0.05 to 0.20. The LNP may comprise a cationic and / or ionisable lipid, a neutral lipid, a PEG- lipid and a sterol. The LNP may comprise a cationic and / or ionisable lipids selected from the non- limiting group consisting of: 3-(didodecylamino)-N1,N1,4-tridodecyl-1- piperazineethanamine (KL10), N1-[2-(didodecylamino)ethyl]-N1,N4,N4-tridodecyl- 1,4-piperazinediethanamine (KL22), 14,25-ditridecyl-15,18,21,24-tetraaza- octatriacontane (KL25), 1,2-dilinoleyloxy-N,N-dimethylaminopropane (DLin-DMA), 2,2-dilinoleyl-4-dimethylaminomethyl-[1,3]-dioxolane (DLin-K-DMA), (6Z,9Z,28Z,31Z)-heptatriacont-6,9,28,31-tetraene-19-yl 4-(dimethylamino)butanoate (DLin-MC3-DMA), 2,2-dilinoleyl-4-(2-dimethylaminoethyl)-[1,3]-dioxolane (DLin-KC2-DMA), 1,2-dioleyloxy-N,N-dimethylaminopropane (DODMA), 2-({8-[(3 )-cholest-5-en-3-yloxy]octyl}oxy)-N,N-dimethyl-3-[(9Z,12Z)-octadeca-9,12-dien-1-yloxy]propan-1-amine (Octyl-CLinDMA), (2R)-2-({8-[(3 )-cholest-5-en-3-yloxy]octyl}oxy)-N,N-dimethyl-3-[(9Z,12Z)-octadeca-9,12-die n-1-yloxy]propan-1-amine (Octyl-CLinDMA (2R)), (2S)-2-({8-[(3 )-cholest-5-en-3-yloxy]octyl}oxy)-N,N-dimethyl-3-[(9Z,12Z)-octadeca-9,12-die n-1-yloxy]propan-1-amine (Octyl-CLinDMA (2S)), ((4-hydroxybutyl)azanediyl)bis(hexane-6,1-diyl)bis(2-hexyldecanoate)) and 8- [(2-hydroxyethyl)[6-oxo-6-(undecyloxy)hexyl]amino]-octanoic acid, 1-octylnonyl ester. It will be apparent to the skilled person that reference to a PEGylated lipid is a lipid that has been modified with polyethylene glycol. Exemplary PEGylated lipids include, but are not limited to, PEG-modified phosphatidylethanolamines, PEG-modified phosphatidic acids, PEG-modified ceramides, PEG-modified dialkylamines, PEG- modified diacylglycerols, and PEG-modified dialkylglycerols. For embodiment, a PEG lipid includes PEG-c-DOMG, PEG-DMG, PEG-DLPE, PEG-DMPE, PEG-DPPC, a PEG-DSPE lipid and combinations thereof. In one example, the lipid nanoparticle comprises a PEG-lipid, a sterol structural lipid and / or a neutral lipid. In one example, the lipid nanoparticle further comprises a cationic lipid. In one example, the lipid nanoparticle does not comprise a cationic lipid. In one example, the LNP comprises a PEG-lipid. For example, the PEG-lipid is selected from the group consisting of PEG-c-DMG, PEG-DMG, PEG-DLPE, PEG- DMPE, PEG-DPPC, a PEG-DSPE lipid and combinations thereof. Exemplary structural lipids or sterols include, but are not limited to, cholesterol fecosterol, sitosterol, campesterol, stigmasterol, brassicasterol, ergosterol, tomatidine, tomatine, ursolic acid and alpha-tocopherol. In one example, the LNP comprises a structural lipid. For example, the structural lipid is selected from the group consisting of cholesterol fecosterol, sitosterol, campesterol, stigmasterol, brassicasterol, ergosterol, tomatidine, tomatine, ursolic acid and alpha-tocopherol and combinations thereof. In one example, the structural lipid is a sterol. In embodiments, the structural lipid is cholesterol. In another embodiment, the structural lipid is campesterol. In one example, the LNP comprises a neutral lipid. Exemplary phospholipids (anionic or zwitterionic) for use in the present disclosure include, for example, phosphatidylethanolamines, phosphatidylcholines, phosphatidylserines, and phosphatidylglycerols. For example, the neutral lipid is selected from the group consisting of 1,2-distearoyl-sn-glycero-3-phosphocholine (DSPC), 1,2-dioleoyl-sn- glycero-3-phosphoethanolamine (DOPE), 1,2-dilinoleoyl-sn-glycero-3-phosphocholine (DLPC), 1,2-dimyristoyl-sn-glycero-phosphocholine (DMPC), 1,2-dioleoyl-sn-glycero- 3-phosphocholine (DOPC), 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), 1,2- diundecanoyl-sn-glycero-phosphocholine (DUPC), 1-palmitoyl-2-oleoyl-sn-glycero-3- phosphocholine (POPC), 1,2-di-O-octadecenyl-sn-glycero-3-phosphocholine (18:0 Diether PC), 1-oleoyl-2-cholesterylhemisuccinoyl-sn-glycero-3-phosphocholine (OChemsPC), 1-hexadecyl-sn-glycero-3-phosphocholine (C16 Lyso PC), 1,2- dilinolenoyl-sn-glycero-3-phosphocholine, 1,2-diarachidonoyl-sn-glycero-3- phosphocholine, 1,2-didocosahexaenoyl-sn-glycero-3-phosphocholine, 1,2- diphytanoyl-sn-glycero-3-phosphoethanolamine (ME 16.0 PE), 1,2-distearoyl-sn- glycero-3-phosphoethanolamine, 1,2-dilinoleoyl-sn-glycero-3-phosphoethanolamine, 1,2-dilinolenoyl-sn-glycero-3-phosphoethanolamine, 1,2-diarachidonoyl-sn-glycero-3- phosphoethanolamine, 1,2-didocosahexaenoyl-sn-glycero-3-phosphoethanolamine, 1,2- dioleoyl-sn-glycero-3-phospho-rac-(1-glycerol) sodium salt (DOPG), sphingomyelin and combinations thereof. The lipids can be saturated or unsaturated. In one example, the LNP comprises a cationic lipid. Exemplary cationic lipids include, but are not limited to, dioleoyl trimethylammonium propane (DOTAP), l,2- distearyloxy-N,N-dimethyl-3-aminopropane (DSDMA), 1 ,2-dioleyloxy- N,Ndimethyl- 3-aminopropane (DODMA), 1 ,2-dilinoleyloxy-N,N-dimethyl-3- aminopropane (DLinDMA), 1 ,2-dilinolenyloxy-N,N-dimethyl-3-aminopropane (DLenDMA), 2,5- bis((9z,12z)-octadeca-9,12,dien-1-yloxyl)benzyl-4-(dimethylamino)butnoate (LKY750). In one example, the phospholipid is 2,5-bis((9z,12z)-octadeca-9,12,dien-1- yloxyl)benzyl-4-(dimethylamino)butnoate (LKY750). Exemplary zwitterionic lipids include, but are not limited to, acyl zwitterionic lipids and ether zwitterionic lipids, such as dipalmitoylphosphatidylcholine (DPPC), dioleoylphosphatidylcholine (DOPC) and dodecylphosphocholine. The lipids can be saturated or unsaturated. Polymeric microparticles In one example, the pharmaceutical composition of the present disclosure further comprises a polymeric microparticle. The skilled person will be aware that various polymers can form microparticles to encapsulate or adsorb the sa-mRNA, the polynucleotide, and / or the nanoparticle of the present disclosure. It will be apparent that use of a substantially non-toxic polymer means that particles are safe, and the use of a biodegradable polymer means that the particles can be metabolised after delivery to avoid long-term persistence. Useful polymers are also sterilisable, to assist in the preparation of pharmaceutical grade formulations. Exemplary non-toxic and biodegradable polymers include, but are not limited to,poly( - hydroxy acids), polyhydroxy butyric acids, polylactones (includingpolycaprolactones), polydioxanones, polyvalerolactone, polyorthoesters, polyanhydrides, polycyanoacrylates, tyrosine-derived polycarbonates, polyvinyl- pyrrolidinones or polyester-amides, and combinations thereof. Oil-in-water cationic emulsions In one example, the pharmaceutical composition of the present disclosure further comprises an oil-in-water cationic emulsion. Suitable oils for use in an oil-in-water emulsion will be apparent to the skilled person and / or are described herein. For example, the emulsion comprises one or more oils derived, for example, from an animal (e.g., fish) or a vegetable source (e.g., nuts, seeds, grains). The skilled person will recognise that biocompatible and biodegradable oils are preferentially used. Exemplary animal oils (i.e., fish oils) include cod liver oil, shark liver oils, and whale oil. Exemplary vegetable oils include peanut oil, coconut oil, olive oil, soybean oil, jojoba oil, safflower oil, cottonseed oil, sunflower seed oil, sesame seed oil, corn oil. In addition to the oil, the oil-in-water emulsion also comprises a cationic lipid to facilitate formation and stabilisation of the emulsion. Suitable cationic lipids will be apparent to the skilled person and / or are described herein. Exemplary cationic lipids include, but are not limited to, limited to: l, 2-dioleoyloxy-3-(trimethylammonio)propane (DOTAP), 3'-[N-(N',N'-Dimethylaminoethane)-carbamoyl] Cholesterol (DC Cholesterol), dimethyldioctadecyl-ammonium (DDA), l,2-Dimyristoyl-3-Trimethyl- AmmoniumPropane (DMTAP), dipalmitoyl[C16:0]trimethyl ammonium propane (DPTAP) and distearoyltrimethylammonium propane (DSTAP). In some examples, the oil-in-water emulsion also comprises a non-ionic surfactant and / or a zwitterionic surfactant. The skilled person will be aware of surfactants suitable for use in the present disclosure. Exemplary surfactants include, but are not limited to: the polyoxyethylene sorbitan esters surfactants (e.g., polysorbate 20 and polysorbate 80) and copolymers of ethylene oxide (EO), propylene oxide (PO), and / or butylene oxide (BO). Pharmaceutically acceptable carrier In compositions or methods for administration of the sa-mRNA, the polynucleotide and / or the nanoparticle of the disclosure to a subject, the sa-mRNA, the polynucleotide and / or the nanoparticle is combined with a suitable pharmaceutically acceptable carrier as is understood in the art. Accordingly, one example of the present disclosure provides a composition (e.g., a pharmaceutical composition) comprising the sa-mRNA of the disclosure (and any delivery system) combined with a pharmaceutically acceptable carrier. Another example of the present disclosure provides a composition (e.g., a pharmaceutical composition) comprising the polynucleotide of the disclosure (and any delivery system) combined with a pharmaceutically acceptable carrier. Another example of the present disclosure provides a composition (e.g., a pharmaceutical composition) comprising the nanoparticle of the disclosure (and any delivery system) combined with a pharmaceutically acceptable carrier. In general terms, by “carrier” is meant a solid or liquid filler, binder, diluent, encapsulating substance, emulsifier, wetting agent, solvent, suspending agent, coating or lubricant that may be safely administered to any subject, e.g., a human. Depending upon the particular route of administration, a variety of acceptable carriers, known in the art may be used, as for example described in Remington's Pharmaceutical Sciences (Mack Publishing Co. N.J. USA, 1991). The sa-mRNA, the polynucleotide and / or the nanoparticle of the present disclosure is useful for parenteral, topical, oral, or local administration, intramuscular administration, aerosol administration, or transdermal administration, for prophylactic or for therapeutic treatment. In one example, the sa-mRNA is administered parenterally, such as intramuscularly, subcutaneously, or intravenously. For example, the sa-mRNA is administered intravenously. In another example, the polynucleotide is administered parenterally, such as intramuscularly, subcutaneously, or intravenously. For example, the polynucleotide is administered intravenously. Formulation of a sa-mRNA, polynucleotide and / or nanoparticle to be administered will vary according to the route of administration and formulation (e.g., solution, emulsion, capsule) selected. An appropriate pharmaceutical composition comprising a sa-mRNA, the polynucleotide and / or the nanoparticle to be administered can be prepared in a physiologically acceptable carrier. For solutions or emulsions, suitable carriers include, for example, aqueous or alcoholic / aqueous solutions, emulsions, or suspensions, including saline and buffered media. Parenteral vehicles can include sodium chloride solution, Ringer’s dextrose, dextrose and sodium chloride, lactated Ringer’s, or fixed oils. A variety of appropriate aqueous carriers are known to the skilled artisan, including water, buffered water, buffered saline, polyols (e.g., glycerol, propylene glycol, liquid polyethylene glycol), dextrose solution and glycine. Intravenous vehicles can include various additives, preservatives, or fluid, nutrient or electrolyte replenishers (See, generally, Remington’s Pharmaceutical Science, 16th Edition, Mack, Ed. 1980). The compositions can optionally contain pharmaceutically acceptable auxiliary substances as required to approximate physiological conditions such as pH adjusting and buffering agents and toxicity adjusting agents, for example, sodium acetate, sodium chloride, potassium chloride, calcium chloride and sodium lactate. The sa-mRNA, the polynucleotide and / or the nanoparticle can be stored in the liquid stage or can be lyophilised for storage and reconstituted in a suitable carrier prior to use according to art-known lyophilisation and reconstitution techniques. The optimum concentration of the active ingredient(s) in the chosen medium can be determined empirically, according to procedures known to the skilled artisan, and will depend on the ultimate pharmaceutical formulation desired. Upon formulation, compositions of the present disclosure will be administered in a manner compatible with the dosage formulation and in such amount as is therapeutically / prophylactically effective. The dosage ranges for the administration of the sa-mRNA, the polynucleotide and / or the nanoparticle of the disclosure are those large enough to produce the desired effect. For example, the composition comprises an effective amount of the sa-mRNA. In one example, the composition comprises a therapeutically effective amount of the sa-mRNA. In another example, the composition comprises a prophylactically effective amount of the sa-mRNA. In one example, the composition comprises an effective amount of the polynucleotide. In one example, the composition comprises a therapeutically effective amount of the polynucleotide. In another example, the composition comprises a prophylactically effective amount of the polynucleotide. In one example, the composition comprises an effective amount of the nanoparticle. In one example, the composition comprises a therapeutically effective amount of the nanoparticle. In another example, the composition comprises a prophylactically effective amount of the nanoparticle. The dosage should not be so large as to cause adverse side effects. Generally, the dosage will vary with the age, condition, sex and extent of the disease in the patient and can be determined by one of skill in the art. The dosage can be adjusted by the individual physician in the event of any complication. Dosage can vary from about 0.1 mg / kg to about 300 mg / kg, e.g., from about 0.2 mg / kg to about 200 mg / kg, such as, from about 0.5 mg / kg to about 20 mg / kg, in one or more dose administrations daily, for one or several days. In some examples, the sa-mRNA, the polynucleotide and / or the nanoparticle is administered at an initial (or loading) dose which is higher than subsequent (maintenance doses). For example, the sa-mRNA, the polynucleotide and / or the nanoparticle is administered at an initial dose of between about 10mg / kg to about 30mg / kg. The sa- mRNA, the polynucleotide and / or the nanoparticle is then administered at a maintenance dose of between about 0.0001mg / kg to about 10mg / kg. The maintenance doses may be administered every 7 to 35 days, such as, every 7 or 14 or 28 days. In some examples, a dose escalation regime is used, in which the sa-mRNA, the polynucleotide and / or the nanoparticle is initially administered at a lower dose than used in subsequent doses. This dosage regime is useful in the case of subjects initially suffering adverse events A subject may be re-treated with sa-mRNA, the polynucleotide and / or the nanoparticle of the present disclosure. A subject may be re-treated with the sa-mRNA, the polynucleotide and / or the nanoparticle, by being given more than one exposure or set of doses, such as at least about two exposures of the binding protein, for example, from about 2 to 60 exposures, and more particularly about 2 to 40 exposures, most particularly, about 2 to 20 exposures. In one example, any retreatment may be given when signs or symptoms of disease return. In another example, any retreatment may be given at defined intervals. For example, subsequent exposures may be administered at various intervals, such as, for example, about 24 to 28 weeks or 48 to 56 weeks or longer. For example, such exposures are administered at intervals each of about 24 to 26 weeks or about 38 to 42 weeks, or about 50 to 54 weeks. In the case of a subject that is not adequately responding to treatment, multiple doses in a week may be administered. Alternatively, or in addition, increasing doses may be administered. In another example, for subjects experiencing an adverse reaction, the initial (or loading) dose may be split over numerous days in one week or over numerous consecutive days. Administration of the sa-mRNA, the polynucleotide and / or the nanoparticle according to the methods of the present disclosure can be continuous or intermittent, depending, for example, on the recipient's physiological condition, whether the purpose of the administration is therapeutic or prophylactic, and other factors known to skilled practitioners. The administration of the sa-mRNA, the polynucleotide and / or the nanoparticle may be essentially continuous over a preselected period of time or may be in a series of spaced doses, e.g., either during or after development of a condition. Polynucleotides / Nucleic acids The disclosure provides polynucleotides and nucleic acids encoding an antigen operably linked to a subgenomic (SG) promoter, wherein the antigen is from an Epstein- Barr virus (EBV). For example, the disclosure provides a polynucleotide encoding the sa-mRNA of the disclosure. As used herein, the term “polynucleotide” refers a molecular chain of nucleotides chemically bonded by a series of ester linkages between the phosphoryl group of one nucleotide and the hydroxyl group of the sugar in an adjacent nucleotide. The polynucleotide of the present disclosure includes DNA and RNA (e.g. mRNA). In one example, the polynucleotide is a DNA, for example, a plasmid DNA. In one example, the polynucleotide is a RNA, for example, a sa-mRNA. Nucleic acids useful in the present disclosure may include a first region of linked nucleosides encoding a polypeptide of interest (e.g., a coding region), a first flankingregion located at the 5 -terminus of the first region (e.g., a 5 -UTR), a second flankingregion located at the 3 -terminus of the first region (e.g., a 3 -UTR), at least one 5 -capregion, and a 3 -stabilising region. In some examples, a nucleic acid further includes apoly-A region or a Kozak sequence (e.g., in the 5 -UTR). In some cases, nucleic acidsmay contain one or more intronic sequences capable of being excised from the nucleicacid. In some examples, a nucleic acid (e.g., an mRNA) may include a 5 cap structure,a chain terminating nucleotide, a stem loop, a poly A sequence, and / or a polyadenylation signal. Any one of the regions of a nucleic acid may include one or more alternativecomponents (e.g., an alternative nucleoside). For example, the 3 -stabilising region maycontain an alternative nucleoside such as an L-nucleoside, an inverted thymidine, or a 2'-O-methyl nucleoside and / or the coding region, 5 -UTR, 3 -UTR, or cap region mayinclude an alternative nucleoside such as a 5-substituted uridine (e.g., 5-methoxy uridine), a 1-substituted pseudouridine (e.g., 1-methyl-pseudouridine or 1-ethyl- pseudouridine), and / or a 5-substituted cytidine (e.g., 5-methyl-cytidine). Nucleic acids suitable for use with the present LNPs may include one or more naturally occurring components, including any of the canonical nucleotides A (adenosine), G (guanosine), C (cytosine), U (uridine), or T (thymidine). In oneembodiment, all or substantially all of the nucleotides comprising (a) the 5 -UTR, (b) theopen reading frame (ORF), (c) the 3 -UTR, (d) the poly A tail, and any combination of(a, b, c, or d above) comprise naturally occurring canonical nucleotides A (adenosine), G (guanosine), C (cytosine), U (uridine), or T (thymidine). In some examples, nucleic acids may include one or more alternative components, as described herein, which impart useful properties including increased stability and / or the lack of a substantial induction of the innate immune response of a cell into which the nucleic acid is introduced. For example, an alternative nucleic acid exhibits reduced degradation in a cell into which the nucleic acid is introduced, relative to a corresponding unaltered nucleic acid. These alternative species may enhance the efficiency of protein production, intracellular retention of the nucleic acids, and / or viability of contacted cells, as well as possess reduced immunogenicity. Nucleic acids may be naturally or non-naturally occurring. Nucleic acids may include one or more modified (e.g., altered or alternative) nucleobases, nucleosides, nucleotides, or combinations thereof. The nucleic acids may include any useful modification or alteration, such as to the nucleobase, the sugar, or the internucleoside linkage (e.g., to a linking phosphate / to a phosphodiester linkage / to the phosphodiester backbone). In some embodiments, one or more alterations are present in each of the nucleobase, the sugar, and the internucleoside linkage. Nucleic acids may or may not be uniformly altered along the entire length of the molecule. For example, one or more or all types of nucleotide (e.g., purine or pyrimidine, or any one or more or all of A, G, U, C) may or may not be uniformly altered in a nucleic acid, or in a given predetermined sequence region thereof. Different sugar alterations and / or internucleoside linkages (e.g., backbone structures) may exist at various positions in a nucleic acid. One of ordinary skill in the art will appreciate that the nucleotide analogues or other alteration(s) may be located at any position(s) of a nucleic acid such that the function of the nucleic acid is notsubstantially decreased. An alteration may also be a 5 - or 3 '-terminal alteration. In someembodiments, the nucleic acid includes an alteration at the 3 -terminus.As used herein, the term “fragment” refers to a portion of a nucleotide sequence or polypeptide of a reference nucleotide sequence or polypeptide disclosed herein which maintains a defined activity of the full-length nucleotide sequence or polypeptide. As used herein, the term “variant” refers to a nucleotide sequence with one or more substitutions, insertions, deletions and / or other modifications compared to the unmodified sequence. It will be apparent to the skilled person that any variant described herein will have the same or similar expression of the encoded protein. For example, the variant is a functional variant. Exemplary modifications to the nucleotide sequence and / or polypeptide will be apparent to the skilled person and / or described herein. In one example, a modification is a chemical modification of one or more nucleotide(s) of the nucleotide sequence. For example, at least one naturally occurring nucleotide of the polynucleotide is replaced with a chemically modified nucleotide (e.g.pseudouridine ( ), and 1-methylpseudouridine (m1 )).In one example, the modification comprises increasing the G / C content of the nucleotide sequence. In one example, the modification comprises codon optimisation of the nucleotide sequence. As used herein, the term “encode”, “encodes” or “encoding” refers to a region of a polynucleotide capable of producing another substance, for example, capable of producing a nucleic acid or protein of interest. Methods of treatment and administration Compositions of the disclosure are suitable for administration to mammals, e.g., humans, and the disclosure provides a method of inducing an immune response in a mammal, comprising administering a composition (e.g., an immunogenic composition or a pharmaceutical composition), or a vaccine, for example a protein subunit vaccine or a sa-mRNA vaccine or a sa-mRNA, or a polynucleotide, or a nanoparticle of the present disclosure to the mammal. In certain examples, the immune response is a neutralising immune response. The compositions (e.g., an immunogenic and / or pharmaceutical compositions) can be used to produce a vaccine formulation for immunising a mammal. The mammal is typically a human. In some examples, the human is a child. The present disclosure provides methods of using the recombinant protein antigen, the sa-mRNA, the immunogenic composition, or the pharmaceutical composition of the present disclosure as a vaccine. The present disclosure also provides methods of treating or preventing a disease or condition in a subject comprising administering the recombinant protein antigen, the protein subunit vaccines, the sa-mRNA, the sa-mRNA vaccines, the immunogenic composition or the pharmaceutical composition of the present disclosure. For example, the disease or condition is an EBV infection. For example, the disease or condition is caused by an EBV infection. For example, the disease or condition is selected from the group consisting of infectious mononucleosis (glandular fever), viral meningitis, encephalitis, optic neuritis, transverse myelitis, facial nerve palsies, Guillain-Barré syndrome, acute cerebellar ataxia, hemiplegia, sleep disorders, lymphocytosis, neutropenia, hemophagocytic syndrome, acquired hypogammaglobulinemia, X-linked lymphoproliferative disease, pneumonia, interstitial lung disease, pancreatitis, myocarditis, oral cavity-oral hairy leukoplakia, and EBV-associated cancers, including Burkitt’s lymphoma nasopharyngeal carcinoma, Hodgkin’s disease and non-Hodgkin’s lymphoma, post-transplant lymphoproliferative disorder, leiomyosarcomas, T-cell lymphomas, and combinations thereof. The disclosure also provides a composition for use as a medicament, e.g., for use in immunising a patient against a viral infection, e.g., EBV infection, e.g., for use in raising a neutralising immune response in a patient. The immune response raised by these methods and uses will generally include an antibody response, preferably a protective antibody response (i.e., a neutralising response). Methods for assessing antibody responses after vaccination are known in the art. Compositions and vaccines of the disclosure can be administered in a number of suitable ways, such as intramuscular injection (e.g., into the arm or leg), subcutaneous injection, intranasal administration, oral administration, intradermal administration, transcutaneous administration, transdermal administration, and the like. The appropriate route of administration will be dependent upon the age, health and other characteristics of the subject, for example, the mammal. A clinician will be able to determine an appropriate route of administration based on these and other factors. Immunogenic compositions, and vaccine formulations, may be used to treat children and adults, including pregnant women. Thus, a subject may be less than 1 year old, 1 to 5 years old, 5 to15 years old, 15 to 55 years old, or at least 55 years old. In one example, the subject is 10 years old. In one example, the subject has not yet been exposed to EBV. The vaccines are suitable for general use in a population. Viral load refers to the amount of virus in an infected person's blood, typically expressed as the number of viral particles in each millilitre of blood. The skilled person will be aware of suitable methods of measuring or determining the viral load in a subject. For example, by using reverse transcription-polymerase chain reaction (RT-PCR) tests, branched DNA (bDNA) tests, and nucleic acid sequence-based amplification (NASBA) tests. Viral load has general implications, such as indicating how fast an infection is progressing, but also has specific implications. In the case of EBV, which has a diverse range of associated diseases and conditions, EBV viral load has implications beyond simply as indicative of the nature of the EBV infection. EBV DNA testing is often performed as part of diagnostic evaluations for EBV-associated diseases, and EBV DNA in the blood is associated with disease activities. For example, the quantification of circulating EBV DNA loads has played an important role in the diagnosis and management of EBV-associated lymphoid malignancies. Viral load measurement is particularly useful for monitoring EBV-DNA in hematopoietic stem cell transplant patients, and for assessing the prognosis or response to therapy of EBV-associated intractable lymphomas like extranodal NK / T-cell lymphoma, nasal type, and to help diagnose, monitor, and predict posttransplant lymphoproliferative disorder. Treatment can be by a single dose schedule or a multiple dose schedule. Multiple doses may be used in a primary immunisation schedule and / or in a booster immunisation schedule. In a multiple dose schedule the various doses may be given by the same or different routes, e.g., a parenteral prime and mucosal boost, a mucosal prime and parenteral boost, etc. Administration of more than one dose (typically two doses) is particularly useful in immunologically naive patients. Multiple doses will typically be administered at least 1 week apart (e.g., about 2 weeks, about 3 weeks, about 4 weeks, about 6 weeks, about 8 weeks, about 10 weeks, about 12 weeks, about 16 weeks, and the like.). The methods of the present disclosure can, in addition to treatment of existing EBV infection or diseases or conditions caused by EBV infection, be used to prevent the onset of EBV infection. Thus, in one example, the subject does not have an EBV infection. The recombinant protein antigen and / or the protein subunit vaccines of the present disclosure are useful for parenteral, topical, oral, or local administration, intramuscular administration, aerosol administration, or transdermal administration, for prophylactic or for therapeutic treatment. In one example, the recombinant protein antigen and / or the protein subunit vaccines is administered parenterally, such as intramuscularly, subcutaneously or intravenously. For example, the recombinant protein antigen is administered intravenously. For example, the protein subunit vaccines is administered intravenously. Formulation of recombinant protein antigen and / or the protein subunit vaccine to be administered will vary according to the route of administration and formulation (e.g., solution, emulsion, capsule) selected. An appropriate pharmaceutical composition comprising a recombinant protein antigen and / or the protein subunit vaccine to be administered can be prepared in a physiologically acceptable carrier. For solutions or emulsions, suitable carriers include, for example, aqueous or alcoholic / aqueous solutions, emulsions or suspensions, including saline and buffered media. Parenteral vehicles can include sodium chloride solution, Ringer's dextrose, dextrose and sodium chloride, lactated Ringer's or fixed oils. A variety of appropriate aqueous carriers are known to the skilled artisan, including water, buffered water, buffered saline, polyols (e.g., glycerol, propylene glycol, liquid polyethylene glycol), dextrose solution and glycine. Intravenous vehicles can include various additives, preservatives, or fluid, nutrient or electrolyte replenishers (See, generally, Remington's Pharmaceutical Science, 16th Edition, Mack, Ed. 1980). The compositions can optionally contain pharmaceutically acceptable auxiliary substances as required to approximate physiological conditions such as pH adjusting and buffering agents and toxicity adjusting agents, for example, sodium acetate, sodium chloride, potassium chloride, calcium chloride and sodium lactate. The recombinant protein antigen and / or the protein subunit vaccines can be stored in the liquid stage or can be lyophilised for storage and reconstituted in a suitable carrier prior to use according to art-known lyophilisation and reconstitution techniques. The optimum concentration of the active ingredient(s) in the chosen medium can be determined empirically, according to procedures known to the skilled artisan, and will depend on the ultimate pharmaceutical formulation desired. Upon formulation, compositions of the present disclosure will be administered in a manner compatible with the dosage formulation and in such amount as is therapeutically / prophylactically effective. The dosage ranges for the administration of the recombinant protein antigen and / or the protein subunit vaccines of the disclosure are those large enough to produce the desired effect. For example, the composition comprises an effective amount of the recombinant protein antigen and / or the protein subunit vaccines. In one example, the composition comprises a therapeutically effective amount of recombinant protein antigen. In one example, the composition comprises a therapeutically effective amount of protein subunit vaccine. In another example, the composition comprises a prophylactically effective amount of the recombinant protein antigen. In another example, the composition comprises a prophylactically effective amount of the protein subunit vaccine. The dosage should not be so large as to cause adverse side effects. Generally, the dosage will vary with the age, condition, sex and extent of the disease in the patient and can be determined by one of skill in the art. The dosage can be adjusted by the individual physician in the event of any complication. In some examples, the recombinant protein antigen and / or the protein subunit vaccine is administered at an initial (or loading) dose which is higher than subsequent (maintenance doses). The recombinant protein antigen and / or the protein subunit vaccines can also be administered at a maintenance dose. The maintenance doses may be administered every 7–35 days, such as, every 7 or 14 or 28 days. In some examples, a dose escalation regime is used, in which the recombinant protein antigen and / or the protein subunit vaccine is initially administered at a lower dose than used in subsequent doses. This dosage regime is useful in the case of subjects initially suffering adverse events. A subject may be re-treated with the recombinant protein antigen and / or the protein subunit vaccine of the present disclosure. A subject may be re-treated with the recombinant protein antigen and / or the protein subunit vaccine, by being given more than one exposure or set of doses, such as at least about two exposures of the recombinant protein antigen and / or the protein subunit vaccine, for example, from about 2 to 60 exposures, and more particularly about 2 to 40 exposures, most particularly, about 2 to 20 exposures. In one example, any retreatment may be given when signs or symptoms of disease return. In another example, any retreatment may be given at defined intervals. For example, subsequent exposures may be administered at various intervals, such as, for example, about 24 to 28 weeks or 48 to 56 weeks or longer. For example, such exposures are administered at intervals each of about 24 to 26 weeks or about 38 to 42 weeks, or about 50 to 54 weeks. In the case of a subject that is not adequately responding to treatment, multiple doses in a week may be administered. Alternatively, or in addition, increasing doses may be administered. In another example, for subjects experiencing an adverse reaction, the initial (or loading) dose may be split over numerous days in one week or over numerous consecutive days. Administration of the recombinant protein antigen and / or the protein subunit vaccines according to the methods of the present disclosure can be continuous or intermittent, depending, for example, on the recipient's physiological condition, whether the purpose of the administration is therapeutic or prophylactic, and other factors known to skilled practitioners. The administration of the recombinant protein antigen and / or the protein subunit vaccines may be essentially continuous over a preselected period of time or may be in a series of spaced doses, e.g., either during or after development of a condition. Combination therapies In some examples, a recombinant protein antigen or a composition comprising the antigen is administered in combination with a further treatment or treatment regime. For example, the recombinant protein antigen or a composition comprising the antigen is administered prior to the further treatment or treatment regime. For example, the recombinant protein antigen or a composition comprising the antigen is administered simultaneously with or approximately contemporaneously with the further treatment or treatment regime. For example, the recombinant protein antigen or a composition comprising the antigen is administered after the further treatment or treatment regime. In some examples, a sa-mRNA of the present disclosure is administered in combination with a further treatment or treatment regime. For example, the sa-mRNA is administered prior to the further treatment or treatment regime. For example, the sa- mRNA is administered simultaneously with or approximately contemporaneously with the further treatment or treatment regime. For example, the sa-mRNA is administered after the further treatment or treatment regime. In some examples, a recombinant protein antigen or a composition comprising the antigen is administered in combination with a sa-mRNA of the present disclosure. For example, provided herein are different regiments combining the sa-mRNA of the present disclosure and the recombinant protein antigen or a composition comprising the antigen. For example, a treatment or immunisation or vaccination regimen of the present disclosure comprises a combination of the sa-mRNA vaccine and the protein subunit vaccine. In some examples, the combination of sa-mRNA and recombinant protein antigen or a composition comprising the antigen is in a proportion represented by ratio of about 1:4, about 1:3, about 1:2, about 1:1, about 2:1, about 3:1, or about 4:1. In some examples, the combination regime is a prime-boost regime. For example, sa-mRNA and recombinant protein antigen or a composition comprising the antigen is administered sequentially. For example, sa-mRNA followed by recombinant protein antigen or a composition comprising the antigen. For example, recombinant protein antigen or a composition comprising the antigen followed by sa-mRNA. For example, where the different sa-mRNA and recombinant protein antigen vaccines are administered sequentially. For example, the protein subunit vaccine followed by the sa-mRNA vaccine. For example, the sa-mRNA vaccine followed by the protein subunit vaccine. In some examples, the sa-mRNA and recombinant protein antigen or a composition comprising the antigen are delivered simultaneously or co-delivered. For example, different sa-mRNA and recombinant protein antigen vaccines are co-delivered. In some examples, the combination of sa-mRNA and recombinant protein antigen or a composition comprising the antigen provides an enhanced response in a patient suffering EBV compared to the response achieved by sa-mRNA alone or recombinant protein antigen alone. The precise treatment regimen will be determined by the skilled clinician and will depend on various factors, including the nature and phase of the symptoms, the condition of the patient, and the actual choice of therapeutic agents used. The determination of the order of administration and the number of repetitions of administration of each therapeutic agent during a treatment protocol is well within the knowledge of the skilled physician after evaluation of the disease being treated, the condition of the patient, and the disclosures of the present application. It is known to those of skill in the art that therapeutically-effective dosages can vary when the drugs are used in treatment combinations. Methods for experimentally determining therapeutically-effective dosages of drugs and other agents for use in combination treatment regimens are described in the literature. For example, the use of metronomic dosing, i.e., providing more frequent, lower doses in order to minimise toxic side effects, has been described extensively in the literature. Combination treatment further includes periodic treatments that start and stop at various times to assist with the clinical management of the patient. For combination therapies, dosages of co-administered therapeutic agents will of course vary depending on the type of co-agents employed and the condition of the patient. In some examples, any other treatment may comprise several different treatments, which treatments may occur at different time points, and the sa-mRNA and recombinant protein antigen or a composition comprising the antigen may be given prior to, contemporaneously or after any one or more of those treatments as either a single dose or as several doses and / or on several different occasions. The time period between the multiple administration steps may range from, a few minutes to several hours, depending upon the properties of each pharmaceutical agent, such as potency, solubility, bioavailability, plasma half-life and kinetic profile of the pharmaceutical agent. Circadian variation of various physiological parameters may also be evaluated to determine the optimal dose interval. Kits Another example of the disclosure provides kits containing an immunogenic composition of the present disclosure useful for the treatment or prevention of a disease or disorder as described above, for example, EBV. Another example of the disclosure provides kits containing a sa-mRNA of the present disclosure useful for the treatment or prevention of a disease or disorder as described above, fro example, EBV. Another example of the disclosure provides kits containing a pharmaceutical composition of the present disclosure useful for the treatment or prevention of a disease or disorder as described above, for example, EBV. Another example of the disclosure provides kits containing a vaccine of the present disclosure useful for the treatment or prevention of a disease or disorder as described above, for example, EBV. Another example of the disclosure provides kits containing a polynucleotide of the present disclosure useful for the treatment or prevention of a disease or disorder as described above, for example, EBV. Another example of the disclosure provides kits containing a nanoparticle of the present disclosure useful for the treatment or prevention of a disease or disorder as described above, for example, EBV. In some examples, the kit comprises (a) a container comprising a polynucleotide optionally in a delivery system and / or a pharmaceutically acceptable carrier or diluent; and (b) a package insert with instructions for treating or preventing EBV or a disease or condition associated with EBV in a subject. In some examples, the kit comprises (a) a container comprising a nanoparticle optionally in a delivery system and / or a pharmaceutically acceptable carrier or diluent; and (b) a package insert with instructions for treating or preventing EBV or a disease or condition associated with EBV in a subject. In some examples, the kit comprises (a) a container comprising a recombinant protein antigen and / or a sa-mRNA, optionally in a delivery system and / or a pharmaceutically acceptable carrier or diluent; and (b) a package insert with instructions for treating or preventing EBV or a disease or condition associated with EBV in a subject. In some examples, the kit comprises (a) a container comprising a protein subunit vaccine optionally with an adjuvant, for example MF59, optionally in a delivery system and / or a pharmaceutically acceptable carrier or diluent; and (b) a package insert with instructions for treating or preventing EBV or a disease or condition associated with EBV in a subject. In some examples, the kit comprises (a) a container comprising a pharmaceutically acceptable carrier or diluent; and (b) a package insert with instructions for treating or preventing EBV or a disease or condition associated with EBV in a subject. In one example, the kit further comprises an adjuvant. In accordance with this example of the disclosure, the package insert is on or associated with the container. Suitable containers include, for example, bottles, vials, syringes, etc. The containers may be formed from a variety of materials such as glass or plastic. The container holds or contains a composition that is effective for a disease or disorder of the disclosure and may have a sterile access port (for example, the container may be an intravenous solution bag or a vial having a stopper pierceable by a hypodermic injection needle). At least one active agent in the composition is the recombinant protein antigen and or sa-mRNA. The label or package insert indicates that the composition is used for treating a subject eligible for treatment, e.g., one having or predisposed to developing an EBV infection and / or a disease or condition associated with an EBV infection, with specific guidance regarding dosing amounts and intervals of treatment and any other medicament being provided. The kit may further comprise an additional container comprising a pharmaceutically acceptable diluent buffer, such as bacteriostatic water for injection (BWFI), phosphate-buffered saline, Ringer's solution, and / or dextrose solution. The kit may further include other materials desirable from a commercial and user standpoint, including other buffers, diluents, filters, needles, and syringes. The present disclosure includes the following non-limiting Examples. EXAMPLES Example 1: Recombinant Protein Materials and methods Antigens gP350, gP42, gL, gH, gb and gP 220 were identified as suitable targets (Figure 1), and used (Table 1). gP220 is a splice variant (~250 aa deletion 502–750 in Mucin like domain) of gP350. gB has a furin cleavage site in aa 427–434 LRRRRDA (SEQ ID NO: 8). Five recombinant proteins: gH, gL, gP42, gB and gP350 were expressed and purified for animal studies, including for mouse immunogenicity study (CRL-12) (SEQ ID NOs 1 or 40, 2 or 41, 3 or 42, 4, and 6 or 44, respectively). A protein subunit vaccine for each of gH-gL, gB mutant (mutated at furin cleavage site: amino acids WY 112–113 to HR; WLIW 193–196 to RVEA; RR469–470 to PP; SEQ ID NO: 5), gH- gL+gP42, and gP350 were produced (Figure 2). A protein subunit vaccine for recombinant gP220 was also produced. Table 1: protein subunit vaccine antigens Example 2: Vaccination with recombinant protein antigen Four protein subunit vaccines expressing five different antigens (CRL-12) were produced and a first mouse immunogenicity study performed. Protein was administered with MF59 adjuvant as per Table 3, below. ELISA and multiplex Luminex assays were optimised for all 5 vaccine antigens. 806 to 8 week-old female BALB / c mice were vaccinated on day 0 with a primary dose of 1 μg or 0.1 μg delivered in 50 μL–100 μ per leg, followed by two booster doses on days 21 and 42. Data was collected at day 63 after a total of 3 vaccine doses, as per summary Table 3. Blood (serum) was collected on days 20, 41 and 62. All protein vaccines induced strong responses (Figure 3), with some cross-reactivity with other recombinant proteins. Table 3: CRL-12 Protein Vaccines in Mice Pooled sera showed that protein vaccines induced induced antigen-specific IgG titres. Pooled sera results demonstrated EBV-neutralisation by adjuvanted recombinant gHgL and gp350. Example 3: sa-mRNA Materials and methods Antigens gP350, gP42, gL, gH, gb and gP 220 were used (Table 1). gP220 is a splice variant (~250 aa deletion 502–750 in Mucin like domain) of gP350. gB has a furin cleavage site in aa 427–434 LRRRRDA (SEQ ID NO: 37), which can be stabilised. Table 1: sa-mRNA antigens Plasmid constructs were made as per Table 2 below. Table 2: sa-mRNA constructs Constructs EBV-01, EBV-02, EBV-05, EBV-06, EBV-09, EBV-10, EBV-11 and EBV-12 (Figure 4) showed good preliminary data using in vitro potency testing and Western blot. IDMS assay was also performed. These constructs were progressed to trials. RNA quality of EBV-03, EBV-04, EBV-07, and EBV-08 was poor as in vitro transcription yielded multiple transcripts. Codon optimisation of gP220 was performed with a different algorithm (Genscript GeneSmart) instead of Geneart algorithm. It showed better RNA structure based on in silico analysis. All 4 constructs were prepared IVT RNA for formulation. Example 4: Vaccination with sa-mRNA Four sa-mRNA vaccines were produced using constructs EBV-01, EBV-02, EBV-05 and EBV-09 (Figure 4). 806 to 8 week-old female BALB / c mice were vaccinated on day 0 with a primary dose of 1 μg or 0.01 μg delivered in 50 μL–100 μ per leg, followed by two booster doses on days 21 and 42. Data was collected at day 63 after a total of 3 vaccine doses, as per summary Table 3. Blood (serum) was collected on days -1 (group 1 / A only) 20, 41 and 62. Table 3: CRL-12 sa-mRNA Vaccines in Mice Pooled sera showed that all sa-mRNA vaccines induced strong AG-specific IgG response (Figure 5). Pooled sera results demonstrated EBV-neutralisation by all vaccine candidates (gHgL, gHgLgp42, gp220, and gB) at 1 μg and for all vaccine candidates except gB at 0.01 μg (Figure 6). Example 5: Antigen production strategy for gH / gL dimer and gH / gL / gp42 hetero- trimer Lead recombinant protein candidates were identified as a gH / gL dimer, and a gH / gL / gp42 trimer. Recombinant peptides were produced according to three different strategies, namely, 1) co-purification of individual antigens, for example, co-purification of gH, gL, and gp42 (for use, for example, in a pooled recombinant peptide composition); 2) co-expression and co-purification, using multivectors and co-transfection, specifically, gH conjugated to gL, with gp42 on its own; 3) co-expression and co- purification of multicistronic single vector, namely gH conjugated to gL conjugated to gp42. Figure 7 provides a schematic of the three different strategies undertaken, as well as illustrates the location of the transmembrane regions and the CMV promoter. Figure 8 provides the structure of the exemplified gH / gL / gp42 hetero trimer. The antigen production strategy for gp350 / gp220 was performed in a similar manner, with Figure 9 providing the corresponding schematic illustrations and protein structures. Size exclusion chromatography (SEC) and SDS-PAGE gel confirmed the production and purification of all antigens, including in monomer, dimer, and trimer variations, and ELISA confirmed the binding affinity of the various antigens and antigen combinations with their anti-antigen antibodies. Purified gH / gL dimer was produced in 1:1 ratio; gH / gL / gp42 hetero-trimer in 1:1:1 ratio. Purified gp220 full-length monomer and purified gp350 / gp220-6HB trimer were also produced. Both gH / gL and gH / gL / gp42 were shown to bind with anti-gH / gL dimer antibody, and specificity was also confirmed, for example, it was demonstrated that only gH / gL / gp42 bound with the anti-gH / gL / gp42 trimer antibody. The gp220 monomer, gp220-6HB and gp350-6HB bound tightly with neutralising antibody 72A1. Example 6: Tri-cistronic constructs to enhance immunogenicity CRL-12 constructs were developed as described previously, EB-17 is the same as EB-01, and EB-18 is the same as EB-05 previously developed except that a mutation in the gH sequence (EB-01 and EB-05) was corrected in EB-17 and EB-18 (evaluated in CRL-31). Codon optimisation was performed by Geneart (gL, gH, gp42 and gB), and Genscript (gp220). Tri-cistronic constructs were further optimised. The tri-cistronic gL-gH-gp42 was optimised to reduce the expression of gp42, after some reduction in epithelial cell microneutralisation of tri-cistronic construct relative to bi-cistronic gH-gL construct was demonstrated (EB-14). This was achieved by inserting a weaker (less efficient) sub- genomic promoter (SGPv1) (SEQ ID NO: 35) to drive gp42 compared to gH and gL (SVPv2), which resulted in improved microneutralisation titres in both epithelial and B cells (Figure 10). It was demonstrated that reducing the length of the gp42 promoter (SGPv1, rather than e.g. SGPv2) reduced the expression of gp42, but enhanced gL-gH expression in EB-14 compared to EB-18 (which used SGPv2 for gp42) (Figure 11). Further, gB, gH and gL and were co-expressed in a sa-mRNA backbone, to make a tricistronic vaccine co-expressing gB with gH-gL (EB-16)(Figure 10). Example 7: CRL-31 sa-mRNA vaccination The objective of CRL-31 were to express 2–4 Antigens (gL, gH, gp42, gp220) either as multi-cistronic or co-formulations to enhance immunogenicity of top hits from CRL-12, to determine whether co-expression of gL-gH or gp220 will enhance the low immunogenicity observed for gB by keeping it in a pre-fusion state, and to compare immune responses of gp350 to gp220. The CRL-31 study was designed as per the serology studies previously described, and according to Table 4 below as a standard prime-boost vaccine regimen, but only the high dose was evaluated. Table 4: CRL-13 serology study design The CRL-31 serology study found that similar to the CRL-12 study, gHgLgp42 and gp220 sa-mRNA vaccines induced the highest neutralising titres in B cell microneutralisation (MN) assays. New gHgL-gp42 constructs (EB-18 and EB-14) performed well in this experiment in B cells, and gp220 / gp350 (EB-09 & EB-10) vaccines also performed well (no significant difference). Figure 13 depicts the results. Combining gB with gHgL, or gp220 vaccines had a minor impact on B cell EBV MN titre, but the multi-cistronic approach reduced immunogenicity (Figure 14). EBV B cell MN titres trended lower for combinations compared to EB-17 alone when combined with EB-02 (ns). Tri-cistronic EB-16 (gL-gH-gB) failed to induce EBV B cell MN titre in this assay. EBV B cell MN titres trended lower compared to EB-09 alone when combined with EB-02 (ns). Bicistronic EB-12 (gp220-gB) induced significantly lower MN titre than EB-09 (gp220). Combining gp220 with gHgL, or gHgL-gp42 vaccines had a minor impact on B cell EBV MN titre (Figure 14). EBV B cell MN titres were lower for combinations compared to EB-09 alone when combined with the EB-17 bicistronic vaccine. EBV B cell MN titres trended slightly lower compared to EB-09 alone when combined with the EB-18 tri-cistronic vaccine (ns). Combining EB-17 and EB-18 had no effect on EBV-B cell MN titres, and both v1 / v2 gL-gH-gp42 were similar (Figure 14). Both new gL-gH EB-17 and gL-gH-gp42 EB-18 constructs induced EBV B-cell MN titres. When combined with different ratios, titres were not significantly different from each other. Both v1 EB-14 and v2 EB-18 gL- gH-gp42 constructs induced EBV B-cell MN titres. No significant difference was found between v1 and v2. gHgL and gHgL-v1gp42 sa-mRNA vaccines induced the highest neutralising titres in Epithelial cell MN assay (Figure 15). Epithelial Findings: CRL-31 produced similar results to CRL-12 EBV epithelial cell MN assay: gHgL constructs (including new EB-17) performed well in EBV Epithelial MN assay, as they did in CRL-12. EB14 gHgL-v1gp42 induced high Epi-MN titres, compared to EB-18 (v2), which produced similar results to EB-05 from CRL-12 (p < 0.0001). gp220 / gp350 (EB-09 and EB-10) vaccines performed similarly to CRL-12, but EB-10 gp350 was lower than EB09 gp220 (p = 0.002). Combining gB with gHgL or gp220 vaccines had little impact on Epithelial MN titre, but the multi-cistronic approach reduced immunogenicity (Figure 16). Epithelial MN titres for EB-17 alone with EB-02 were both above ULOD. The multi-cistronic EB- 16 (gL-gH-gB) was significantly lower than gL-gH EB-17. Epithelial MN titres were lower compared to EB-09 alone when combined with EB-02 (p = 0.0201). Bicistronic EB-12 (gp220-gB) trended lower compared to EB-09, but was not significantly different (ns). Combining gp220 with gHgL, or gHgL-gp42 vaccines had no impact on Epithelial EBV MN titre compared to each alone (Figure 16). EBV Epithelial-cell MN titre was lower for EB-09 alone compared to EB-17 alone. The titre for combinations was above ULOD, similar to EB-17. EBV Epithelial-cell MN titre was higher for EB-09 alone compared to EB-18 alone. The titre for combinations was similar to EB-18, and significantly lower than EB-09 alone. EBV MN titres with EB-17 were above ULD, and adding EB-18 had no measured impact on MN titres (Figure 16). gL-gH EB-17 induced significantly higher Epithelial MN titres compared to gL-gH-gp42 EB-18. When combined with different ratios, titres were similar to EB-17, above ULOD. Epithelial-based EBV MN titres for EB-14 (v1) were above ULOD, a significantly higher titre compared to EB-18 (v2) gL-gH-gp42. CRL-31 summary: Like CRL-12 the gHgL was best for Epithelial-based MN titers, and gHgLgp42 for B cells (Figure 17). Findings: sa-mRNA vaccines to gHgL (EB-17 and EB-01), and gHgL-gp42 (EB- 14) were top candidates in epithelial cell-based EBV MN. sa-mRNA vaccines to gHgL- gp42, and gp350 / gp220 induced top neutralising antibodies in B cell-based MN. Combining new gHgL EB-17 with new gHgL-gp42 EB-18 construct increased both Epithelial or B cell-based MN titre. The data demonstrate the value of a gB component in vaccine: Combining gB EB- 02 with other constructs had no clear benefit when combined in bivalent vaccines. gB in bi- or tricistronic vaccine (EB-12 & EB-16) had negative impact compared to monocistronic gp220 or gLgH, though further optimisation of the study may provide further findings. Example 8: sa-mRNA construct design and characterisation IVT RNA of co-transcriptional sa-mRNA constructs was investigated. EB027* has several mutations in its backbone and Genscript has resynthesised this construct. Codon optimisation was performed using GeneArt, and codon optimized RNA produced were EB01, 02, and 05 Table 5: sa-mRNA constructs Table 6: sa-mRNA constructs gL-gH / gp42 constructs showed good activity in HEK293 cells (Figure 18, Table 7). Table 7: sa-mRNA construct activity in HEK293 cells Co-transcriptional capping of EB14 showed improved activity and antigen expression (Figure 19), activity improved by about 55% (Figure 19). IVT RNA of gp220 co-transcriptional sa-mRNA constructs was investigated. Table 8: sa-mRNA constructs mRNAid codon optimised RNA has increased expression, shown in Figure 20, mRNAid codon optimisation showed improved activity, shown in Figure 21. sa-mRNA constructs in ARCT platform were constructed as shown in Figure 22. The ARCT Sgp1 was 62 bp, and the Sgp for the second and third antigens was 92 bp unless specified (v1 is 49 bp). Gel plot shoed that co-transcriptional IVT improved RNA integrity. EBV antigens in ARCT sa-mRNA show comparable activity to those in the original backbone. gp220 mono-cistronic construct show comparable activity in both backbones, but the antigen expression in the ARCT construct was greater than in the original construct (Figures 23 and 24). ARCT sa-mRNA showed good in vitro activity, assessed as previously for the original construct and shown in Figures 25–27. It was demonstrated that co-transcriptional capping resulted in improved RNA activity. gL-gH constructs were similarly effective with and without codon optimisation compared to the wild type sequence. gp220 codon optimization (mRNAid with U depletion (EB47)) gave better antigen expression and activity in both interferon competent cells. The linear algorithm-designed EB50, demonstrated similarly high RNA activity in both cell types. All ARCT sa-mRNA constructs (EB51 to EB56) evaluated showed good RNA activity, and constructs with gp42 in the first position showed balanced antigen expression. Example 9: LNP formulations Sa-mRNA constructs were incorporated into LNP formulations. LNPs had the characteristics described in Table 9, below. It was demonstrated that co-transcriptional capping enhanced gp220 potency, and the capped ARCT monocistronic sa-mRNA showed greater antigen expression than the original uncapped backbone (Figure 28). ARCT tricistronic constructs with gp42 as the first gene of interest (i.e. first in the schematic representation of the sa-mRNA constructs) showed improved potency (Figure 29). Similarly to the mono-cistronic construct, co-transcriptional capping enhanced the potency of tri-cistronic constructs, and ARCT tri-cistronic sa-mRNA showed lower potency relative to original cap 1 (Figure 30). Example 10: CRL-66 EBV sa-mRNA vaccines in mice - Study 3 An in vivo study was performed using CRL-31 (heat map Figure 31) similarly to previous in vivo studies to evaluate whether candidates gp220 and gL-gH-gp42 from CRL-12 and CRL-31 produced good immunogenicity in BoBw.v1 (ARCT) sa-mRNA backbones in vivo, and to evaluate if gene of interest sequence optimization and / or co- transcriptional capping resulted in better immunogenicity in vivo. 2206 to 8 week-old BALB / c mice were vaccinated on days 0 and 21, 100μL in total (50 μL per leg). Blood collection (serum) was taken on day -1, 20, and 42, for all groups, except at day -1 which was group 1 only. Serology assays performed where the luminex assay for IgG response, and microneutralisation assays on both epithelial and b cells. Table 10: Animal study design Table 11below describes the relevant administered components and vaccines.nix nopIiLKLKLKLKLKLKLKLKLKLKL 015 6 9A4 5202 2 3 6 5 4 5NB B B0B5 5 5 0 5 5RE E E EBEBEBEBEBEBEleGoc 5-2 2dt .r3Lv4G(4 Lg-gpgl pg -Go +oc tae.1 e.HgcSlew neHg 5. o3ctv-d1v- -2S Gd-24G5. ocv- raHGg )Hg4pG02 G PH3v tr2a4 en- Lo.)4- Lg02 2+t g. g- -Lepg e g c 1 g o.o.ne2gppgw1-v-Lg gneG trBctcrtigTH HT TGTHg atnLC S RgeEf Tar-gL- e TaelC C2R R4C R5.L neolCnCnA AgAv SReReA C AgLgedp 3CG(edA G A G tnemire172737479708188 9 0p 4 4 4 4 4 4 4949 0x G G G G G G G G4G5E J J J J J J J J JGJ saaP lra / anpieN Fr L8.p E6 / tsu aioSEn4i SW 7B m / E dar 4rotoc e900417 epsy- -5-4-19-5B - 35B - UfVTBEBEBEBEE E BE+eoncicU / trt tararad liecdav o.c o.di ec Ane eAeneneN GdR+ n tpitp o.N RG G G2 2mnasricrcscs tpm4p42p4p0oit2 te nneni ercg0.g1.1 g.2l espp n2 v v5.gedoG Gnp0 e 2 - - 3m20PH Hvo22p2Gggp0 -g- -2o. L LHgC)Ag g 21p c g g -:1 laN0p1papgac no0p1Lpg11iRcacita a0e remTCel c cT5 lGJb taa-aLMs( SLSRLS pLeSoLC .So.R o.T C C A CdCcCcAc 2P2P2P1X X XPE.E EXE3.63.3.30606060N L N N N ELELELE 10101010V V V V -6A84A 55A 56A056202a1BEBEBEBtEoLTPE-4ecc ieruXTouppSW A 4055-5655627B - E B - Y EB-EBEKL tra denole.c o.iw Gtcrtar22ea4ne 4p)pene g.tng.G 1vLG1vavH- ujd-g- gHg diH H -g gL -Ag Lg,Ppil- -L2-2 Ncig4p41L ngpg pa (loitT T T caiacC C CrR oL eetPA.R R c A AS p aCytMNL Antibody-dependent cellular cytotoxicity (ADCC) was investigated (described in the schematic of Figure 32). A binding assay was performed which demonstrated binding of monoclonal mice sera to gp350, gB, and gp42 independently. ADCC activity was the highest for gHgL and gp42 sa-mRNA constructs (Figures 33 and 34). ADCC activity was the highest for sa-mRNA vaccinated animals: gHgL>sa- mRNA gp42>sa-mRNA gB. No ADCC activity was observed against gp350 antigen. There was no ADCC activity induced by any of the sera of animals vaccinated with recombinant vaccines. ADCC activity was similar for gHgL and gHgLgp42 vaccinated animals (Figure 34). Example 11: EBV pseudovirus generation To confirm the infectivity of the antigens, EBV pseudovirus (PVs)was generated according to Table 12: Table 12: EBV psuedovirus (PVs) generation gHgLgB glycoproteins were shown to be sufficient for PVs to infect epithelial cells (Figure 35), and gp42 was shown to be required to infect B cells (Figure 36). VSV EBV gBgHL, gBgHgLgp350, gBgHgLgp42, and gBgHgLgp350gp42 pseudoviruses were able to infect epithelial cells (HEK-293T). Only VSV EBV gBgHgLgp42, and gBgHgLgp350gp42 pseudoviruses were able to infect B cells (4e3). Example 12: CRL-66 EBV sa-mRNA vaccines in mice study #3 An in vivo study was performed using CRL-66 (schematic Figure 38 and heat map Figure 39) similarly to previous in vivo studies. Similar to CRL-12 the gHgL was the best performing epithelial-based microneutralisation (MN) titre, and gHgLgp42 was the best performing for B cell-based MN. sa-mRNA vaccines to gHgL-gp42, and gp350 / gp220 induced good neutralizing antibodies in both epithelial and B cell-based MN assays. Combining new gHgL EB-17 with new gHgL-gp42 EB-18 construct had little impact on either epithelial or B-based MN titres. Combining gB EB-02 with other constructs had no clear benefit when combined in bivalent vaccines. Adding gB in bi- or tricistronic vaccine (EB-12 & EB-16) had a negative impact compared to monocistronic gp220 or gLgH (Figure 39). Similar to previous in vivo studies, this study objective was to evaluate whether gp220 and gL-gH-gp42 from CRL-12 and CRL-31 produced good immunogenicity in the BoBw.v1 (ARCT) sa-mRNA backbone, and to evaluate if the gene of interest sequence order optimization and or co-transcriptional capping results in better immunogenicity. The animal study design is described in Table 13, below. 220 6 to 8 week-old BALB / c mice were vaccinated on days 0 and 21, 100μL in total (50 μL per leg). Blood collection (serum) was taken on day -1, 20, and 42, for all groups, except at day -1 which was group 1 only. Serology assays performed where the luminex assay for IgG response, and microneutralisation (MN) assays on both epithelial and b cells. Table 13: Animal study design Both gp220 and gHgLgp42-targeting vaccines induced serum antibodies that block epithelial infection by EBV (Figure 40). Like CRL-31 and CRL-12: sa-mRNA vaccines to gHgL-gp42, and gp220 induced good neutralizing antibodies in epithelial cell-based MN assay. The highest titres were observed with tri-cistronic gHgL+gp42 vaccines, including the previously tested EB-14. Both gp220 and gHgLgp42-targeting vaccines induced serum antibodies that block B cell infection by EBV. Like CRL-31 and CRL-12: sa-mRNA vaccines to gHgL-gp42, and gp220 induced good neutralizing antibodies in B cell-based MN assay (Figure 41). The highest titres were observed with tri-cistronic gHgL+gp42 vaccines, including the previously tested EB-14. CSL cap1 performed better than cap0 in gp220 vaccines, ARCT performed well, and U-depletion was lowest (Figure 42). CSL vaccines targeting gp220 showed improvement in both B and epithelial cell-based MN titres when going from cap0 to cap1, however ARCT backbone gp220 vaccines had similar or higher titres. The EB-47 vaccine with uridine depletion had a lower titre for the high dose group, although the low dose was similar to other gp220 vaccines. EB-14 (cap0) still performed well in both Epi and B cell-based MN (Figure 43). Epithelial-based MN titres were similar for all gHgLgp42 vaccines, except sgp v3.5 (EB-53). Moving gp42 into the first position, as in EB-55 and EB-56, did not decrease the MN titres in the B cell-based assay. The CSL cap1 wildtype gLgH.gp42 vaccine, EB-26, had the lowest B cell-based MN titres of all trimer-targeting vaccines. The following embodiments are specifically contemplated by the inventors: Embodiment 1. A recombinant protein antigen or a composition comprising the antigen, wherein the antigen is from an Epstein-Barr virus (EBV) and comprises at least one antigen selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220, or an antigenic fragment thereof. Embodiment 2. The recombinant protein antigen or composition of embodiment 1, further comprising a second antigen selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220, or an antigenic fragment thereof. Embodiment 3. The recombinant protein antigen or composition of embodiment 2, wherein the first and second antigens or antigenic fragments are pooled. Embodiment 4. The recombinant protein antigen or composition of embodiment 2, wherein the first and second antigens or antigenic fragments are joined by a linker. Embodiment 5. The recombinant protein antigen or composition of any one of embodiments 2 to 4, wherein the first and second antigens or antigenic fragments are different antigens or antigenic fragments thereof. Embodiment 6. The recombinant protein antigen or composition of any one of embodiments 1 to 5, further comprising a third antigen selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220 or an antigenic fragment thereof. Embodiment 7. The recombinant protein antigen or composition of embodiment 6, wherein the first and second and third antigens or antigenic fragments are pooled. Embodiment 8. The recombinant protein antigen or composition of embodiment 5, wherein the first and second antigens or antigenic fragments are joined by a linker, and / or the second and third antigens are joined by a linker. Embodiment 9. The recombinant protein antigen or composition of any one of embodiments 6 to 8, wherein the first and second and third antigens are different antigens, or antigenic fragments thereof. Embodiment 10. The recombinant protein antigen or composition of any one of embodiments 1 to 9, further comprising a fourth antigen selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220, or an antigenic fragment thereof. Embodiment 11. The recombinant protein antigen or composition of embodiment 10, wherein the first and second and third and fourth antigens or antigenic fragments are pooled. Embodiment 12. The recombinant protein antigen or composition of embodiment 10 or 11, wherein the first and second antigens or antigenic fragments are joined by a linker, and / or the second and third antigens or antigenic fragments are joined by a linker, and / or the third and fourth antigens or antigenic fragments are joined by a linker. Embodiment 13. The recombinant protein antigen or composition of any one of embodiments 10 to 12, wherein the first and second and third and fourth antigens are different antigens, or antigenic fragments thereof. Embodiment 14. The recombinant protein antigen or composition of embodiment 1, wherein the antigen is gP220, or an antigenic fragment thereof. Embodiment 15. The recombinant protein antigen or composition of any one of embodiments 1 to 14, wherein the recombinant protein antigen or composition comprises SEQ ID NO: 7, 43, or 45, or an antigenic fragment thereof. Embodiment 16. The recombinant protein antigen or composition of embodiment 1, wherein the antigen is gP350, or an antigenic fragment thereof. Embodiment 17. The recombinant protein antigen or composition of any one of embodiments 1 to 13 or embodiment 16, wherein the recombinant protein antigen or composition comprises SEQ ID NO: 6 or 44, or an antigenic fragment thereof. Embodiment 18. The recombinant protein antigen or composition of any one of embodiments 1 to 13, wherein the recombinant protein antigen or composition comprises two or more of the antigens set forth in SEQ ID NOs: 1 to 7 or 40 to 45, or an antigenic fragment thereof. Embodiment 19. The recombinant protein antigen or composition of any one of embodiments 1 to 13, wherein the recombinant protein antigen or composition comprises three or more of the antigens set forth in SEQ ID NOs: 1 to 7 or 40 to 45, or an antigenic fragment thereof. Embodiment 20. The recombinant protein antigen or composition of any one of embodiments 1 to 13, wherein the recombinant protein antigen or composition comprises four of the antigens set forth in SEQ ID NOs: 1 to 7 or 40 to 45, or an antigenic fragment thereof. Embodiment 21. The recombinant protein antigen or composition of any one of embodiments 18 to 20, wherein the recombinant protein antigen or composition comprises SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41, or an antigenic fragment thereof. Embodiment 22. The recombinant protein antigen or composition of any one of embodiments 19 to 21, wherein the recombinant protein antigen or composition comprises SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41 and SEQ ID NO: 3 or 42, or an antigenic fragment thereof. Embodiment 23. The recombinant protein antigen or composition of any one of embodiments 19 to 21, wherein the recombinant protein antigen or composition comprises SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41 and SEQ ID NO: 4, or an antigenic fragment thereof. Embodiment 24. The recombinant protein antigen or composition of any one of embodiments 19 to 21, wherein the recombinant protein antigen or composition comprises SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41 and SEQ ID NO: 7, 43, or 45, or an antigenic fragment thereof. Embodiment 25. The recombinant protein antigen or composition of any one of embodiments 19 to 21, wherein the recombinant protein antigen or composition comprises SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41 and SEQ ID NO: 3 or 42 and SEQ ID NO: 7, 43, or 45, or an antigenic fragment thereof. Embodiment 26. The recombinant protein antigen or composition of any one of embodiments 6 to 9, comprising EBV antigens gH, gL, and gp42, or antigenic fragments thereof. Embodiment 27. The recombinant protein antigen or composition of any one of embodiments 2 to 13, wherein the first and second antigens consist of the pair gH and gL, or the pair gB and gP220. Embodiment 28. A self-amplifying RNA (sa-mRNA) comprising a nucleotide sequence encoding an antigen of any one of embodiments 1 to 27 operably linked to a subgenomic (SG) promoter. Embodiment 29. The sa-mRNA of embodiment 28, wherein the SG promoter is a minimal or an extended promoter. Embodiment 30. The sa-mRNA of embodiment 28 or 29, further comprising a second nucleotide sequence encoding a second EBV antigen operably linked to a second subgenomic (SG) promoter. Embodiment 31. The sa-mRNA of embodiment 30, further comprising a third nucleotide sequence encoding a third EBV antigen operably linked to a third subgenomic (SG) promoter. Embodiment 32. A bicistronic self-amplifying RNA (sa-mRNA) comprising: a) a first nucleotide sequence encoding a first antigen of any one of embodiments 1 to 27 operably linked to a subgenomic (SG) promoter; and b) a second nucleotide sequence encoding a second antigen of any one of embodiments 1 to 27 operably linked to a second SG promoter. Embodiment 33. The bicistronic sa-mRNA of embodiment 32, wherein the first SG promoter is a minimal promoter and the second SG promoter is an extended promoter. Embodiment 34. The bicistronic sa-mRNA of embodiment 32, wherein the first SG promoter is an extended promoter and the second SG promoter is an extended promoter. Embodiment 35. The bicistronic sa-mRNA of any one of embodiments 32 to 34,wherein the sa-mRNA comprises, in order from 5 to 3 :a) a first nucleotide sequence encoding gL operably linked to a SG promoter; and a second nucleotide sequence encoding gH operably linked to a SG promoter; or b) a first nucleotide sequence encoding gB operably linked to a SG promoter; and a second nucleotide sequence encoding gP220 operably linked to a SG promoter; or c) a first nucleotide sequence encoding gP220 operably linked to a SG promoter; and a second nucleotide sequence encoding gB operably linked to a SG promoter. Embodiment 36. A multicistronic self-amplifying RNA (sa-mRNA) comprising: a) a first nucleotide sequence encoding a first antigen operably linked to a subgenomic (SG) promoter; and b) a second nucleotide sequence encoding a second antigen operably linked to a second SG promoter; c) a third nucleotide sequence encoding a third antigen operatively linked to a third SG promoter; and d) optionally a fourth nucleotide sequence encoding a fourth antigen operatively linked to a fourth SG promoter, wherein the first and second and third and optional fourth antigens are the antigens of any one of embodiments 1 to 27. Embodiment 37. The multicistronic sa-mRNA of embodiment 36, wherein the sa-mRNA comprises, in order from 5 to 3 :a) a first nucleotide sequence encoding a first antigen operably linked to a SG promoter; b) a second nucleotide sequence encoding a second antigen operably linked to a SG SG promoter; and c) a third nucleotide sequence encoding a third antigen operably linked to a SG promoter. Embodiment 38. The multicistronic sa-mRNA of embodiment 36 or 37, wherein the first SG promoter is a minimal promoter and the second SG promoter is an extended promoter and the third SG promoter is an extended promoter and the optional fourth SG promoter is an extended promoter. Embodiment 39. The multicistronic sa-mRNA of any one of embodiments 36 to 38, wherein the sa-mRNA comprises one or more additional nucleotide sequences, wherein each sequence encodes an additional EBV antigen operably linked to a SGpromoter, and wherein the one or more nucleotide sequences are located 3 of the thirdnucleotide sequence. Embodiment 40. The multicistronic sa-mRNA of any one of embodiments 36 to 39, wherein the first and second and third antigens consist of any combination of each of gL, gH, and gP42. Embodiment 41. The multicistronic sa-mRNA of any one of embodiments 36 to40, wherein the sa-mRNA comprises, in order from 5 to 3 :a) a first nucleotide sequence encoding gH operably linked to a SG promoter; b) a second nucleotide sequence encoding gL operably linked to a SG promoter; and c) a third nucleotide sequence encoding gP42 operably linked to a SG promoter. Embodiment 42. The multicistronic sa-mRNA of any one of embodiments 36 to 39, wherein the first and second and third antigens consist of any combination of each of gL, gH, and gB. Embodiment 43. The multicistronic sa-mRNA of any one of embodiments 36 to39 or 42, wherein the sa-mRNA comprises, in order from 5 to 3 :a) a first nucleotide sequence encoding gL operably linked to a SG promoter; b) a second nucleotide sequence encoding gH operably linked to a SG promoter; and c) a third nucleotide sequence encoding gB operably linked to a SG promoter. Embodiment 44. The multicistronic sa-mRNA of any one of embodiments 36 to 39, wherein the first and second and third antigens consist of any combination of each of gL, gH, and gP220. Embodiment 45. The multicistronic sa-mRNA of any one of embodiments 36 to39 and 44, wherein the sa-mRNA comprises, in order from 5 to 3 :a) a first nucleotide sequence encoding gL operably linked to a SG promoter; b) a second nucleotide sequence encoding gH operably linked to a SG promoter; and c) a third nucleotide sequence encoding gP220 operably linked to a SG promoter. Embodiment 46. The multicistronic sa-mRNA of any one of embodiments 36 to39, wherein the sa-mRNA comprises, in order from 5 to 3 :a) a first nucleotide sequence encoding gL operably linked to a SG promoter; b) a second nucleotide sequence encoding gH operably linked to a SG promoter; c) a third nucleotide sequence encoding gP42 operably linked to a SG promoter; and d) a fourth nucleotide sequence encoding gP220 operably linked to a SG promoter. Embodiment 47. The sa-mRNA of any one of embodiments 28 to 46, wherein the antigen is codon optimised. Embodiment 48. The sa-mRNA of any one of embodiments 28 to 47, wherein the SG promoter is encoded by a sequence comprising SEQ ID NOs: 25, 26, and / or 35. Embodiment 49. The sa-mRNA of any one of embodiments 28 to 48, wherein the sa-mRNA is from an alphavirus. Embodiment 50. The sa-mRNA of embodiment 49, wherein the alphavirus is selected from the group consisting of Semliki Forest virus (SFV), Sindbis virus (SIN), and Venezuelan equine encephalitis virus (VEEV), and combinations thereof. Embodiment 51. The sa-mRNA of any one of embodiments 28 to 50, wherein the sa-mRNA comprises a sequence set forth in any one or more of SEQ ID NOs: 23 to 28. Embodiment 52. The sa-mRNA of any one of embodiments 28 to 51, wherein the sa-mRNA is encoded by a sequence set forth in any one or more of SEQ ID NOs: 27 to 34. Embodiment 53. A polynucleotide encoding the sa-mRNA of any one of embodiments 28 to 52. Embodiment 54. The polynucleotide of embodiment 53, wherein the polynucleotide is RNA. Embodiment 55. The polynucleotide of embodiment 53, wherein the polynucleotide is a recombinant DNA. Embodiment 56. The polynucleotide of embodiment 55, wherein the recombinant DNA is a plasmid. Embodiment 57. The polynucleotide of embodiment 56, wherein the plasmid comprises a sequence set forth in any one of SEQ ID NOs: 27 to 34. Embodiment 58. A nanoparticle comprising the sa-mRNA of any one of embodiments 28 to 52 or the polynucleotide of any one of embodiments 53 to 57. Embodiment 59. A protein subunit vaccine comprising The recombinant protein antigen or composition of any one of embodiments 1 to 27. Embodiment 60. The protein subunit vaccine comprises a sequence having at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 90% at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99% or 100% identity to any one of SEQ ID NOs: 1 to 7 or 40 to 45. Embodiment 61. A monovalent protein subunit vaccine comprising any one of recombinant EBV antigens selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220, or an antigenic fragment thereof. Embodiment 62. The monovalent protein subunit vaccine of embodiment 61, wherein the recombinant antigen is gp350, or an antigenic fragment thereof. Embodiment 63. The monovalent protein subunit vaccine of embodiment 61, wherein the recombinant antigen is gp220, or an antigenic fragment thereof. Embodiment 63. The monovalent protein subunit vaccine of embodiment 61, wherein the antigen comprises one of the amino acid sequences set forth in SEQ ID NOs: 1 to 7 or 40 to 45, or an antigenic fragment thereof. Embodiment 64. The monovalent protein subunit vaccine of embodiment 61, wherein the antigen comprises the amino acid sequences set forth in SEQ ID NO: 6 or 44, or an antigenic fragment thereof. Embodiment 65. The monovalent protein subunit vaccine of embodiment 61, wherein the antigen comprises the amino acid sequences set forth in SEQ ID NO: 7, 43, or 45, or an antigenic fragment thereof. Embodiment 66. A bivalent protein subunit vaccine comprising any two of recombinant EBV antigens selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220, or an antigenic fragment thereof. Embodiment 67. The bivalent protein subunit vaccine of embodiment 66, wherein the recombinant EBV antigens are gH and gL, or an antigenic fragment thereof. Embodiment 68. The bivalent protein subunit vaccine of embodiment 66, wherein the antigen comprises one of the amino acid sequences set forth in SEQ ID NOs: 1 to 7 or 40 to 45, or an antigenic fragment thereof. Embodiment 69. The bivalent protein subunit vaccine of embodiment 66, wherein the antigen comprises the amino acid sequences SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41, or an antigenic fragment thereof. Embodiment 70. The bivalent protein subunit vaccine of embodiment 66, wherein the recombinant EBV antigens are gB and gp220, or an antigenic fragment thereof. Embodiment 71. The bivalent protein subunit vaccine of embodiment 66, wherein the antigen comprises the amino acid sequences SEQ ID NO: 4 or 5 and SEQ ID NO: 7, 43, or 45, or an antigenic fragment thereof. Embodiment 72. A trivalent protein subunit vaccine comprising any three of recombinant EBV antigens selected from the group comprising: gP350, gP42, gL, gH, gB, and gP220, or an antigenic fragment thereof. Embodiment 73. The trivalent protein subunit vaccine of embodiment 72, wherein the antigen comprises three of the amino acid sequences set forth in SEQ ID NOs: 1 to 7 or 40 to 45, or an antigenic fragment thereof. Embodiment 74. The trivalent protein subunit vaccine of embodiment 72 or 73, wherein the antigens are gH, gL and gP42, or an antigenic fragment thereof. Embodiment 75. The trivalent protein subunit vaccine of any one of embodiments 72 to 74, wherein the antigen comprises the amino acid sequences SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41 and SEQ ID NO: 3 or 42, or an antigenic fragment thereof. Embodiment 76. The trivalent protein subunit vaccine of embodiment 72 or 73, wherein the antigens are gH, gL and gB, or an antigenic fragment thereof. Embodiment 77. The trivalent protein subunit vaccine of any one of embodiment 72, 73, or 76, wherein the antigen comprises the amino acid sequences SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41 and SEQ ID NO: 4, or an antigenic fragment thereof. Embodiment 78. The trivalent protein subunit vaccine of embodiment 72 or 73, wherein the antigens are gH, gL and gP220, or an antigenic fragment thereof. Embodiment 79. The trivalent protein subunit vaccine of any one of embodiments 72, 73, or 78, wherein the antigen comprises the amino acid sequences SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41 and SEQ ID NO: 7, 43, or 45, or an antigenic fragment thereof. Embodiment 80. A multivalent protein subunit vaccine comprising any four of recombinant EBV antigens selected from the group comprising: gP350, gP42, gL, gH, gB, and gP220, or an antigenic fragment thereof. Embodiment 81. The multivalent protein subunit vaccine of embodiment 80, wherein the antigens are gH, gL gP42, and gP220, or an antigenic fragment thereof. Embodiment 82. The multivalent protein subunit vaccine of embodiment 80 or 81, wherein the antigen comprises three of the amino acid sequences set forth in SEQ ID NOs: 1 to 7 or 40 to 45, or an antigenic fragment thereof. Embodiment 83. The multivalent protein subunit vaccine of any one of embodiments 80 to 82, wherein the antigen comprises the amino acid sequences SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41 and SEQ ID NO: 3 or 42 and SEQ ID NO: 7, 43, or 45, or an antigenic fragment thereof. Embodiment 84. An immunogenic composition comprising The recombinant protein antigen or composition of any one of embodiments 1 to 27 and / or the sa-mRNA of any one of embodiments 28 to 52. Embodiment 85. The immunogenic composition of embodiment 84, comprising a plurality of recombinant protein antigens of any one of embodiments 1 to 27 and / or a plurality of the sa-mRNA of any one of embodiments 28 to 52. Embodiment 86. The immunogenic composition of embodiment 85, wherein the plurality of recombinant protein antigens comprises different polypeptide antigen sequences or an antigenic fragment thereof, and / or each of the plurality of sa-mRNA encodes different polypeptide antigen sequences. Embodiment 87. The immunogenic composition of any one of embodiments 84 to 86, further comprising an adjuvant. Embodiment 88. The immunogenic composition of embodiment 55, wherein the adjuvant is MF59 and / or a nanoparticle. Embodiment 89. A pharmaceutical composition comprising an immunogenic composition of embodiments 84 to 88 and a pharmaceutically acceptable carrier. Embodiment 90. The pharmaceutical composition of embodiment 89, further comprising a lipid nanoparticle (LNP), a polymeric microparticle, an oil-in-water emulsion, or other adjuvant. Embodiment 91. The pharmaceutical composition of embodiment 89 or 90, wherein the sa-mRNA is encapsulated in, bound to or adsorbed on a LNP, a polymeric microparticle or an oil-in-water emulsion. Embodiment 92. The nanoparticle of embodiment 58, the immunogenic composition of any one of embodiments 84 to 88, or the pharmaceutical composition of any one of embodiments 89 to 91 for use as a vaccine. Embodiment 93. The protein subunit vaccine of any one of embodiments 59 to 83, the nanoparticle of embodiment 58, the immunogenic composition of any one of embodiments 84 to 88, the pharmaceutical composition of any one of embodiments 89 to 91, or the vaccine of embodiment 92, for use in the treatment or prevention or delaying progression of an EBV infection or a disease or condition caused by EBV infection. Embodiment 94. A method of treating or preventing or delaying progression of a disease or condition in a subject, the method comprising administering The recombinant protein antigen or composition of any one of embodiments 1 to 27, the sa-mRNA of any one of embodiments 28 to 52, the protein subunit vaccine of any one of embodiments 59 to 83, the nanoparticle of embodiment 58, the immunogenic composition of any one of embodiments 84 to 88, the pharmaceutical composition of any one of embodiments 89 to 91, or the vaccine of embodiment 92, to a subject in need thereof. Embodiment 95. Use of The recombinant protein antigen or composition of any one of embodiments 1 to 27, the sa-mRNA of any one of embodiments 28 to 52, the polynucleotide of any one of embodiments 53 to 57, the protein subunit vaccine of any one of embodiments 59 to 83, the nanoparticle of embodiment 58, the immunogenic composition of any one of embodiments 84 to 88, or the pharmaceutical composition of any one of embodiments 89 to 91, in the manufacture of a medicament for treating or preventing or delaying progression of a disease or condition in a subject in need thereof. Embodiment 96. The method of embodiment 94, or the use of embodiment 95, wherein the disease or condition is an EBV infection, or a disease or condition caused by an EBV infection. Embodiment 97. The method or use of embodiment 96, wherein the disease or condition caused by EBV infection is selected from the group consisting of infectious mononucleosis (glandular fever), viral meningitis, encephalitis, optic neuritis, transverse myelitis, facial nerve palsies, Guillain-Barré syndrome, acute cerebellar ataxia, hemiplegia, sleep disorders, lymphocytosis, neutropenia, hemophagocytic syndrome, acquired hypogammaglobulinemia, X-linked lymphoproliferative disease, pneumonia, interstitial lung disease, pancreatitis, myocarditis, oral cavity-oral hairy leukoplakia, and EBV-associated cancers, including Burkitt’s lymphoma nasopharyngeal carcinoma, Hodgkin’s disease and non-Hodgkin’s lymphoma, post-transplant lymphoproliferative disorder, leiomyosarcomas, T-cell lymphomas, and combinations thereof. Embodiment 98. A method of inducing an immune response in a subject, the method comprising administering The recombinant protein antigen or composition of any one of embodiments 1 to 27, the sa-mRNA of any one of embodiments 28 to 52, the polynucleotide of any one of embodiments 53 to 57, the protein subunit vaccine of any one of embodiments 59 to 83, the nanoparticle of embodiment 58, the immunogenic composition of any one of embodiments 84 to 88, or the pharmaceutical composition of any one of embodiments 89 to 91, or the vaccine of embodiment 92, to a subject in need thereof. Embodiment 99. Use of The recombinant protein antigen or composition of any one of embodiments 1 to 27, the sa-mRNA of any one of embodiments 28 to 52, the polynucleotide of any one of embodiments 53 to 57, the protein subunit vaccine of any one of embodiments 59 to 83, the nanoparticle of embodiment 58, the immunogenic composition of any one of embodiments 84 to 88, or the pharmaceutical composition of any one of embodiments 89 to 91, in the manufacture of a medicament for inducing an immune response in a subject in need thereof. Embodiment 100. A method of immunising a subject, the method comprising administering The recombinant protein antigen or composition of any one of embodiments 1 to 27, the sa-mRNA of any one of embodiments 28 to 52, the polynucleotide of any one of embodiments 53 to 57, the protein subunit vaccine of any one of embodiments 59 to 83, the nanoparticle of embodiment 58, the immunogenic composition of any one of embodiments 84 to 88, or the pharmaceutical composition of any one of embodiments 89 to 91, or the vaccine of embodiment 92 to the subject. Embodiment 101. Use of The recombinant protein antigen or composition of any one of embodiments 1 to 27, the sa-mRNA of any one of embodiments 28 to 52, the polynucleotide of any one of embodiments 53 to 57, the protein subunit vaccine of any one of embodiments 59 to 83, the nanoparticle of embodiment 58, the immunogenic composition of any one of embodiments 84 to 88, or the pharmaceutical composition of any one of embodiments 89 to 91, or the vaccine of embodiment 92 in the preparation of a medicament for reducing viral load in a subject having an EBV viral infection or a disease or condition caused by an EBV infection. Embodiment 102. The recombinant protein antigen or composition of any one of embodiments 1 to 27, the sa-mRNA of any one of embodiments 28 to 52, the polynucleotide of any one of embodiments 53 to 57, the protein subunit vaccine of any one of embodiments 59 to 83, the nanoparticle of embodiment 58, the immunogenic composition of any one of embodiments 84 to 88, or the pharmaceutical composition of any one of embodiments 89 to 91,, or the vaccine of embodiment 92, for use in reducing viral load in a subject having an EBV viral infection or a disease or condition caused by an EBV infection. Embodiment 103. A kit comprising at least one of The recombinant protein antigen or composition of any one of embodiments 1 to 27, the sa-mRNA of any one of embodiments 28 to 52, the polynucleotide of any one of embodiments 53 to 57, the protein subunit vaccine of any one of embodiments 59 to 83, the nanoparticle of embodiment 58, the immunogenic composition of any one of embodiments 84 to 88, or the pharmaceutical composition of any one of embodiments 89 to 91, or the vaccine of embodiment 92, optionally in a delivery system, and / or a pharmaceutically acceptable carrier or diluent, packaged with instructions to administer The recombinant protein antigen or composition and / or protein subunit vaccine to a subject who is suffering from or at risk of suffering from an EBV infection or a disease or condition caused by an EBV infection. Embodiment 104. The kit of embodiment 103, wherein the recombinant protein antigen, the sa-mRNA, the polynucleotide, the protein subunit vaccine, the nanoparticle, the immunogenic composition, the pharmaceutical composition, or the vaccine is supplied in a vial. Embodiment 105. The kit of embodiment 104, wherein the recombinant protein antigen, the sa-mRNA, the polynucleotide, the protein subunit vaccine, the nanoparticle, the immunogenic composition, the pharmaceutical composition, or the vaccine is supplied in a syringe.

Claims

CLAIMS 1. A recombinant protein antigen or a composition comprising the antigen, wherein the antigen is from an Epstein-Barr virus (EBV) and comprises at least one antigen selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220, or an antigenic fragment thereof.

2. The recombinant protein antigen or composition of claim 1, further comprising a second antigen selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220, or an antigenic fragment thereof.

3. The recombinant protein antigen or composition of claim 2, wherein the first and second antigens or antigenic fragments are pooled.

4. The recombinant protein antigen or composition of claim 2, wherein the first and second antigens or antigenic fragments are joined by a linker.

5. The recombinant protein antigen or composition of claim 2, wherein the first and second antigens or antigenic fragments are different antigens or antigenic fragments thereof.

6. The recombinant protein antigen or composition of claim 1, further comprising a third antigen selected from the group comprising: gP350; gP42; gL; gH; gB; and gP220 or an antigenic fragment thereof.

7. The recombinant protein antigen or composition of claim 6, wherein the first and second and third antigens or antigenic fragments are pooled.

8. The recombinant protein antigen or composition of claim 5, wherein the first and second antigens or antigenic fragments are joined by a linker, and / or the second and third antigens are joined by a linker.

9. The recombinant protein antigen or composition of claim 6, wherein the first and second and third antigens are different antigens, or antigenic fragments thereof.

10. The recombinant protein antigen or composition of claim 1, wherein the recombinant protein antigen or composition comprises two or more of the antigens set forth in SEQ ID NOs: 1 to 7 or 40 to 45, or an antigenic fragment thereof.

11. The recombinant protein antigen or composition of claim 1, wherein the recombinant protein antigen or composition comprises three or more of the antigens set forth in SEQ ID NOs: 1 to 7 or 40 to 45, or an antigenic fragment thereof.

12. The recombinant protein antigen or composition of claim 12, wherein the recombinant protein antigen or composition comprises SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41, or an antigenic fragment thereof.

13. The recombinant protein antigen or composition of claim 12, wherein the recombinant protein antigen or composition comprises SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41 and SEQ ID NO: 3 or 42, or an antigenic fragment thereof.

14. The recombinant protein antigen or composition of claim 6, comprising EBV antigens gH, gL, and gp42, or antigenic fragments thereof.

15. The recombinant protein antigen or composition of claim 2, wherein the first and second antigens consist of the pair gH and gL, or the pair gB and gP220 16. A self-amplifying RNA (sa-mRNA) comprising a nucleotide sequence encoding an antigen of claim 1 operably linked to a subgenomic (SG) promoter.

17. The sa-mRNA of claim 16, wherein the SG promoter is a minimal or an extended promoter.

18. The sa-mRNA of claim 16, further comprising a second nucleotide sequence encoding a second EBV antigen operably linked to a second subgenomic (SG) promoter.

19. The sa-mRNA of claim 18, further comprising a third nucleotide sequence encoding a third EBV antigen operably linked to a third subgenomic (SG) promoter.

20. A bicistronic self-amplifying RNA (sa-mRNA) comprising:a) a first nucleotide sequence encoding a first antigen of claim 1 operably linked to a subgenomic (SG) promoter; and b) a second nucleotide sequence encoding a second antigen of claim 1 operably linked to a second SG promoter.

21. The bicistronic sa-mRNA of claim 20, wherein the first SG promoter is a minimal promoter and the second SG promoter is an extended promoter.

22. The bicistronic sa-mRNA of claim 20, wherein the first SG promoter is an extended promoter and the second SG promoter is an extended promoter.

23. The bicistronic sa-mRNA of claim 20, wherein the sa-mRNA comprises, in orderfrom 5 to 3 :a) a first nucleotide sequence encoding gL operably linked to a SG promoter; and a second nucleotide sequence encoding gH operably linked to a SG promoter; or b) a first nucleotide sequence encoding gB operably linked to a SG promoter; and a second nucleotide sequence encoding gP220 operably linked to a SG promoter; or c) a first nucleotide sequence encoding gP220 operably linked to a SG promoter; and a second nucleotide sequence encoding gB operably linked to a SG promoter.

24. A multicistronic self-amplifying RNA (sa-mRNA) comprising: a) a first nucleotide sequence encoding a first antigen operably linked to a subgenomic (SG) promoter; and b) a second nucleotide sequence encoding a second antigen operably linked to a second SG promoter; c) a third nucleotide sequence encoding a third antigen operatively linked to a third SG promoter; and d) optionally a fourth nucleotide sequence encoding a fourth antigen operatively linked to a fourth SG promoter, wherein the first and second and third and optional fourth antigens are the antigens of claim 1.

25. The multicistronic sa-mRNA of claim 24, wherein the sa-mRNA comprises, inorder from 5 to 3 :a) a first nucleotide sequence encoding a first antigen operably linked to a SG promoter;b) a second nucleotide sequence encoding a second antigen operably linked to a SG SG promoter; and c) a third nucleotide sequence encoding a third antigen operably linked to a SG promoter.

26. The multicistronic sa-mRNA of claim 24, wherein the first SG promoter is a minimal promoter and the second SG promoter is an extended promoter and the third SG promoter is an extended promoter and the optional fourth SG promoter is an extended promoter.

27. The multicistronic sa-mRNA of claim 36, wherein the sa-mRNA comprises one or more additional nucleotide sequences, wherein each sequence encodes an additional EBV antigen operably linked to a SG promoter, and wherein the one or more nucleotidesequences are located 3 of the third nucleotide sequence.

28. The multicistronic sa-mRNA of claim 24, wherein the first and second and third antigens consist of any combination of each of gL, gH, and gP42.

29. The sa-mRNA of claim 28, wherein the antigen is codon optimised.

30. A nanoparticle comprising the sa-mRNA of claim 16.

31. A protein subunit vaccine comprising the recombinant protein antigen or composition of claim 1.

32. The protein subunit vaccine of claim 31, wherein the recombinant protein antigen or composition comprises a sequence having at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 90% at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99% or 100% identity to any one of SEQ ID NOs: 1 to 7 or 40 to 45.

33. A trivalent protein subunit vaccine comprising any three of recombinant EBV antigens selected from the group comprising: gP350, gP42, gL, gH, gB, and gP220, or an antigenic fragment thereof.

34. The trivalent protein subunit vaccine of claim 33, wherein the antigen comprises three of the amino acid sequences set forth in SEQ ID NOs: 1 to 7 or 40 to 45, or an antigenic fragment thereof.

35. The trivalent protein subunit vaccine of claim 33, wherein the antigens are gH, gL and gP42, or an antigenic fragment thereof.

36. The trivalent protein subunit vaccine of claim 33, wherein the antigen comprises the amino acid sequences SEQ ID NO: 1 or 40 and SEQ ID NO: 2 or 41 and SEQ ID NO: 3 or 42, or an antigenic fragment thereof.

37. An immunogenic composition comprising the recombinant protein antigen or composition of claim 1 and / or the sa-mRNA of claim 16.

38. The immunogenic composition of claim 37, comprising a plurality of recombinant protein antigens of claim 1 and / or a plurality of the sa-mRNA of claim 16.

39. The immunogenic composition of claim 38, wherein the plurality of recombinant protein antigens comprises different polypeptide antigen sequences or an antigenic fragment thereof, and / or each of the plurality of sa-mRNA encodes different polypeptide antigen sequences.

40. The immunogenic composition of claim 37, further comprising an adjuvant.

41. The immunogenic composition of claim 37, wherein the adjuvant is MF59 and / or a nanoparticle.

42. A pharmaceutical composition comprising an immunogenic composition of claim 37 and a pharmaceutically acceptable carrier.

43. The pharmaceutical composition of claim 42, further comprising a lipid nanoparticle (LNP), a polymeric microparticle, an oil-in-water emulsion, or other adjuvant.

44. The pharmaceutical composition of claim 42, wherein the sa-mRNA is encapsulated in, bound to or adsorbed on a LNP, a polymeric microparticle or an oil-in- water emulsion.

45. The nanoparticle of claim 30, the immunogenic composition of claim 37, or the pharmaceutical composition of claim 42 for use as a vaccine.

46. A method of treating or preventing or delaying progression of a disease or condition in a subject, the method comprising administering the recombinant protein antigen or composition of claim 1, the sa-mRNA of claim 16, the protein subunit vaccine of claim 31, the nanoparticle of claim 30, the immunogenic composition of claim 37, the pharmaceutical composition of claim 42, or the vaccine of claim 45, to a subject in need thereof.

47. The method of claim 46, or the use of claim 45, wherein the disease or condition is an EBV infection, or a disease or condition caused by an EBV infection.

48. The method or use of claim 47, wherein the disease or condition caused by EBV infection is selected from the group consisting of infectious mononucleosis (glandular fever), viral meningitis, encephalitis, optic neuritis, transverse myelitis, facial nerve palsies, Guillain-Barré syndrome, acute cerebellar ataxia, hemiplegia, sleep disorders, lymphocytosis, neutropenia, hemophagocytic syndrome, acquired hypogammaglobulinemia, X-linked lymphoproliferative disease, pneumonia, interstitial lung disease, pancreatitis, myocarditis, oral cavity-oral hairy leukoplakia, and EBV- associated cancers, including Burkitt’s lymphoma nasopharyngeal carcinoma, Hodgkin’s disease and non-Hodgkin’s lymphoma, post-transplant lymphoproliferative disorder, leiomyosarcomas, T-cell lymphomas, and combinations thereof.

49. A method of inducing an immune response in a subject, the method comprising administering the recombinant protein antigen or composition of claim 1, the sa-mRNA of 16, the nanoparticle of claim 30, the protein subunit vaccine of claim 31, the immunogenic composition of claim 37, the pharmaceutical composition of 42, or the vaccine of claim 45, to a subject in need thereof.

50. A method of immunising a subject, the method comprising administering The recombinant protein antigen or composition of claim 1 the sa-mRNA of 16, thenanoparticle of claim 30, the protein subunit vaccine of claim31, the immunogenic composition of claim37, the pharmaceutical composition of claim 42, or the vaccine of claim 45 to the subject.

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