SYNTHETIC PEPTIDES AND USES THEREFORE

Abstract: A synthetic polypeptide is disclosed, which comprises a plurality of different segments of at least one parent polypeptide, wherein the segments are linked together in a different relationship relative to their linkage in the at least one parent polypeptide to impede, abrogate or otherwise alter at least one function associated with the parent polypeptide. Synthetic polynucleotides are also disclosed that code for the synthetic polypeptides of the invention as well as expression constructs comprising the synthetic polynucleotides. Also disclosed are methods for constructing the aforementioned molecules and immunopotentiating compositions and methods for treating and/or preventing a disease or condition.

Description: Synthetic Peptides And Uses Therefore. FIELD OF THE INVENTION THIS INVENTION relates generally to agents for modulating immune responses. More particularly, the present invention relates to a synthetic polypeptide comprising a plurality of different segments of a parent polypeptide, wherein the segments are linked to each other such that one or more functions of the parent polypeptide are impeded, abrogated or otherwise altered and such that the synthetic polypeptide, when introduced into a suitable host, can elicit an immune response against the parent polypeptide. The invention also relates to synthetic polynucleotides encoding the synthetic polypeptides and to synthetic constructs comprising these polynucleotides. The invention further relates to the use of the polypeptides and polynucleotides of the invention in compositions for modulating immune responses. The invention also extends to methods of using such compositions for prophylactic and/or therapeutic purposes. Bibliographic details of various publications referred to in this specification are collected at the end of the description. BACKGROUND OF THE INVENTION The modern reductionist approach to vaccine and therapy development has been pursued for a number of decades and attempts to focus only on those parts of pathogens or of cancer proteins which are relevant to the immune system. To date the performance of this approach has been relatively poor considering the vigorous research carried out and the number of effective vaccines and therapies that it has produced. This approach is still being actively pursued, however, despite its poor performance because vaccines developed using this approach are often extremely safe and because only by completely understanding the immune system can new vaccine strategies be developed. One area that has benefited greatly from research efforts is knowledge about how the adaptive immune system operates and more specifically how T and B cells learn to recognise specific parts of pathogens and cancers. T cells are mainly involved in cell- mediated immunity whereas B cells are involved in the generation of antibody-mediated immunity. The two most important types of T cells involved in adaptive cellular immunity are αβ CD8 + cytotoxic T lymphocytes (CTL) and CD4 + T helper lymphocytes. CTL are important mediators of cellular immunity against many viruses, tumours, some bacteria and some parasites because they are able to kill infected cells directly and secrete various factors which can have powerful effects on. the spread of infectious organisms. CTLs recognise epitopes derived from foreign intracellular proteins, which are 8-10 amino acids long and which are presented by class I major histocompatibility complex (MHC) molecules (in humans called human lymphocyte antigens - HLAs) (Jardetzky et al, 1991; Fremont et al, 1992; Rotzschke et al, 1990). T helper cells enhance and regulate CTL responses and are necessary for the establishment of long-lived memory CTL. They also inhibit infectious organisms by secreting cytokines such as IFN-γ. T helper cells recognise epitopes derived mostly from extracellular proteins which are 12-25 amino acids long and which are presented by class II MHC molecules (Chicz et al, 1993; Newcomb et al, 1993). B cells, or more specifically the antibodies they secrete, are important mediators in the control and clearance of mostly extracellular organisms. Antibodies recognise mainly conformational determinants on the surface of organisms, for example, although sometimes they may recognise short linear determinants. Despite significant advances towards understanding how T and linear B cell epitopes are processed and presented to the immune system, the full potential of epitope- based vaccines has not been fully exploited. The main reason for this is the large number of different T cell epitopes, which have to be included into such vaccines to cover the extreme HLA polymorphism in the human population. The human HLA diversity is one of the main reasons why whole pathogen vaccines frequently provide better population coverage than subunit or peptide-based vaccine strategies. There is a range of epitope- based strategies though which have tried to solve this problem, e.g., peptide blends, peptide conjugates and polyepitope vaccines (ie comprising strings of multiple epitopes) (Dyall et al, 1995; Thomson et al, 1996; Thomson et al, 1998; Thomson et al, 1998). These approaches however will always be sub optimal not only because of the slow pace of epitope characterisation but also, because it is virtually impossible for them to cover every existing HLA polymorphism in the population. A number of strategies have sought to avoid both problems by not identifying epitopes and instead incorporating larger amounts of sequence information e.g., approaches using whole genes or proteins and approaches that mix multiple protein or gene sequences together. The proteins used by these strategies however sometimes still function and therefore can compromise vaccine safety e.g., whole cancer proteins. Alternative strategies have tried to improve the safety of vaccines by fragmenting the genes and expressing them either separately or as complex mixtures e.g., library DNA immunisation or by ligating such fragments back together. These approaches are still sub-optimal because they are too complex, generate poor levels of immunity, cannot guarantee that all proteins no longer function and/or that all fragments are present, which compromises substantially complete immunological coverage. The lack of a safe and efficient vaccine strategy that can provide substantially complete immunological coverage is an important problem, especially when trying to develop vaccines against rapidly mutating and persistent viruses such as HIV and hepatitis C virus, because partial population coverage could allow vaccine-resistant pathogens to re- emerge in the future. Human immunodeficiency virus (HIV) is an RNA lentiviras virus approximately 9 kb in length, which infects CD4 + T cells, causing T cell decline and AIDS typically 3-8 years after infection. It is currently the most serious human viral infection, evidenced by the number of people currently infected with HIV or who have died from AIDS, estimated by the World Health Organisation (WHO) and UNAIDS in their AIDS epidemic update (December 1999) to be 33.6 and 16.3 million people, respectively. The spread of HIV is also now increasing fastest in areas of the world where over half of the human population reside, hence an effective vaccine is desperately needed to curb the spread of this epidemic. Despite the urgency, an effective vaccine for HIV is still some way off because of delays in defining the correlates of immune protection, lack of a suitable animal model, existence of up to 8 different subtypes of HIV and a high HIV mutation rate. A significant amount of research has been carried out to try and develop a vaccine capable of generating neutralising antibody responses that can protect against field isolates of HIV. Despite these efforts, it is now clear that the variability, instability and inaccessibility of critical determinants on the HIV envelope protein will make it extremely difficult and perhaps impossible to develop such a vaccine (Kwong et al, 1998). The limited ability of antibodies to block HIV infection is also supported by the observation that development of ALDS correlates primarily with a reduction in CTL responsiveness to HIV and not to altered antibody levels (Ogg et al, 1998). Hence CTL-mediated and not antibody-mediated responses appear to be critical for maintaining the asymptomatic state in vivo. There is also some evidence to suggest that pre-existing HlV-specific CTL responses can block the establishment of a latent HIV infection. This evidence comes from a number of cases where individuals have generated HlV-specific CTL responses without becoming infected and appear to be protected from establishing latent HIV infections despite repeated virus exposure (Rowland-Jones et al, 1995; Parmiani 1998). Taken together, these observations suggest that a vaccine capable of generating a broad range of strong CTL responses may be able to stop individuals from becoming latently infected with HIV or at least allow infected individuals to remain asymptomatic for life. Virtually all of the candidate HJV vaccines developed to date have been derived from subtype B HIV proteins (western world subtype) whereas the majority of the HIV infections worldwide are caused by subtypes A/E or C (E and A are similar except in the envelop protein)(referred to as developing world subtypes). Hence existing candidate vaccines may not be suitable for the more common HIV subtypes. Recently, there has been some evidence that B subtype vaccines may be partially effective against other common HIV subtypes (Rowland-Jones et al, 1998). Accordingly, the desirability of a vaccine still remains, whose effectiveness is substantially complete against all isolates of all strains of HΓV. SUMMARY OF THE INVENTION The present invention is predicated in part on a novel strategy for enhancing the efficacy of an immunopotentiating composition. This strategy involves utilising the sequence information of a parent polypeptide to produce a synthetic polypeptide that comprises a plurality of different segments of the parent polypeptide, which are linked sequentially together in a different arrangement relative to that of the parent polypeptide. As a result of this change in relationship, the sequence of the linked segments in the synthetic polypeptide is different to a sequence contained within the parent polypeptide. As more fully described hereinafter, the present strategy is used advantageously to cause significant disruption to the structure and/or function of the parent polypeptide while minimising the destruction of potentially useful epitopes encoded by the parent polypeptide. Thus, in one aspect of the present invention, there is provided a synthetic polypeptide comprising a plurality of different segments of at least one parent polypeptide, wherein the segments are linked together in a different relationship relative to their linkage in the at least one parent polypeptide. In one embodiment, the synthetic polypeptide consists essentially of different segments of a single parent polypeptide. In an alternate embodiment, the synthetic polypeptide consists essentially of different segments of a plurality of different parent polypeptides. Suitably, said segments in said synthetic polypeptide are linked sequentially in a different order or arrangement relative to that of corresponding segments in said at least one parent polypeptide. Preferably, at least one of said segments comprises partial sequence identity or homology to one or more other said segments. The sequence identity or homology is preferably contained at one or both ends of said at least one segment. In another aspect, the invention resides in a synthetic polynucleotide encoding the synthetic polypeptide as broadly described above. According to yet another aspect, the invention contemplates a synthetic construct comprising a said polynucleotide as broadly described above that is operably linked to a regulatory polynucleotide. In a further aspect of the invention, there is provided a method for producing a synthetic polynucleotide as broadly described above, comprising: - linking together in the same reading frame a plurality of nucleic acid sequences encoding different segments of at least one parent polypeptide to form a synthetic polynucleotide whose sequence encodes said segments linked together in a different relationship relative to their linkage in the at least one parent polypeptide. Preferably, the method further comprises fragmenting the sequence of a respective parent polypeptide into fragments and linking said fragments together in a different relationship relative to their linkage in said parent polypeptide sequence. In a preferred embodiment of this type, the fragments are randomly linked together. Suitably, the method further comprises reverse translating the sequence of a respective parent polypeptide or a segment thereof to provide a nucleic acid sequence encoding said parent polypeptide or said segment. In a preferred embodiment of this type, an amino acid of said parent polypeptide sequence is reverse translated to provide a codon, which has higher translational efficiency than other synonymous codons in a cell of interest. Suitably, an amino acid of said parent polypeptide sequence is reverse translated to provide a codon which, in the context of adjacent or local sequence elements, has a lower propensity of forming an undesirable sequence (e.g., a palindromic sequence or a duplicated sequence) that is refractory to the execution of a task (e.g., cloning or sequencing). In another aspect, the invention encompasses a computer program product for designing the sequence of a synthetic polypeptide as broadly described above, comprising: - code that receives as input the sequence of at least one parent polypeptide; - code that fragments the sequence of a respective parent polypeptide into fragments; - code that links together said fragments in a different relationship relative to their linkage in said parent polypeptide sequence; and - a computer readable medium that stores the codes. In yet another aspect, the invention provides a computer program product for designing the sequence of a synthetic polynucleotide as broadly described above, comprising: - code that receives as input the sequence of at least one parent polypeptide; - code that fragments the sequence of a respective parent polypeptide into fragments; - code that reverse translates the sequence of a respective fragment to provide a nucleic acid sequence encoding said fragment; - code that links together in the same reading frame each said nucleic acid sequence to provide a polynucleotide sequence that codes for a polypeptide sequence in which said fragments are linked together in a different relationship relative to their linkage in the at least one parent polypeptide sequence; and - a computer readable medium that stores the codes. In still yet another aspect, the invention provides a computer for designing the sequence of a synthetic polypeptide as broadly described above, wherein said computer comprises: (a) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein said machine-readable data comprise the sequence of at least one parent polypeptide; (b) a working memory for storing instructions for processing said machine-readable data; (c) a central-processing unit coupled to said working memory and to said machine- readable data storage medium, for processing said machine readable data to provide said synthetic polypeptide sequence; and (d) an output hardware coupled to said central processing unit, for receiving said synthetic polypeptide sequence. In a preferred embodiment, the processing of said machine readable data comprises fragmenting the sequence of a respective parent polypeptide into fragments and linking together said fragments in a different relationship relative to their linkage in the sequence of said parent polypeptide. In still yet another aspect, the invention resides in a computer for designing the sequence of a synthetic polynucleotide as broadly described above, wherein said computer comprises: (a) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein said machine-readable data comprise the sequence of at least one parent polypeptide; (b) a working memory for storing instructions for processing said machine-readable data; (c) a central-processing unit coupled to said working memory and to said machine- readable data storage medium, for processing said machine readable data to provide said synthetic polynucleotide sequence; and (d) an output hardware coupled to said central processing unit, for receiving said synthetic polynucleotide sequence. In a preferred embodiment, the processing of said machine readable data comprises fragmenting the sequence of a respective parent polypeptide into fragments, reverse translating the sequence of a respective fragment to provide a nucleic acid sequence encoding said fragment and linking together in the same reading frame each said nucleic acid sequence to provide a polynucleotide sequence that codes for a polypeptide sequence in which said fragments are linked together in a different relationship relative to their linkage in the at least one parent polypeptide sequence. According to another aspect, the invention contemplates a composition, comprising an immunopotentiating agent selected from the group consisting of a synthetic polypeptide as broadly described above, a synthetic polynucleotide as broadly described above and a synthetic construct as broadly described above, together with a pharmaceutically acceptable carrier. The composition may optionally comprise an adjuvant. In a further aspect, the invention encompasses a method for modulating an immune response, which response is preferably directed against a pathogen or a cancer, comprising administering to a patient in need of such treatment an effective amount of an immunopotentiating agent selected from the group consisting of a synthetic polypeptide as broadly described above, a synthetic polynucleotide as broadly described above and a synthetic construct as broadly described above, or a composition as broadly described above. According to still a further aspect of the invention, there is provided a method for treatment and/or prophylaxis of a disease or condition, comprising administering to a patient in need of such treatment an effective amount of an immunopotentiating agent selected from the group consisting of a synthetic polypeptide as broadly described above, a synthetic polynucleotide as broadly described above and a synthetic construct as broadly described above, or a composition as broadly described above. The invention also encompasses the use of the synthetic polypeptide, the synthetic polynucleotide and the synthetic construct as broadly described above in the study, and modulation of immune responses. BRIEF DESCRIPTION OF THE DRAWINGS Figure 1 is a diagrammatic representation showing the number of people living with AIDS in 199-8 in various parts of the world and most prevalent HIV clades in these regions. Estimates generated by UNAIDS. Figure 2 is a graphical representation showing trends in the incidence of the common HIV clades and estimates for the future. Graph from the International Aids Vaccine Initiative (IAVI). Figure 3 is a diagrammatic representation showing overlapping segments of a parent polypeptide sequence for HIV gag [SEQ JD NO: 1] used for the construction of an embodiment of an HIV Savine. Also shown are the alignments of common HIV clade consensus sequences for the HJV gag protein from the HIV Molecular Immunology Database 1997, Editors Bette Korber, John Moore, Cristian Brander, Richard Koup, Barton Haynes and Bruce Walker. Publisher, Los Alamos National Laboratory, Theoretical Biology and Biophysics, Los Alamos, New Mexico, Pub LAUR 98-485. Figure 4 is a diagrammatic representation showing overlapping segments of a parent polypeptide sequence for HIV pol [SEQ ID NO: 2] used for the construction of an embodiment of an HIV Savine. Also shown are the alignments of common HJV clade consensus sequences for the HIV pol protein from the HIV Molecular Immunology Database 1997, Editors Bette Korber, John Moore, Cristian Brander, Richard Koup, Barton Haynes and Bruce Walker. Publisher, Los Alamos National Laboratory, Theoretical Biology and Biophysics, Los Alamos, New Mexico, Pub LAUR98-485. Figure 5 is a diagrammatic representation showing overlapping segments of a parent polypeptide sequence for HIV vif [SEQ ID NO: 3] used for the construction of an embodiment of an HIV Savine. Also shown are the alignments of common HJV clade consensus sequences for the HIV vif protein from the HIV Molecular Immunology Database 1997, Editors Bette Korber, John Moore, Cristian Brander, Richard Koup, Barton Haynes and Bruce Walker. Publisher, Los Alamos National Laboratory, Theoretical Biology and Biophysics, Los Alamos, New Mexico, Pub LAUR98-485. Figure 6 is a diagrammatic representation showing overlapping segments of a parent polypeptide sequence for HJV vpr [SEQ ID NO: 4] used for the construction of an embodiment of an HJV Savine. Also shown are the alignments of common HJV clade consensus sequences for the HIV vpr protein from the HJV Molecular Immunology Database 1997, Editors Bette Korber, John Moore, Cristian Brander, Richard Koup, Barton Haynes and Bruce Walker. Publisher, Los Alamos National Laboratory, Theoretical Biology and Biophysics, Los Alamos, New Mexico, Pub LAUR 98-485. Figure 7 is a diagrammatic representation showing overlapping segments of a parent polypeptide sequence for HJV tat [SEQ ID NO: 5] used for the construction of an embodiment of an HIV Savine. Also shown are the alignments of common HJV clade consensus sequences for the HIV tat protein from the HIV Molecular Immunology Database 1997, Editors Bette Korber, John Moore, Cristian Brander, Richard Koup, Barton Haynes and Bruce Walker. Publisher, Los Alamos National Laboratory, Theoretical Biology and Biophysics, Los Alamos, New Mexico, Pub LAUR 98-485. Figure 8 is a diagrammatic representation showing overlapping segments of a parent polypeptide sequence for HIV rev [SEQ ID NO: 6] used for the construction of an embodiment of an HJV Savine. Also shown are the alignments of common HJV clade consensus sequences for the HJV rev protein from the HJV Molecular Immunology Database 1997, Editors Bette Korber, John Moore, Cristian Brander, Richard Koup, Barton Haynes and Bruce Walker. Publisher, Los Alamos National Laboratory, Theoretical Biology and Biophysics, Los Alamos, New Mexico, Pub LAUR 98-485. Figure 9 is a diagrammatic representation showing overlapping segments of a parent polypeptide sequence for HJV vpu [SEQ ID NO: 7] used for the construction of an embodiment of an HIV Savine. Also shown are the alignments of common HJV clade consensus sequences for the HJV vpu protein from the HJV Molecular Immunology Database 1997, Editors Bette Korber, John Moore, Cristian Brander, Richard Koup, Barton Haynes and Bruce Walker. Publisher, Los Alamos National Laboratory, Theoretical Biology and Biophysics, Los Alamos, New Mexico, Pub LAUR 98-485. Figure 10 is a diagrammatic representation showing overlapping segments of a parent polypeptide sequence for HJV env [SEQ ID NO: 8] used for the construction of an embodiment of an HJV Savine. Also shown are the alignments of common HJV clade consensus sequences for the HJV env protein from the HIV Molecular Immunology Database 1997, Editors Bette Korber, John Moore, Cristian Brander, Richard Koup, Barton Haynes and Bruce Walker. Publisher, Los Alamos National Laboratory, Theoretical Biology and Biophysics, Los Alamos, New Mexico, Pub LAUR 98-485. Figure 11 is a diagrammatic representation showing overlapping segments of a parent polypeptide sequence for HIV nef [SEQ ID NO: 9] used for the construction of an embodiment of an HIV Savine. Also shown are the alignments of common HJV clade consensus sequences for the HIV nef protein from the HIV Molecular Immunology Database 1997, Editors Bette Korber, John Moore, Cristian Brander, Richard Koup, Barton Haynes and Bruce Walker. Publisher, Los Alamos National Laboratory, Theoretical Biology and Biophysics, Los Alamos, New Mexico, Pub LAUR 98-485. Figure 12 is a diagrammatic representation depicting the systematic segmentation of the designed degenerate consensus sequences for each HJV protein and the reverse translation of each segment into a DNA sequence. Also shown is the number of segments used during random rearrangement and amino acids that were removed. Amino acids surrounded by an open square were removed from the design, because degenerate codons to cater for the desired amino acid combination required too many degenerate bases to comply with the incorporation of degenerate sequence rules outlined in the description of the invention herein. Amino acids surrounded by an open circle were removed only in the segment concerned mainly because they were coded for in an oligonucleotide overlap region. Amino acids marked with an asterisk were designed differently in one fragment compared to the corresponding overlap region (see tat gene) Figure 13 is a diagrammatic representation showing the first and second most frequently used codons in mammals used to reverse translate HIV protein segments. Also shown are all first and second most frequently used degenerate codons for two amino acids where only one base is varied. Codons used where more than one base was varied were worked out in each case by comparing all the codons for each amino acid. The IUPAC codes for degenerate bases are also shown. Figure 14 illustrates the construction plan for the HJV Savine showing the approximate sizes of the subcassettes, cassettes and full-length Savine cDNA and the restriction sites involved in joining them together. Also shown are the extra sequences added onto each subcassette during their design and a brief description of how the subcassettes, cassettes and full length cDNA were constructed and transferred into appropriate DNA plasmids. Description of full length construction: pA was cleaved with XlioVSaR and cloned into Xhol arms of the B cassette; pAB was cleaved with Xhol and cloned into Xhol arms of the C cassette; full length construct is excisable with either Xbal/BamΗI at the 5' end or Bglϊl at the 3' end. Options for excising cassettes: A) XbaVBamBI at the 5' end, BglWXhol at the 3' end; B) XbaVBamHl at the 5' end, BgUHSaH at the 3' end; C) Xbaϊ/BamΗI at the 5' end, Bgltt/Sal at the 3' end. Cleaving plasmid vectors: pDNAVacc is cleavable with Xbaϊ/Xhol (DNA vaccination); pBCB07 or pTK7.5 vectors are cleavable with BamΑVSaK (Recombinant Vaccinia); pAvipox vector pAF09 is cleavable with BamΗUSaK (Recombinant Avipox). Figure 15 shows the full length DNA (17253 bp) and protein sequence (5742 aas) of the HTV Savine construct. Fragment boundaries are shown, together with the position of each fragment in each designed HJV protein, fragment number (in brackets), spacer residues (two alanine residues) and which fragment the spacer was for (open boxes and arrows). The location of residual restriction site joining sequences corresponding to subcassette or cassette boundaries (shaded boxes) are also shown, along with start and stop codons, Kozak sequence, the location of the murine influenza virus CTL epitope sequence (near the 3' end), important restriction sites at each end and the position of each degenerate amino acid (indicated by 'X'). Figure 16 depicts the layout and position of oligonucleotides in the designed DNA sequence for subcassette Al. The sequences which anneal to the short amplification oligonucleotides are indicated by hatched boxes and the position of oligonucleotide overlap regions are dark shaded. Figure 17: Panel (a) depicts the stepwise asymmetric PCR of the two halves of subcassette Al (lanes 2-5 and 7-9, respectively) and final splicing together by SOEing (lane 10). DNA standards in lane 1 are pUC18 digested with Sau3Aϊ. Panel (b) shows the stepwise ligation-mediated joining and PCR amplification of each cassette as indicated. DNA standards in lane 1 are SPP1 cut with EcoRI. Figure 18: Panel (a) shows summary of the construction of the DNA vaccine plasmids that express one HIV Savine cassette. Panel (b) shows a summary of the construction of the plasmids used for marker rescue recombination to generate Vaccinia viruses expressing one HJV Savine cassette. Panel (c) shows a summary of the construction of the DNA vaccine plasmids which each express a version of the full-length HIV Savine cDNA Figure 19 shows restimulation of HIV specific polyclonal CTL responses from three HrV-infected patients by the HIV Savine constructs. PBMCs from three different patients were restimulated for 7 days by infection with Vaccinia virus pools expressing the HTV Savine cassettes: Pool 1 included W-AC1 and VV-BCl; Pool 2 included VV-AC2, VV-BC2 andW-CC2. The restimulated PBMCs were then mixed with autologous LCLs (effector to target ratio of 50:1), which were either uninfected or infected with either Vaccinia viruses expressing the HJV proteins gag (VV-gag), env (VV-env) or pol (W- pol), VV- HIV Savine pools 1 (light bars) or 2 (dark bars) or a control Vaccinia virus (VV- Lac) and the amount of 51 Cr released used to determine percent specific lysis. K562 cells were used to determine the level of NK cell-mediated killing in their stimulated culture. Figure 20 is a diagrammatic representation showing CD4+ proliferation of PBMCs from HJV-1 infected patients restimulated with either Pooll or Pool2 of the HTV-1 Savine. Briefly PBMCs were stained with CFSE and culture for 6 days with or without Ws encoding either pooll or pool2 of the HJV-l Savine. Restimulated Cells were then labelled with antibodies and analysed by FACS. Figure 21 is a graphical representation showing the CTL response in mice vaccinated with the HJV Savine. C57BL6 mice were immunised with the HTV-1 Savine DNA vaccine comprising the six plasmids described in Figure 18a (100 μg total DNA was given as 50 μg/leg i.m.). One week later Poxviruses (lxl0 7 pfu) comprising Pool 1 of the HJV-l Savine were used to boost the immune responses. Three weeks later splenocytes from these mice were restimulated with W-Pool 1 or VV-Pool 2 for 5 days and the resultant effectors used in a 51 Cr release cytotoxicity assay against targets infected with CTRW, W-pools or VV expressing the natural antigens from HJV-l. Figure 22 shows immune responses of HIV Immune Macaques (vaccinated with recombinant FPV expressing gag-pol and challenged with HJV-l 2 years prior to experiment). Monkeys 1 and 2 were immunised once at day 0 with W Savine pool 1 (Three VVs which together express the entire HJV Savine ). Monkey 3 was immunised twice with FPV-gag-pol i.e., Day 0 is 3 weeks after first FPV-gag-pol immunisation. A) JFN-y detection by ELISPOT of whole blood (0.5 mL, venous blood heparin- anticoagulated) stimulated with Aldrithiol-2 inactivated whole HJV-l (20 hours, 20 / g/mL). Plasma samples were then centrifuged (lOOOxg) and assayed in duplicate for antigen-specific JFN using capture ELISA. B) Flow cytometric detection of HJV-l specific CD69+/CD8+ T cells. Freshly isolated PBMCs were stimulated with inactivated fflV-1 as above for 16 hours, washed and labelled with the antibodies. Cells were then analysed using a FACScalibur™ flow cytometer and data, analysed using Cell-Quest software. C) Flow cytometric detection of HIV-1 specific CD69+/CD4+ T cells carried out as in B). Figure 23 shows a diagram of a system used to carry out the instructions encoded by the storage medium of Figures 28 and 29. Figure 24 depicts a flow diagram showing an embodiment of a method for designing synthetic polynucleotide and synthetic polypeptides of the invention. Figure 25 shows an algorithm, which inter alia utilises the steps of the method shown in Figure 24. Figure 26 shows an example of applying the algorithm of Figure 25 to an input consensus polyprotein sequence of Hepatitis C la to execute the segmentation of the polyprotein sequence, the rearrangement of the segments, the linkage of the rearranged segments and the outputting of synthetic polynucleotide and polypeptide sequences for the preparation of Savines for treating and/or preventing Hepatitis C infection. Figure 27 illustrates an example of applying the algorithm of Figure 25 to input consensus melanocyte differentiation antigens (gplOO, MART, TRP-1, Tyros, Trp-2, MC1R, MUCIF and MUC1R) and to consensus melanoma specific antigens (BAGE, GAGE-1, gpl00In4, MAGE-1, MAGE-3, PRAME, TRP2JN2, NYNSOla, NYNSOlb and LAGEl) to facilitate segmentation of those sequences, to rearrange the segments, to link the rearranged segments and to synthetic polynucleotide and polypeptide sequences for the preparation of Savines for treating and/or preventing melanoma. Figure 28 shows a cross section of a magnetic storage medium. Figure 29 shows a cross section of an optically readable data storage medium. Figure 30 shows six HIV Savine cassette sequences (Al [SEQ ID NO: 393], A2 [SEQ ID NO: 399], B1[SEQ ID NO: 395], B2 [SEQ ID NO: 401], Cl [SEQ ID NO: 397] and C2 [SEQ JD NO: 403]). Al, BI and Cl can be joined together using, for example, convenient restriction enzyme sites provided at the ends of each cassette to construct an embodiment of a full length HJV Savine [SEQ JD NO: 405]. A2, B2 and C2 can also be joined together to provide another embodiment of a full length HJV Savine with 350 aa mutations common in major HJV clades. The cassettes A B/C can be joined into single constructs using specific restriction enzyme sites incorporated after the start codon or before the stop codon in the cassettes BRIEF DESCRIPTION OF THE SEQUENCES: SUMMARY TABLE TABLE A SEQUENCEID SEQUENCE LENGTH NUMBER SEQ JD NO: 95 Polypeptide encoded by SEQ JD NO: 94 30 aa SEQ JD NO: 96 POL segment 11 90nts SEQ ID NO: 97 Polypeptide encoded by SEQ JD NO: 96 30 aa SEQ JD NO: 98 POL segment 12 90nts SEQ JD NO: 99 Polypeptide encoded by SEQ JD NO: 98 30 aa SEQ ID NO: 100 POL segment 13 90nts SEQJDNO: 101 Polypeptide encoded by SEQ JD NO: 100 30 aa SEQJDNO: 102 POL segment 14 90nts SEQJDNO: 103 Polypeptide encoded by SEQ ID NO: 102 30 aa SEQ JD NO: 104 POL segment 15 90nts SEQ JD NO: 105 Polypeptide encoded by SEQ JD NO: 104 30 aa SEQJDNO: 106 POL segment 16 90nts SEQJDNO: 107 Polypeptide encoded by SEQ JD NO: 106 30 aa SEQJDNO: 108 POL segment 17 90nts SEQJDNO: 109 Polypeptide encoded by SEQ ID NO: 108 30 aa SEQ ID NO: 110 POL segment 18 90nts SEQJDNO: 111 Polypeptide encoded by SEQ JD NO: 110 30 aa SEQJDNO: 112 POL segment 19 90nts SEQJDNO: 113 Polypeptide encoded by SEQ ID NO: 112 30 aa SEQJDNO: 114 POL segment 20 90nts SEQ ID NO: 115 Polypeptide encoded by SEQ JD NO: 114 30 aa SEQJDNO: 116 POL segment 21 90nts SEQJDNO: 117 Polypeptide encoded by SEQ JD NO: 116 30 aa SEQJDNO: 118 POL segment 22 90nts SEQUENCE ID SEQUENCE LENGTH NUMBER SEQ H NO: 311 Polypeptide encoded by SEQ HD NO: 310 30 aa SEQ H NO: 312 GAP A segment 7 75 nts SEQ DD NO: 313 Polypeptide encoded by SEQ ID NO: 312 25 nts SEQ HD NO: 314 GAP B segment 1 90 nts SEQ DD NO: 315 Polypeptide encoded by SEQ JD NO: 314 30 aa SEQ JD NO: 316 GAP B segment 2 90 nts SEQ DD NO: 317 Polypeptide encoded by SEQ HD NO: 316 30 aa SEQ DD NO: 318 GAP B segment 3 90 nts SEQ DD NO: 319 Polypeptide encoded by SEQ HD NO: 318 30 aa SEQ DD NO: 320 GAP B segment 4 90 nts SEQ DD NO: 321 Polypeptide encoded by SEQ ID NO: 320 30 aa SEQ DD NO: 322 GAP B segment 5 90 nts SEQ DD NO: 323 Polypeptide encoded by SEQ ID NO: 322 30 aa SEQ JD NO: 324 GAP B segment 6 90 nts SEQ JD NO: 325 Polypeptide encoded by SEQ JD NO: 324 30 aa SEQ ID NO: 326 GAP B segment 7 90 nts SEQ DD NO: 327 Polypeptide encoded by SEQ DD NO: 326 30 aa SEQ JD NO: 328 GAP B segment 8 90 nts SEQ ID NO: 329 Polypeptide encoded by SEQ DD NO: 328 30 aa SEQ JD NO: 330 GAP B segment 9 90 nts SEQ DD NO: 331 Polypeptide encoded by SEQ DD NO: 330 30 aa SEQ DD NO: 332 GAP B segment 10 90 nts SEQ DD NO: 333 Polypeptide encoded by SEQ DD NO: 332 30 aa SEQ DD NO: 334 GAP B segment 11 90 nts SEQUENCEID SEQUENCE LENGTH , NUMBER SEQ ED NO: 335 Polypeptide encoded by SEQ DD NO: 334 30 aa SEQ DD NO: 336 GAP B segment 12 90 nts SEQ JD NO: 337 Polypeptide encoded by SEQ DD NO: 336 30 aa SEQ JD NO: 338 GAP B segment 13 90 nts SEQ JD NO: 339 Polypeptide encoded by SEQ DD NO: 338 30 aa SEQ JD NO: 340 GAP B segment 14 90 nts SEQ JD NO: 341 Polypeptide encoded by SEQ DD NO: 340 30 aa SEQ JD NO: 342 GAP B segment 15 90 nts SEQ JD NO: 343 Polypeptide encoded by SEQ DD NO: 342 30 aa SEQ JD NO: 344 GAP B segment 16 90 nts SEQ JD NO: 345 Polypeptide encoded by SEQ ID NO: 344 30 aa SEQ JD NO: 346 GAP B segment 17 90 nts SEQ DD NO: 347 Polypeptide encoded by SEQ JD NO: 346 30 aa SEQ DD NO: 348 GAP B segment 18 90 nts SEQ DD NO: 349 Polypeptide encoded by SEQ JD NO: 348 30 aa SEQ DD NO: 350 GAP B segment 19 90 nts SEQ DD NO: 351 Polypeptide encoded by SEQ JD NO: 350 30 aa SEQ DD NO: 352 GAP B segment 20 90 nts SEQ DD NO: 353 Polypeptide encoded by SEQ JD NO: 352 30 aa SEQ DD NO: 354 GAP B segment 21 90 nts SEQ DD NO: 355 Polypeptide encoded by SEQ HD NO: 354 30 aa SEQ DD NO: 356 GAP B segment 22 90 nts SEQ DD NO: 357 Polypeptide encoded by SEQ DD NO: 356 30 aa SEQ DD NO: 358 GAP B segment 23 90 nts SEQUENCE ID SEQUENCE LENGTH NUMBER SEQ DD NO: 383 Polypeptide encoded by SEQ DD NO: 382 30 aa SEQ JD NO: 384 NEF segment 10 90 nts SEQ J O: 385 Polypeptide encoded by SEQ DD NO: 384 30 aa SEQ JD NO: 386 NEF segment 11 90 nts SEQ JD NO: 387 Polypeptide encoded by SEQ JD NO: 386 30 aa SEQ JD NO: 388 NEF segment 12 90 nts SEQ JD NO: 389 Polypeptide encoded by SEQ ID NO: 388 30 aa SEQ JD NO: 390 NEF segment 13 78 nts SEQ JD NO: 391 Polypeptide encoded by SEQ DD NO: 390 26 aa SEQ JD NO: 392 HIV Cassette Al 5703 nts SEQ JD NO: 393 Polypeptide encoded by SEQ ID NO:392 1896 aa SEQ DD NO: 394 HJV Cassette BI 5685 nts SEQ DD NO: 395 Polypeptide encoded by SEQ ED NO: 394 1890 aa SEQ DD NO: 396 HJV Cassette Cl 5925 nts SEQ DD NO: 397 Polypeptide encoded by SEQ JD NO: 396 1967 aa SEQ DD NO: 398 HJV Cassette A2 5703 nts SEQ HD NO: 399 Polypeptide encoded by SEQ ED NO: 398 1896 aa SEQ ID NO: 400 HJV Cassette B2 5685 nts SEQ DD NO: 401 Polypeptide encoded by SEQ JD NO: 400 1890 aa SEQ DD NO: 402 HJV Cassette C2 5925 nts SEQ ED NO: 403 Polypeptide encoded by SEQ JD NO: 402 1967 aa SEQ HD NO: 404 HJV complete Savine 17244 nts SEQ HD NO: 405 Polypeptide encoded by SEQ JD NO: 404 5747 aa SEQ H NO: 406 HepCla consensus polyprotein sequence 3011 aa SEQUENCE E ) SEQUENCE LENGTH NUMBER SEQ DD NO: 407 HepCla segment 1 90 nts SEQ DD NO: 408 Polypeptide encoded by SEQ DD NO: 407 30 aa SEQ DD NO: 409 HepCla segment 2 90 nts SEQ ED NO: 410 Polypeptide encoded by SEQ DD NO: 409 30 aa SEQ DD NO: 411 HepCla segment 3 90 nts SEQ DD NO: 412 Polypeptide encoded by SEQ DD NO: 411 30 aa SEQ DD NO: 413 HepCla segment 4 90 nts SEQ HD NO: 414 Polypeptide encoded by SEQ DD NO: 413 30 aa SEQ HD NO: 415 HepCla segment 5 90 nts SEQ HD NO: 416 Polypeptide encoded by SEQ HD NO: 415 30 aa SEQ DD NO: 417 HepCla segment 6 90 nts SEQ DD NO: 418 Polypeptide encoded by SEQ DD NO: 417 30 aa SEQ HD NO: 419 HepCla segment 7 90 nts SEQ HD NO: 420 Polypeptide encoded by SEQ JD NO: 419 30 aa SEQ HD NO: 421 HepCla segment 8 90 nts SEQ HD NO: 422 Polypeptide encoded by SEQ DD NO: 421 30 aa SEQ ID NO: 423 HepCla segment 9 90 nts SEQ ID NO: 424 Polypeptide encoded by SEQ DD NO: 423 30 aa SEQ HD NO: 425 HepCla segment 10 90 nts SEQ JD NO: 426 Polypeptide encoded by SEQ DD NO: 425 30 aa SEQ JD NO: 427 HepCla segment 11 90 nts SEQ JD NO: 428 Polypeptide encoded by SEQ ID NO: 427 30 aa SEQ JD NO: 429 HepCla segment 12 90 nts SEQ HD NO: 430 Polypeptide encoded by SEQ DD NO: 429 30 aa SEQUENCE ID SEQUENCE LENGTH NUMBER SEQ DD NO: 431 HepCla segment 13 90 nts SEQ DD NO: 432 Polypeptide encoded by SEQ JD NO: 431 30 aa SEQ DD NO: 433 HepCla segment 14 90 nts SEQ DD NO: 434 Polypeptide encoded by SEQ DD NO: 433 30 aa SEQ HD NO: 435 HepCla segment 15 90 nts SEQ DD NO: 436 Polypeptide encoded by SEQ DD NO: 435 30 aa SEQ ED NO: 437 HepCla segment 16 90 nts SEQ DD NO: 438 Polypeptide encoded by SEQ DD NO: 437 30 aa SEQ HD NO: 439 HepCla segment 17 90 nts SEQ ED NO: 440 Polypeptide encoded by SEQ DD NO: 439 30 aa SEQ DD NO: 441 HepCla segment 18 90 nts SEQ DD NO: 442 Polypeptide encoded by SEQ ID NO: 441 30 aa SEQ HD NO: 443 HepCla segment 19 90 nts SEQ DD NO: 444 Polypeptide encoded by SEQ HD NO: 443 30 aa SEQ HD NO: 445 HepCla segment 20 90 nts SEQ DD NO: 446 Polypeptide encoded by SEQ DD NO: 445 30 aa SEQ DD NO: 447 HepCla segment 21 90 nts SEQ ED NO: 448 Polypeptide encoded by SEQ ID NO: 447 30 aa SEQ HD NO: 449 HepCla segment 22 90 nts SEQ DD NO: 450 Polypeptide encoded by SEQ JD NO: 449 30 aa SEQ DD NO: 451 HepCla segment 23 90 nts SEQ DD NO: 452 Polypeptide encoded by SEQ DD NO: 451 30 aa SEQ DD NO: 453 HepCla segment 24 90 nts SEQ JD NO: 454 Polypeptide encoded by SEQ DD NO: 453 30 aa SEQUENCE E> SEQUENCE LENGTH NUMBER SEQ ID NO: 455 HepCla segment 25 90 nts SEQ DD NO: 456 Polypeptide encoded by SEQ DD NO: 455 30 aa SEQ HD NO: 457 HepCla segment 26 90 nts SEQ DD NO: 458 Polypeptide encoded by SEQ DD NO: 457 30 aa SEQ DD NO: 459 HepCla segment 27 90 nts SEQ DD NO: 460 Polypeptide encoded by SEQ DD NO: 459 30 aa SEQ DD NO: 461 HepCla segment 28 90 nts SEQ DD NO: 462 Polypeptide encoded by SEQ HD NO: 461 30 aa SEQ DD NO: 463 HepCla segment 29 90 nts SEQ HD NO: 464 Polypeptide encoded by SEQ JD NO: 463 30 aa SEQ HD NO: 465 HepCla segment 30 90 nts SEQ HD NO: 466 Polypeptide encoded by SEQ DD NO: 465 30 aa SEQ HD NO: 467 HepCla segment 31 90 nts SEQ HD NO: 468 Polypeptide encoded by SEQ DD NO: 467 30 aa SEQ HD NO: 469 HepCla segment 32 90 nts SEQ DD NO: 470 Polypeptide encoded by SEQ DD NO: 469 30 aa SEQ DD NO: 471 HepCla segment 33 90 nts SEQ HD NO: 472 Polypeptide encoded by SEQ DD NO: 471 30 aa SEQ HD NO: 473 HepCla segment 34 90 nts SEQ HD NO: 474 Polypeptide encoded by SEQ DD NO: 473 30 aa SEQ HD NO: 475 HepCla segment 35 90 nts SEQ DD NO: 476 Polypeptide encoded by SEQ DD NO: 475 30 aa SEQ HD NO: 477 HepCla segment 36 90 nts SEQ DD NO: 478 Polypeptide encoded by SEQ DD NO: 477 30 aa SEQUENCE ID SEQUENCE LENGTH NUMBER SEQ ID NO: 479 HepCla segment 37 90 nts SEQ DD NO: 480 Polypeptide encoded by SEQ DD NO: 479 30 aa SEQ H NO: 481 HepCla segment 38 90 nts SEQ DD NO: 482 Polypeptide encoded by SEQ DD NO: 481 30 aa SEQ HD NO: 483 HepCla segment 39 90 nts SEQ DD NO: 484 Polypeptide encoded by SEQ DD NO: 483 30 aa SEQ DD NO: 485 HepCla segment 40 90 nts SEQ DD NO: 486 Polypeptide encoded by SEQ DD NO: 485 30 aa SEQ DD NO: 487 HepCla segment 41 90 nts SEQ DD NO: 488 Polypeptide encoded by SEQ DD NO: 487 30 aa SEQ DD NO: 489 HepCla segment 42 90 nts SEQ DD NO: 490 Polypeptide encoded by SEQ DD NO: 489 30 aa SEQ DD NO: 491 HepCla segment 43 90 nts SEQ DD NO: 492 Polypeptide encoded by SEQ DD NO: 491 30 aa SEQ DD NO: 493 HepCla segment 44 90 nts SEQ DD NO: 494 Polypeptide encoded by SEQ DD NO: 493 30 aa SEQ DD NO: 495 HepCla segment 45 90 nts SEQ DD NO: 496 Polypeptide encoded by SEQ DD NO: 495 30 aa SEQ DD NO: 497 HepCla segment 46 90 nts SEQ HD NO: 498 Polypeptide encoded by SEQ DD NO: 497 30 aa SEQ HD NO: 499 HepCla segment 47 90 nts SEQ DD NO: 500 Polypeptide encoded by SEQ DD NO: 499 30 aa SEQ DD NO: 501 HepCla segment 48 90 nts SEQ DD NO: 502 Polypeptide encoded by SEQ DD NO: 501 30 aa SEQUENCE ID SEQUENCE LENGTH NUMBER SEQ HD NO: 503 HepCla segment 49 90 nts SEQ DD NO: 504 Polypeptide encoded by SEQ JD NO: 503 30 aa SEQ DD NO: 505 HepCla segment 50 90 nts SEQ HD NO: 506 Polypeptide encoded by SEQ DD NO: 505 30 aa SEQ DD NO: 507 HepCla segment 51 90 nts SEQ ED NO: 508 Polypeptide encoded by SEQ JD NO: 507 30 aa SEQ HD NO: 509 HepCla segment 52 90 nts SEQ HD NO: 510 Polypeptide encoded by SEQ HD NO: 509 30 aa SEQ ID NO: 511 HepCla segment 53 90 nts SEQ DD NO: 512 Polypeptide encoded by SEQ HD NO: 511 30 aa SEQ ID NO: 513 HepCla segment 54 90 nts SEQ DD NO: 514 Polypeptide encoded by SEQ HD NO: 513 30 aa SEQ DD NO: 515 HepCla segment 55 90 nts SEQ DD NO: 516 Polypeptide encoded by SEQ JD NO: 515 30 aa SEQ DD NO: 517 HepCla segment 56 90 nts SEQ DD NO: 518 Polypeptide encoded by SEQ JD NO: 517 30 aa SEQ DD NO: 519 HepCla segment 57 90 nts SEQ DD NO: 520 Polypeptide encoded by SEQ HD NO: 519 30 aa SEQ DD NO: 521 HepCla segment 58 90 nts SEQ DD NO: 522 Polypeptide encoded by SEQ HD NO: 521 30 aa SEQ DD NO: 523 HepCla segment 59 90 nts SEQ DD NO: 524 Polypeptide encoded by SEQ JD NO: 523 30 aa SEQ DD NO: 525 HepCla segment 60 90 nts SEQ DD NO: 526 Polypeptide encoded by SEQ ED NO: 525 30 aa SEQUENCE ID SEQUENCE LENGTH NUMBER SEQ HD NO: 527 HepCla segment 61 90 nts SEQ HD NO: 528 Polypeptide encoded by SEQ DD NO: 527 30 aa SEQ HD NO: 529 HepCla segment 62 90 nts SEQ HD NO: 530 Polypeptide encoded by SEQ DD NO: 529 30 aa SEQ DD NO: 531 HepCla segment 63 90 nts SEQ DD NO: 532 Polypeptide encoded by SEQ DD NO: 531 30 aa SEQ DD NO: 533 HepCla segment 64 90 nts SEQ DD NO: 534 Polypeptide encoded by SEQ DD NO: 533 30 aa SEQ DD NO: 535 HepCla segment 65 90 nts SEQ DD NO: 536 Polypeptide encoded by SEQ DD NO: 535 30 aa SEQ DD NO: 537 HepCla segment 66 90 nts SEQ DD NO: 538 Polypeptide encoded by SEQ DD NO: 537 30 aa SEQ DD NO: 539 HepCla segment 67 90 nts SEQ DD NO: 540 Polypeptide encoded by SEQ JD NO: 539 30 aa SEQ DD NO: 541 HepCla segment 68 90 nts SEQ DD NO: 542 Polypeptide encoded by SEQ ED NO: 541 30 aa SEQ HD NO: 543 HepCla segment 69 90 nts SEQ DD NO: 544 Polypeptide encoded by SEQ HD NO: 543 30 aa SEQ DD NO: 545 HepCla segment 70 90 nts SEQ ID NO: 546 Polypeptide encoded by SEQ DD NO: 545 30 aa SEQ JD NO: 547 HepCla segment 71 90 nts SEQ ID NO: 548 Polypeptide encoded by SEQ ED NO: 547 30 aa SEQ JD NO: 549 HepCla segment 72 90 nts SEQ ED NO: 550 Polypeptide encoded by SEQ ED NO: 549 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ ED NO: 551 HepCla segment 73 90 nts SEQ ED NO: 552 Polypeptide encoded by SEQ DD NO: 551 30 aa SEQ DD NO: 553 HepCla segment 74 90 nts SEQ DD NO: 554 Polypeptide encoded by SEQ ED NO: 553 30 aa SEQ DD NO: 555 HepCla segment 75 90 nts SEQ DD NO: 556 Polypeptide encoded by SEQ JD NO: 555 30 aa SEQ ED NO: 557 HepCla segment 76 90 nts SEQ DD NO: 558 Polypeptide encoded by SEQ JD NO: 557 30 aa SEQ DD NO: 559 HepCla segment 77 90 nts SEQ DD NO: 560 Polypeptide encoded by SEQ ED NO: 559 30 aa SEQ DD NO: 561 HepCla segment 78 90 nts SEQ DD NO: 562 Polypeptide encoded by SEQ DD NO: 561 30 aa SEQ DD NO: 563 HepCla segment 79 90 nts SEQ DD NO: 564 Polypeptide encoded by SEQ JD NO: 563 30 aa SEQ DD NO: 565 HepCla segment 80 90 nts SEQ DD NO: 566 Polypeptide encoded by SEQ ED NO: 565 30 aa SEQ J NO: 567 HepCla segment 81 90 nts SEQ JD NO: 568 Polypeptide encoded by SEQ JD NO: 567 30 aa SEQ JD NO: 569 HepCla segment 82 90 nts SEQ DD NO: 570 Polypeptide encoded by SEQ DD NO: 569 30 aa SEQ DD NO: 571 HepCla segment 83 90 nts SEQ ED NO: 572 Polypeptide encoded by SEQ ED NO: 571 30 aa SEQ ED NO: 573 HepCla segment 84 90 nts SEQ DD NO: 574 Polypeptide encoded by SEQ JD NO: 573 30 aa SEQUENCE ID SEQUENCE LENGTH NUMBER SEQ HD NO: 575 HepCla segment 85 90 nts SEQ DD NO: 576 Polypeptide encoded by SEQ JD NO: 575 30 aa SEQ ED NO: 577 HepCla segment 86 90 nts SEQ DD NO: 578 Polypeptide encoded by SEQ DD NO: 577 30 aa SEQ ED NO: 579 HepCla segment 87 90 nts SEQ DD NO: 580 Polypeptide encoded by SEQ DD NO: 579 30 aa SEQ DD NO: 581 HepCla segment 88 90 nts SEQ DD NO: 582 Polypeptide encoded by SEQ ED NO: 581 30 aa SEQ JD O: 583 HepCla segment 89 90 nts SEQ JD NO: 584 Polypeptide encoded by SEQ ED NO: 583 30 aa SEQ ED NO: 585 HepCla segment 90 90 nts SEQ ED NO: 586 Polypeptide encoded by SEQ ED NO: 585 30 aa SEQ DD NO: 587 HepCla segment 91 90 nts SEQ DD NO: 588 Polypeptide encoded by SEQ ED NO: 587 30 aa SEQ ED NO: 589 HepCla segment 92 90 nts SEQ DD NO: 590 Polypeptide encoded by SEQ DD NO: 589 30 aa SEQ DD NO: 591 HepCla segment 93 90 nts SEQ DD NO: 592 Polypeptide encoded by SEQ ED NO: 591 30 aa SEQ ED NO: 593 HepCla segment 94 90 nts SEQ ED NO: 594 Polypeptide encoded by SEQ ED NO: 593 30 aa SEQ ED NO: 595 HepCla segment 95 90 nts SEQ DD NO: 596 Polypeptide encoded by SEQ DD NO: 595 30 aa SEQ HD NO: 597 HepCla segment 96 90 nts SEQ ED NO: 598 Polypeptide encoded by SEQ ED NO: 597 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ DD NO: 599 HepCla segment 97 90 nts SEQ DD NO: 600 Polypeptide encoded by SEQ DD NO: 599 30 aa SEQ DD NO: 601 HepCla segment 98 90 nts SEQ ED NO: 602 Polypeptide encoded by SEQ ED NO: 601 30 aa SEQ DD NO: 603 HepCla segment 99 90 nts SEQ DD NO: 604 Polypeptide encoded by SEQ DD NO: 603 30 aa SEQ DD NO: 605 HepCla segment 100 90 nts SEQ DD NO: 606 Polypeptide encoded by SEQ ED NO: 605 30 aa SEQ DD NO: 607 HepCla segment 101 90 nts SEQ DD NO: 608 Polypeptide encoded by SEQ ED NO: 607 30 aa SEQ DD NO: 609 HepCla segment 102 90 nts SEQ DD NO: 610 Polypeptide encoded by SEQ ED NO: 609 30 aa SEQ ED NO: 611 HepCla segment 103 90 nts SEQ ED NO: 612 Polypeptide encoded by SEQ ED NO: 611 30 aa SEQ DD NO: 613 HepCla segment 104 90 nts SEQ DD NO: 614 Polypeptide encoded by SEQ ED NO: 613 30 aa SEQ ED NO: 615 HepCla segment 105 90 nts SEQ DD NO: 616 Polypeptide encoded by SEQ JD NO: 615 30 aa SEQ ED NO: 617 HepCla segment 106 90 nts SEQ DD NO: 618 Polypeptide encoded by SEQ ED NO: 617 30 aa SEQ DD NO: 619 HepCla segment 107 90 nts SEQ DD NO: 620 Polypeptide encoded by SEQ ED NO: 619 30 aa SEQ DD NO: 621 HepCla segment 108 90 nts SEQ DD NO: 622 Polypeptide encoded by SEQ DD NO: 621 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ ED NO: 623 HepCla segment 109 90 nts SEQ ED NO: 624 Polypeptide encoded by SEQ ED NO: 623 30 aa SEQ ED NO: 625 HepCla segment 110 90 nts SEQ DD NO: 626 Polypeptide encoded by SEQ DD NO: 625 30 aa SEQ ED NO: 627 HepCla segment 111 90 nts SEQ ED NO: 628 Polypeptide encoded by SEQ DD NO: 627 30 aa SEQ ED NO: 629 HepCla segment 112 90 nts SEQ ID NO: 630 Polypeptide encoded by SEQ ED NO: 629 30 aa SEQ ED NO: 631 HepC 1 a segment 113 90 nts SEQ ED NO: 632 Polypeptide encoded by SEQ ED NO: 631 30 aa SEQ HD NO: 633 HepCla segment 114 90 nts SEQ ED NO: 634 Polypeptide encoded by SEQ ED NO: 633 30 aa SEQ ED NO: 635 HepCla segment 115 90 nts SEQ ED NO: 636 Polypeptide encoded by SEQ ED NO: 635 30 aa SEQ ED NO: 637 HepC 1 a segment 116 90 nts SEQ DD NO: 638 Polypeptide encoded by SEQ DD NO: 637 30 aa SEQ ED NO: 639 HepCla segment 117 90 nts SEQ ED NO: 640 Polypeptide encoded by SEQ ED NO: 639 30 aa SEQ ED NO: 641 HepC 1 a segment 118 90 nts SEQ ED NO: 642 Polypeptide encoded by SEQ ED NO: 641 30 aa SEQ DD NO: 643 HepC 1 a segment 119 90 nts SEQ ED NO: 644 Polypeptide encoded by SEQ ED NO: 643 30 aa SEQ DD NO: 645 HepCla segment 120 90 nts I SEQ DD NO: 646 Polypeptide encoded by SEQ ED NO: 645 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ ED NO: 647 HepCla segment 121 90 nts SEQ HD NO: 648 Polypeptide encoded by SEQ DD NO: 647 30 aa SEQ ED NO: 649 HepCla segment 122 90 nts SEQ ED NO: 650 Polypeptide encoded by SEQ ED NO: 649 30 aa SEQ HD NO: 651 HepCla segment 123 90 nts SEQ ED NO: 652 Polypeptide encoded by SEQ ED NO: 651 30 aa SEQ ED NO: 653 HepCla segment 124 90 nts SEQ DD NO: 654 Polypeptide encoded by SEQ ED NO: 653 30 aa SEQ DD NO: 655 HepCla segment 125 90 nts SEQ DD NO: 656 Polypeptide encoded by SEQ ED NO: 655 30 aa SEQ DD NO: 657 HepCla segment 126 90 nts SEQ ED NO: 658 Polypeptide encoded by SEQ ED NO: 657 30 aa SEQ ED NO: 659 HepCla segment 127 90 nts SEQ ED NO: 660 Polypeptide encoded by SEQ ED NO: 659 30 aa SEQ ED NO: 661 HepCla segment 128 90 nts SEQ ED NO: 662 Polypeptide encoded by SEQ ED NO: 661 30 aa SEQ ED NO: 663 HepCla segment 129 90 nts SEQ ED NO: 664 Polypeptide encoded by SEQ DD NO: 663 30 aa SEQ ED NO: 665 HepCla segment 130 90 nts SEQ ED NO: 666 Polypeptide encoded by SEQ ED NO: 665 30 aa SEQ ED NO: 667 HepCla segment 131 90 nts SEQ DD NO: 668 Polypeptide encoded by SEQ ED NO: 667 30 aa SEQ DD NO: 669 HepCla segment 132 90 nts SEQ ED NO: 670 Polypeptide encoded by SEQ ED NO: 669 30 aa SEQUENCE ID SEQUENCE LENGTH NUMBER SEQ ED NO: 671 HepCla segment 133 90 nts SEQ ED NO: 672 Polypeptide encoded by SEQ ED NO: 671 30 aa SEQ ED NO: 673 HepCla segment 134 90 nts SEQ ED NO: 674 Polypeptide encoded by SEQ ED NO: 673 30 aa SEQ ED NO: 675 HepCla segment 135 90 nts SEQ ED NO: 676 Polypeptide encoded by SEQ ED NO: 675 30 aa SEQ ED NO: 677 HepCla segment 136 90 nts SEQ ED NO: 678 Polypeptide encoded by SEQ ED NO: 677 30 aa SEQ ED NO: 679 HepCla segment 137 90 nts SEQ ED NO: 680 Polypeptide encoded by SEQ JD NO: 679 30 aa SEQ ED NO: 681 HepCla segment 138 90 nts SEQ ED NO: 682 Polypeptide encoded by SEQ ED NO: 681 30 aa SEQ ED NO: 683 HepCla segment 139 90 nts SEQ ED NO: 684 Polypeptide encoded by SEQ HD NO: 683 30 aa SEQ ED NO: 685 HepCla segment 140 90 nts SEQ DD NO: 686 Polypeptide encoded by SEQ ED NO: 685 30 aa SEQ DD NO: 687 HepCla segment 141 90 nts SEQ ED NO: 688 Polypeptide encoded by SEQ ED NO: 687 30 aa SEQ ED NO: 689 HepCla segment 142 90 nts SEQ ED NO: 690 Polypeptide encoded by SEQ DD NO: 689 30 aa SEQ DD NO: 691 HepCla segment 143 90 nts SEQ ED NO: 692 Polypeptide encoded by SEQ DD NO: 691 30 aa SEQ ED NO: 693 HepCla segment 144 90 nts SEQ ED NO: 694 Polypeptide encoded by SEQ DD NO: 693 30 aa SEQUENCE ID SEQUENCE LENGTH NUMBER SEQ ED NO: 695 HepCla segment 145 90 nts SEQ ED NO: 696 Polypeptide encoded by SEQ ED NO: 695 30 aa SEQ DD NO: 697 HepCla segment 146 90 nts SEQ DD NO: 698 Polypeptide encoded by SEQ ED NO: 697 30 aa SEQ ED NO: 699 HepCla segment 147 90 nts SEQ DD NO: 700 Polypeptide encoded by SEQ ED NO: 699 30 aa SEQ HD NO: 701 HepCla segment 148 90 nts SEQ HD NO: 702 Polypeptide encoded by SEQ ED NO: 701 30 aa SEQ ED NO: 703 HepCla segment 149 90 nts SEQ ED NO: 704 Polypeptide encoded by SEQ ED NO: 703 30 aa SEQ ED NO: 705 HepCla segment 150 90 nts SEQ ED NO: 706 Polypeptide encoded by SEQ DD NO: 705 30 aa SEQ ED NO: 707 HepCla segment 151 90 nts SEQ ED NO: 708 Polypeptide encoded by SEQ ED NO: 707 30 aa SEQ ED NO: 709 HepCla segment 152 90 nts SEQ ED NO: 710 Polypeptide encoded by SEQ ED NO: 709 30 aa SEQ ED NO: 711 HepCla segment 153 90 nts SEQ ED NO: 712 Polypeptide encoded by SEQ ED NO: 711 30 aa SEQ DD NO: 713 HepCla segment 154 90 nts SEQ DD NO: 714 Polypeptide encoded by SEQ ED NO: 713 30 aa SEQ ED NO: 715 HepCla segment 155 90 nts SEQ ED NO: 716 Polypeptide encoded by SEQ ED NO: 715 30 aa SEQ ED NO: 717 HepCla segment 156 90 nts SEQ DD NO: 718 Polypeptide encoded by SEQ DD NO: 717 30 aa SEQUENCE ID SEQUENCE LENGTH NUMBER SEQ ED NO: 719 HepCla segment 157 90 nts SEQ ED NO: 720 Polypeptide encoded by SEQ ED NO: 719 30 aa SEQ DD NO: 721 HepCla segment 158 90 nts SEQ ED NO: 722 Polypeptide encoded by SEQ ED NO: 721 30 aa SEQ DD NO: 723 HepCla segment 159 90 nts SEQ DD NO: 724 Polypeptide encoded by SEQ ED NO: 723 30 aa SEQ ED NO: 725 HepCla segment 160 90 nts SEQ DD NO: 726 Polypeptide encoded by SEQ ED NO: 725 30 aa SEQ DD NO: 727 HepCla segment 161 90 nts SEQ DD NO: 728 Polypeptide encoded by SEQ JD NO: 727 30 aa SEQ DD NO: 729 HepCla segment 162 90 nts SEQ DD NO: 730 Polypeptide encoded by SEQ ED NO: 729 30 aa SEQ ED NO: 731 HepCla segment 163 90 nts SEQ ED NO: 732 Polypeptide encoded by SEQ ED NO: 731 30 aa SEQ ED NO: 733 HepCla segment 164 90 nts SEQ ED NO: 734 Polypeptide encoded by SEQ ED NO: 733 30 aa SEQ DD NO: 735 HepCla segment 165 90 nts SEQ ED NO: 736 Polypeptide encoded by SEQ ED NO: 735 30 aa SEQ ED NO: 737 HepCla segment 166 90 nts SEQ ED NO: 738 Polypeptide encoded by SEQ ED NO: 737 30 aa SEQ ED NO: 739 HepCla segment 167 90 nts SEQ ED NO: 740 Polypeptide encoded by SEQ DD NO: 739 30 aa SEQ DD NO: 741 HepCla segment 168 90 nts SEQ ED NO: 742 Polypeptide encoded by SEQ ED NO: 741 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ ED NO: 743 HepCla segment 169 90 nts SEQ ED NO: 744 Polypeptide encoded by SEQ ED NO: 743 30 aa SEQ ED NO: 745 HepCla segment 170 90 nts SEQ ID NO: 746 Polypeptide encoded by SEQ ED NO: 745 30 aa SEQ ED NO: 747 HepCla segment 171 90 nts SEQ ED NO: 748 Polypeptide encoded by SEQ DD NO: 747 30 aa SEQ ID NO: 749 HepCla segment 172 90 nts SEQ ED NO: 750 Polypeptide encoded by SEQ ED NO: 749 30 aa SEQ JD NO: 751 HepCla segment 173 90 nts SEQ JD NO: 752 Polypeptide encoded by SEQ ED NO: 751 30 aa SEQ JD NO: 753 HepCla segment 174 90 nts SEQ DD NO: 754 Polypeptide encoded by SEQ ED NO: 753 30 aa SEQ ID NO: 755 HepCla segment 175 90 nts SEQ ED NO: 756 Polypeptide encoded by SEQ ED NO: 755 30 aa SEQ ED NO: 757 HepCla segment 176 90 nts SEQ ED NO: 758 Polypeptide encoded by SEQ ED NO: 757 30 aa SEQ ED NO: 759 HepCla segment 177 90 nts SEQ ED NO: 760 Polypeptide encoded by SEQ DD NO: 759 30 aa SEQ ED NO: 761 HepCla segment 178 90 nts SEQ ED NO: 762 Polypeptide encoded by SEQ ED NO: 761 30 aa SEQ ED NO: 763 HepCla segment 179 90 nts SEQ ED NO: 764 Polypeptide encoded by SEQ ED NO: 763 30 aa SEQ ED NO: 765 HepCla segment 180 90 nts SEQ ED NO: 766 Polypeptide encoded by SEQ ED NO: 765 30 aa SEQUENCE ID SEQUENCE LENGTH NUMBER SEQ ED NO: 767 HepCla segment 181 90 nts SEQ ED NO: 768 Polypeptide encoded by SEQ DD NO: 767 30 aa SEQ ED NO: 769 HepCla segment 182 90 nts SEQ DD NO: 770 Polypeptide encoded by SEQ ED NO: 769 30 aa SEQ ED NO: 771 HepCla segment 183 90 nts SEQ ED NO: 772 Polypeptide encoded by SEQ ED NO: 771 30 aa SEQ ED NO: 773 HepCla segment 184 90 nts SEQ ED NO: 774 Polypeptide encoded by SEQ ED NO: 773 30 aa SEQ ED NO: 775 HepCla segment 185 90 nts SEQ ED NO: 776 Polypeptide encoded by SEQ ED NO: 775 30 aa SEQ ED NO: 777 HepCla segment 186 90 nts SEQ ED NO: 778 Polypeptide encoded by SEQ ED NO: 777 30 aa SEQ ED NO: 779 HepCla segment 187 90 nts SEQ DD NO: 780 Polypeptide encoded by SEQ ED NO: 779 30 aa SEQ HD NO: 781 HepCla segment 188 90 nts SEQ HD NO: 782 Polypeptide encoded by SEQ ED NO: 781 30 aa SEQ ED NO: 783 HepCla segment 189 90 nts SEQ ED NO: 784 Polypeptide encoded by SEQ ED NO: 783 30 aa SEQ ED NO: 785 HepCla segment 190 90 nts SEQ DD NO: 786 Polypeptide encoded by SEQ ED NO: 785 30 aa SEQ ED NO: 787 HepCla segment 191 90 nts SEQ JD NO: 788 Polypeptide encoded by SEQ ED NO: 787 30 aa SEQ ED NO: 789 HepCla segment 192 90 nts SEQ ED NO: 790 Polypeptide encoded by SEQ ED NO: 789 30 aa SEQUENCE ID SEQUENCE LENGTH NUMBER SEQ ED NO: 791 HepCla segment 193 90 nts SEQ ED NO: 792 Polypeptide encoded by SEQ ED NO: 791 30 aa SEQ ED NO: 793 Hep C 1 a segment 194 90 nts SEQ ED NO: 794 Polypeptide encoded by SEQ ED NO: 793 30 aa SEQ DD NO: 795 HepCla segment 195 90 nts SEQ ED NO: 796 Polypeptide encoded by SEQ ED NO: 795 30 aa SEQ ED NO: 797 HepCla segment 196 90 nts SEQ ED NO: 798 Polypeptide encoded by SEQ ED NO: 797 30 aa SEQ ED NO: 799 HepCla segment 197 90 nts SEQ ED NO: 800 Polypeptide encoded by SEQ ED NO: 799 30 aa SEQ ED NO: 801 HepCla segment 198 90 nts SEQ ED NO: 802 Polypeptide encoded by SEQ ED NO: 801 30 aa SEQ ED NO: 803 HepCla segment 199 90 nts SEQ ED NO: 804 Polypeptide encoded by SEQ ED NO: 803 30 aa SEQ ED NO: 805 HepCla segment 200 90 nts SEQ ED NO: 806 Polypeptide encoded by SEQ ED NO: 805 30 aa SEQ ED NO: 807 HepCla segment 201 45 nts SEQ ED NO: 808 Polypeptide encoded by SEQ ED NO: 807 15 aa SEQ D' NO: 809 HepCla scrambled 17955 nts SEQ ED NO: 810 Polypeptide encoded by SEQ ED NO: 809 5985 aa SEQ ED NO: 811 HepC Cassette A 6065 nts SEQ ED NO: 812 Polypeptide encoded by SEQ DD NO: 811 2011 aa SEQ ED NO: 813 HepC Cassette B 6069 nts SEQ ED NO: 814 Polypeptide encoded by SEQ DD NO: 813 2010 aa SEQUENCE ID SEQUENCE LENGTH NUMBER SEQ ED NO: 815 HepC Cassette C 6030 nts SEQ ED NO: 816 Polypeptide encoded by SEQ ED NO: 815 1997 aa SEQ ED NO: 817 gplOO consensus polypeptide 661 aa SEQ DD NO: 818 MART consensus polypeptide 118 aa SEQ ED NO: 819 TRP-1 consensus polypeptide 248 aa SEQ ED NO: 820 Tyros consensus polypeptide 529 aa SEQ ED NO: 821 TRP2 consensus polypeptide 519 aa SEQ ED NO: 822 MC1R consensus polypeptide 317 aa SEQ ED NO: 823 MUC1F consensus polypeptide 125 aa SEQ DD NO: 824 MUCIR consensus polypeptide 312 aa SEQ ED NO: 825 BAGE consensus polypeptide 43 aa SEQ DD NO: 826 GAGE-1 consensus polypeptide 138 aa SEQ DD NO: 827 gpl001n4 consensus polypeptide 51 aa SEQ DD NO: 828 MAGE-1 consensus polypeptide 309 aa SEQ ED NO: 829 MAGE-3 consensus polypeptide 314 aa SEQ ED NO: 830 PRAME consensus polypeptide 509 aa SEQ ED NO: 831 TRP21N2 consensus polypeptide 54 aa SEQ ED NO: 832 NYNSO la consensus polypeptide 180 aa SEQ ED NO: 833 NYNSOlb consensus polypeptide 58 aa SEQ ED NO: 834 LAGEl consensus polypeptide 180 aa SEQ ED NO: 835 gplOO segment 1 90 nts SEQ ED NO: 836 Polypeptide encoded by SEQ JD NO: 835 30 aa SEQ DD NO: 837 gplOO segment 2 90 nts SEQ JD NO: 838 Polypeptide encoded by SEQ ED NO: 837 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ ED NO: 863 gplOO segment 15 90 nts SEQ ED NO: 864 Polypeptide encoded by SEQ ED NO: 863 30 aa SEQ ED NO: 865 gplOO segment 16 90 nts SEQ ED NO: 866 Polypeptide encoded by SEQ ED NO: 865 30 aa SEQ ED NO: 867 g lOO segment 17 90 nts SEQ ED NO: 868 Polypeptide encoded by SEQ ED NO: 867 30 aa SEQ ED NO: 869 gplOO segment 18 90 nts SEQ ED NO: 870 Polypeptide encoded by SEQ ED NO: 869 30 aa SEQ HD NO: 871 gp 100 segment 19 90 nts SEQ ED NO: 872 Polypeptide encoded by SEQ ED NO: 871 30 aa SEQ HD NO: 873 gplOO segment 20 90 nts SEQ HD NO: 874 Polypeptide encoded by SEQ ED NO: 873 30 aa SEQ ED NO: 875 gplOO segment 21 90 nts SEQ ED NO: 876 Polypeptide encoded by SEQ ED NO: 875 30 aa SEQ ED NO: 877 gplOO segment 22 90 nts SEQ ED NO: 878 Polypeptide encoded by SEQ ED NO: 877 30 aa SEQ ED NO: 879 gplOO segment 23 90 nts SEQ ED NO: 880 Polypeptide encoded by SEQ ED NO: 879 30 aa SEQ ED NO: 881 gplOO segment 24 90 nts SEQ HD NO: 882 Polypeptide encoded by SEQ ED NO: 881 30 aa SEQ ED NO: 883 gplOO segment 25 90 nts SEQ ED NO: 884 Polypeptide encoded by SEQ DD NO: 883 30 aa SEQ ED NO: 885 gplOO segment 26 90 nts SEQ ED NO: 886 Polypeptide encoded by SEQ ED NO: 885 30 aa SEQUENCE ID SEQUENCE LENGTH NUMBER SEQ ED NO: 887 gplOO segment 27 90 nts SEQ ED NO: 888 Polypeptide encoded by SEQ DD NO: 887 30 aa SEQ ED NO: 889 gplOO segment 28 90 nts SEQ ED NO: 890 Polypeptide encoded by SEQ ED NO: 889 30 aa SEQ ED NO: 891 gplOO segment 29 90 nts SEQ ED NO: 892 Polypeptide encoded by SEQ ED NO: 891 30 aa SEQ ED NO: 893 gplOO segment 30 90 nts SEQ ED NO: 894 Polypeptide encoded by SEQ ED NO: 893 30 aa SEQ ED NO: 895 gplOO segment 31 90 nts SEQ ED NO: 896 Polypeptide encoded by SEQ ED NO: 895 30 aa SEQ ED NO: 897 gplOO segment 32 90 nts SEQ ED NO: 898 Polypeptide encoded by SEQ ED NO: 897 30 aa SEQ ED NO: 899 gplOO segment 33 90 nts SEQ ED NO: 900 Polypeptide encoded by SEQ ED NO: 899 30 aa SEQ ED NO: 901 gplOO segment 34 90 nts SEQ ED NO: 902 Polypeptide encoded by SEQ ED NO: 901 30 aa SEQ DD NO: 903 gplOO segment 35 90 nts SEQ ED NO: 904 Polypeptide encoded by SEQ ED NO: 903 30 aa SEQ ED NO: 905 gplOO segment 36 90 nts SEQ ED NO: 906 Polypeptide encoded by SEQ ED NO: 905 30 aa SEQ ED NO: 907 gplOO segment 37 90 nts SEQ ED NO: 908 Polypeptide encoded by SEQ ED NO: 907 30 aa SEQ ED NO: 909 gplOO segment 38 90 nts SEQ ED NO: 910 Polypeptide encoded by SEQ ED NO: 909 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ ED NO: 911 gplOO segment 39 90 nts SEQ ED NO: 912 Polypeptide encoded by SEQ ED NO: 911 30 aa SEQ ED NO: 913 gplOO segment 40 90 nts SEQ DD NO: 914 Polypeptide encoded by SEQ ED NO: 913 30 aa SEQ ED NO: 915 gplOO segment 41 90 nts SEQ DD NO: 916 Polypeptide encoded by SEQ DD NO: 915 30 aa SEQ ED NO: 917 gplOO segment 42 90 nts SEQ ED NO: 918 Polypeptide encoded by SEQ ED NO: 917 30 aa SEQ ED NO: 919 gplOO segment 43 90 nts SEQ DD NO: 920 Polypeptide encoded by SEQ ED NO: 919 30 aa SEQ ED NO: 921 gplOO segment 44 60nts SEQ ED NO: 922 Polypeptide encoded by SEQ ED NO: 921 20 aa SEQ ED NO: 923 MART segment 1 90 nts SEQ ED NO: 924 Polypeptide encoded by SEQ ED NO: 923 30 aa SEQ ED NO: 925 MART segment 2 90 nts SEQ ED NO: 926 Polypeptide encoded by SEQ ED NO: 925 30 aa SEQ ED NO: 927 MART segment 3 90 nts SEQ ED NO: 928 Polypeptide encoded by SEQ ED NO: 927 30 aa SEQ ED NO: 929 MART segment 4 90 nts SEQ HD NO: 930 Polypeptide encoded by SEQ ED NO: 929 30 aa SEQ ED NO: 931 MART segment 5 90 nts SEQ ED NO: 932 Polypeptide encoded by SEQ ED NO: 931 30 aa SEQ ED NO: 933 MART segment 6 90 nts SEQ ED NO: 934 Polypeptide encoded by SEQ ED NO: 933 30 aa SEQUENCE ID SEQUENCE LENGTH NUMBER SEQ ED NO: 1007 tyros segment 19 90 nts SEQ ED NO: 1008 Polypeptide encoded by SEQ ED NO: 1007 30 aa SEQ ED NO: 1009 tyros segment 20 90 nts SEQ ED NO: 1010 Polypeptide encoded by SEQ ED NO: 1009 30 aa SEQ ED NO: 1011 tyros segment 21 90 nts SEQ ED NO: 1012 Polypeptide encoded by SEQ ED NO: 1011 30 aa SEQ ED NO: 1013 tyros segment 22 90 nts SEQ ED NO: 1014 Polypeptide encoded by SEQ ED NO: 1013 30 aa SEQ ED NO: 1015 tyros segment 23 90 nts SEQ ED NO: 1016 Polypeptide encoded by SEQ ED NO: 1015 30 aa SEQ ED NO: 1017 tyros segment 24 90 nts SEQ ED NO: 1018 Polypeptide encoded by SEQ ED NO: 1017 30 aa SEQ ED NO: 1019 tyros segment 25 90 nts SEQ ED NO: 1020 Polypeptide encoded by SEQ DD NO: 1019 30 aa SEQ ED NO: 1021 tyros segment 26 90 nts SEQ ED NO: 1022 Polypeptide encoded by SEQ ID NO: 1021 30 aa SEQ ED NO: 1023 tyros segment 27 90 nts SEQ ED NO: 1024 Polypeptide encoded by SEQ ED NO: 1023 30 aa SEQ ED NO: 1025 tyros segment 28 90 nts SEQ ED NO: 1026 Polypeptide encoded by SEQ ED NO: 1025 30 aa SEQ ED NO: 1027 tyros segment 29 90 nts SEQ DD NO: 1028 Polypeptide encoded by SEQ ED NO: 1027 30 aa SEQ ED NO: 1029 tyros segment 30 90 nts SEQ ED NO: 1030 Polypeptide encoded by SEQ ID NO: 1029 30 aa SEQUENCER) SEQUENCE LENGTH NUMBER SEQ DD NO: 1103 trp2 segment 32 90 nts SEQ ED NO: 1104 Polypeptide encoded by SEQ DD NO: 1103 30 aa SEQ DD NO: 1105 trp2 segment 33 90 nts SEQ DD NO: 1106 Polypeptide encoded by SEQ ED NO: 1105 30 aa SEQ ED NO: 1107 trp2 segment 34 84 nts SEQ ED NO: 1108 Polypeptide encoded by SEQ ED NO: 1107 28 aa SEQ ED NO: 1109 MC1R segment 1 90 nts SEQ ED NO: 1110 Polypeptide encoded by SEQ ED NO: 1109 30 aa SEQ ED NO: l lll MC1R segment 2 90 nts SEQ ED NO: 1112 Polypeptide encoded by SEQ JD NO: l l l l 30 aa SEQ ED NO: 1113 MC1R segment 3 90 nts SEQ DD NO: 1114 Polypeptide encoded by SEQ ED NO: 1113 30 aa SEQ DD NO: 1115 MC1R segment 4 90 nts SEQ DD NO: 1116 Polypeptide encoded by SEQ ED NO: 1115 30 aa SEQ ED NO: 1117 MC1R segment 5 90 nts SEQ ED NO: 1118 Polypeptide encoded by SEQ ED NO: 1117 30 aa SEQ ED NO: 1119 MC1R segment 6 90 nts SEQ ED NO: 1120 Polypeptide encoded by SEQ ED NO: 1119 30 aa SEQ ED NO: 1121 MC1R segment 7 90 nts SEQ ED NO: 1122 Polypeptide encoded by SEQ ED NO: 1121 30 aa SEQ JD NO: 1123 MC1R segment 8 90 nts SEQ ED NO: 1124 Polypeptide encoded by SEQ ED NO: 1123 30 aa SEQ ED NO: 1125 MC1R segment 9 90 nts SEQ D NO: 1126 Polypeptide encoded by SEQ ED NO: 1125 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ ED NO: 1127 MC1R segment 10 90 nts SEQ ED NO: 1128 Polypeptide encoded by SEQ ED NO: 1127 30 aa SEQ ED NO: 1129 MC1R segment 11 90 nts SEQ ED NO: 1130 Polypeptide encoded by SEQ ED NO: 1129 30 aa SEQ ED NO: 1131 MC1R segment 12 90 nts SEQ ED NO: 1132 Polypeptide encoded by SEQ ED NO: 1131 30 aa SEQ ED NO: 1133 MC1R segment 13 90 nts SEQ ED NO: 1134 Polypeptide encoded by SEQ ED NO: 1133 30 aa SEQ ED NO: 1135 MC1R segment 14 90 nts SEQ ED NO: 1136 Polypeptide encoded by SEQ ED NO: 1135 30 aa SEQ ED NO: 1137 MC1R segment 15 90 nts SEQ ED NO: 1138 Polypeptide encoded by SEQ ED NO: 1137 30 aa SEQ ED NO: 1139 MC1R segment 16 90 nts SEQ ED NO: 1140 Polypeptide encoded by SEQ ED NO: 1139 30 aa SEQ ED NO: 1141 MC1R segment 17 90 nts SEQ ED NO: 1142 Polypeptide encoded by SEQ ID NO: 1141 30 aa SEQ ED NO: 1143 MC1R segment 18 90 nts SEQ ED NO: 1144 Polypeptide encoded by SEQ DD NO: 1143 30 aa SEQ ED NO: 1145 MC1R segment 19 90 nts SEQ ED NO: 1146 Polypeptide encoded by SEQ ED NO: 1145 30 aa SEQ ED NO: 1147 MC1R segment 20 90 nts SEQ ED NO: 1148 Polypeptide encoded by SEQ ED NO: 1147 30 aa SEQ HD NO: 1149 MC1R segment 21 63 nts SEQ ED NO: 1150 Polypeptide encoded by SEQ ED NO: 1149 21 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ DD O: 1151 MUC1F segment 1 90 nts SEQ DD NO: 1152 Polypeptide encoded by SEQ ED NO: 1151 30 aa SEQ DD NO: 1153 MUC1F segment 2 90 nts SEQ DD NO: 1154 Polypeptide encoded by SEQ ED NO: 1153 30 aa SEQ DD NO: 1155 MUCIF segment 3 90 nts SEQ DD NO: 1156 Polypeptide encoded by SEQ ED NO: 1155 30 aa SEQ DD NO: 1157 MUCIF segment 4 90 nts SEQ ED NO: 1158 Polypeptide encoded by SEQ DD NO: 1157 30 aa SEQ ED NO: 1159 MUCIF segment 5 90 nts SEQ ED NO: 1160 Polypeptide encoded by SEQ ED NO: 1159 30 aa SEQ DD NO: 1161 MUCIF segment 6 90 nts SEQ ED NO: 1162 Polypeptide encoded by SEQ DD NO: 1161 30 aa SEQ ED NO: 1163 MUCIF segment 7 90 nts SEQ DD NO: 1164 Polypeptide encoded by SEQ ED NO: 1163 30 aa SEQ ED NO: 1165 MUCIF segment 8 72 nts SEQ ED NO: 1166 Polypeptide encoded by SEQ ED NO: 1165 24 aa SEQ ED NO: 1167 MUC1R segment 1 90 nts SEQ ED NO: 1168 Polypeptide encoded by SEQ ED NO: 1167 30 aa SEQ ED NO: 1169 MUC1R segment 2 90 nts SEQ ED NO: 1170 Polypeptide encoded by SEQ ED NO: 1169 30 aa SEQ ED NO: 1171 MUC1R segment 3 90 nts SEQ ED NO: 1172 Polypeptide encoded by SEQ ED NO: 1171 30 aa SEQ ED NO: 1173 MUC1R segment 4 90 nts SEQ ED NO: 1174 Polypeptide encoded by SEQ ED NO: 1173 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ ED NO: 1175 MUC1R segment 5 90 nts SEQ ED NO: 1176 Polypeptide encoded by SEQ DD NO: 1175 30 aa SEQ ED NO: 1177 MUCIR segment 6 90 nts SEQ ED NO: 1178 Polypeptide encoded by SEQ ED NO: 1177 30 aa SEQ ED NO: 1179 MUCIR segment 7 90 nts SEQ ED NO: 1180 Polypeptide encoded by SEQ ED NO: 1179 30 aa SEQ ED NO: 1181 MUCIR segment 8 90 nts SEQ ED NO: 1182 Polypeptide encoded by SEQ ED NO: 1181 30 aa SEQ DD NO: 1183 MUCIR segment 9 90 nts SEQ DD NO: 1184 Polypeptide encoded by SEQ ED NO: 1183 30 aa SEQ ED NO: 1185 MUCIR segment 10 90 nts SEQ ED NO: 1186 Polypeptide encoded by SEQ ED NO: 1185 30 aa SEQ D NO: 1187 MUCIR segment 11 90 nts SEQ ED NO: 1188 Polypeptide encoded by SEQ ED NO: 1187 30 aa SEQ ED NO: 1189 MUCIR segment 12 90 nts SEQ ED NO: 1190 Polypeptide encoded by SEQ ED NO: 1189 30 aa SEQ ED NO: 1191 MUCIR segment 13 90 nts SEQ ED NO: 1192 Polypeptide encoded by SEQ ED NO: 1191 30 aa SEQ ED NO: 1193 MUCIR segment 14 90 nts SEQ ED NO: 1194 Polypeptide encoded by SEQ ED NO: 1193 30 aa SEQ ED NO: 1195 MUCIR segment 15 90 nts SEQ DD NO: 1196 Polypeptide encoded by SEQ DD NO: 1195 30 aa SEQ DD NO: 1197 MUCIR segment 16 90 nts SEQ DD NO: 1198 Polypeptide encoded by SEQ ED NO: 1197 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ DD NO: 1199 MUCIR segment 17 90 nts SEQ DD NO: 1200 Polypeptide encoded by SEQ ED NO: 1199 30 aa SEQ DD NO: 1201 MUCIR segment 18 90 nts SEQ ED NO: 1202 Polypeptide encoded by SEQ ED NO: 1201 30 aa SEQ ED NO: 1203 MUCIR segment 19 90 nts SEQ ED NO: 1204 Polypeptide encoded by SEQ ED NO: 1203 30 aa SEQ ED NO: 1205 MUCIR segment 20 90 nts SEQ ED NO: 1206 Polypeptide encoded by SEQ ED NO: 1205 30 aa SEQ ED NO: 1207 MUCIR segment 21 48 nts SEQ JD NO: 1208 Polypeptide encoded by SEQ ED NO: 1207 16 aa SEQ DD NO: 1209 Differentiation Savine 16638 nts SEQ DD NO: 1210 Polypeptide encoded by SEQ ED NO: 1209 5546 aa SEQ DD NO: 1211 BAGE segment 1 90 nts SEQ ED NO: 1212 Polypeptide encoded by SEQ ED NO: 1211 30 aa SEQ ED NO: 1213 BAGE segment 2 90 nts SEQ ED NO: 1214 Polypeptide encoded by SEQ ED NO: 1213 30 aa SEQ ED NO: 1215 BAGE segment 3 51 nts SEQ ED NO: 1216 Polypeptide encoded by SEQ ED NO: 1215 17 aa SEQ ED NO: 1217 GAGE-1 segment 1 90 nts SEQ DD NO: 1218 Polypeptide encoded by SEQ HD NO: 1217 30 aa SEQ ED NO: 1219 GAGE-1 segment 2 90 nts SEQ ED NO: 1220 Polypeptide encoded by SEQ ED NO: 1219 30 aa SEQ ED NO: 1221 GAGE-1 segment 3 90 nts SEQ ED NO: 1222 Polypeptide encoded by SEQ DD NO: 1221 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ ED NO: 1223 GAGE-1 segment 4 90 nts SEQ ED NO: 1224 Polypeptide encoded by SEQ ED NO: 1223 30 aa SEQ ED NO: 1225 GAGE-1 segment 5 90 nts SEQ ED NO: 1226 Polypeptide encoded by SEQ ED NO: 1225 30 aa SEQ ID NO: 1227 GAGE-1 segment 6 90 nts SEQ ED NO: 1228 Polypeptide encoded by SEQ DD NO: 1227 30 aa SEQ ED NO: 1229 GAGE-1 segment 7 90 nts SEQ ED NO: 1230 Polypeptide encoded by SEQ ED NO: 1229 30 aa SEQ ED NO: 1231 GAGE-1 segment 8 90 nts SEQ ED NO: 1232 Polypeptide encoded by SEQ ED NO: 1231 30 aa SEQ ED NO: 1233 GAGE-1 segment 9 66 nts SEQ ED NO: 1234 Polypeptide encoded by SEQ ED NO: 1233 22 aa SEQ ED NO: 1235 gpl001n4 segment 1 90 nts SEQ ED NO: 1236 Polypeptide encoded by SEQ ED NO: 1235 30 aa SEQ DD NO: 1237 gpl001n4 segment 2 90 nts SEQ ED NO: 1238 Polypeptide encoded by SEQ ED NO: 1237 30 aa SEQ ED NO: 1239 gpl001n4 segment 3 75 nts SEQ ED NO: 1240 Polypeptide encoded by SEQ ED NO: 1239 25 aa SEQ ED NO: 1241 MAGE-1 segment 1 90 nts SEQ ED NO: 1242 Polypeptide encoded by SEQ ED NO: 1241 30 aa SEQ ED NO: 1243 MAGE-1 segment 2 90 nts SEQ ED NO: 1244 Polypeptide encoded by SEQ ED NO: 1243 30 aa SEQ ED NO: 1245 MAGE-1 segment 3 90 nts SEQ ED NO: 1246 Polypeptide encoded by SEQ ED NO: 1245 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ JD NO: 1247 MAGE-1 segment 4 90 nts SEQ D NO: 1248 Polypeptide encoded by SEQ ED NO: 1247 30 aa SEQ DD NO: 1249 MAGE-1 segment 5 90 nts SEQ ED NO: 1250 Polypeptide encoded by SEQ ED NO: 1249 30 aa SEQ DD O: 1251 MAGE-1 segment 6 90 nts SEQ ED NO: 1252 Polypeptide encoded by SEQ ED NO: 1251 30 aa SEQ DD NO: 1253 MAGE-1 segment 7 90 nts SEQ DD NO: 1254 Polypeptide encoded by SEQ HD NO: 1253 30 aa SEQ ED NO: 1255 MAGE-1 segment 8 90 nts SEQ DD NO: 1256 Polypeptide encoded by SEQ ED NO: 1255 30 aa SEQ ED NO: 1257 MAGE-1 segment 9 90 nts SEQ ED NO: 1258 Polypeptide encoded by SEQ ED NO: 1257 30 aa SEQ ED NO: 1259 MAGE-1 segment 10 90 nts SEQ ED NO: 1260 Polypeptide encoded by SEQ ED NO: 1259 30 aa SEQ ED NO: 1261 MAGE-1 segment 11 90 nts SEQ ED NO: 1262 Polypeptide encoded by SEQ ED NO: 1261 30 aa SEQ ED NO: 1263 MAGE-1 segment 12 90 nts SEQ ED NO: 1264 Polypeptide encoded by SEQ ED NO: 1263 30 aa SEQ ED NO: 1265 MAGE-1 segment 13 90 nts SEQ ED NO: 1266 Polypeptide encoded by SEQ ED NO: 1265 30 aa SEQ ED NO: 1267 MAGE-1 segment 14 90 nts SEQ ED NO: 1268 Polypeptide encoded by SEQ ED NO: 1267 30 aa SEQ ED NO: 1269 MAGE-1 segment 15 90 nts SEQ ED NO: 1270 Polypeptide encoded by SEQ ED NO: 1269 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ HD NO: 1271 MAGE-1 segment 16 90 nts SEQ HD NO: 1272 Polypeptide encoded by SEQ ED NO: 1271 30 aa SEQ ED NO: 1273 MAGE-1 segment 17 90 nts SEQ ED NO: 1274 Polypeptide encoded by SEQ ED NO: 1273 30 aa SEQ ED NO: 1275 MAGE-1 segment 18 90 nts SEQ ED NO: 1276 Polypeptide encoded by SEQ ED NO: 1275 30 aa SEQ ED NO: 1277 MAGE-1 segment 19 90 nts SEQ ED NO: 1278 Polypeptide encoded by SEQ ED NO: 1277 ' 30 aa SEQ ED NO: 1279 MAGE-1 segment 20 84 nts SEQ ED NO: 1280 Polypeptide encoded by SEQ DD NO: 1279 28 aa SEQ ED NO: 1281 MAGE-3 segment 1 90 nts SEQ DD NO: 1282 Polypeptide encoded by SEQ ED NO: 1281 30 aa SEQ ED NO: 1283 MAGE-3 segment 2 90 nts SEQ ED NO: 1284 Polypeptide encoded by SEQ ED NO: 1283 30 aa SEQ ED NO: 1285 MAGE-3 segment 3 90 nts SEQ ED NO: 1286 Polypeptide encoded by SEQ ED NO: 1285 30 aa SEQ ED NO: 1287 MAGE-3 segment 4 90 nts SEQ ED NO: 1288 Polypeptide encoded by SEQ ED NO: 1287 30 aa SEQ ED NO: 1289 MAGE-3 segment 5 90 nts SEQ ED NO: 1290 Polypeptide encoded by SEQ ED NO: 1289 30 aa SEQ HD NO: 1291 MAGE-3 segment 6 90 nts SEQ ED NO: 1292 Polypeptide encoded by SEQ ED NO: 1291 30 aa SEQ ED NO: 1293 MAGE-3 segment 7 90 nts SEQ ED NO: 1294 Polypeptide encoded by SEQ ED NO: 1293 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ ED NO: 1295 MAGE-3 segment 8 90 nts SEQ ED NO: 1296 Polypeptide encoded by SEQ ED NO: 1295 30 aa SEQ ED NO: 1297 MAGE-3 segment 9 90 nts SEQ ED NO: 1298 Polypeptide encoded by SEQ ED NO: 1297 30 aa SEQ ED NO: 1299 MAGE-3 segment 10 90 nts SEQ ED NO: 1300 Polypeptide encoded by SEQ ED NO: 1299 30 aa SEQ ED NO: 1301 MAGE-3 segment 11 90 nts SEQ DD NO: 1302 Polypeptide encoded by SEQ ED NO: 1301 30 aa SEQ ED NO: 1303 MAGE-3 segment 12 90 nts SEQ ED NO: 1304 Polypeptide encoded by SEQ ED NO: 1303 30 aa SEQ ED NO: 1305 MAGE-3 segment 13 90 nts SEQ ED NO: 1306 Polypeptide encoded by SEQ D NO: 1305 30 aa SEQ DD NO: 1307 MAGE-3 segment 14 90 nts SEQ DD NO: 1308 Polypeptide encoded by SEQ DD NO: 1307 30 aa SEQ ED NO: 1309 MAGE-3 segment 15 90 nts SEQ ED NO: 1310 Polypeptide encoded by SEQ DD NO: 1309 30 aa SEQ ED NO: 1311 MAGE-3 segment 16 90 nts SEQ HD NO: 1312 Polypeptide encoded by SEQ ED NO: 1311 30 aa SEQ DD NO: 1313 MAGE-3 segment 17 90 nts SEQ DD NO: 1314 Polypeptide encoded by SEQ ED NO: 1313 30 aa SEQ DD NO: 1315 MAGE-3 segment 18 90 nts SEQ ED NO: 1316 Polypeptide encoded by SEQ ED NO: 1315 30 aa SEQ ED NO: 1317 MAGE-3 segment 19 90 nts SEQ ED NO: 1318 Polypeptide encoded by SEQ ED NO: 1317 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ ED NO: 1319 MAGE-3 segment 20 90 nts SEQ ED NO: 1320 Polypeptide encoded by SEQ ED NO: 1319 30 aa SEQ ED NO: 1321 MAGE-3 segment 21 54 nts SEQ ED NO: 1322 Polypeptide encoded by SEQ DD NO: 1321 18 aa SEQ ED NO: 1323 PRAME segment 1 90 nts SEQ ED NO: 1324 Polypeptide encoded by SEQ ED NO: 1323 30 aa SEQ ED NO: 1325 PRAME segment 2 90 nts SEQ ED NO: 1326 Polypeptide encoded by SEQ ED NO: 1325 30 aa SEQ ED NO: 1327 PRAME segment 3 90 nts SEQ ED NO: 1328 Polypeptide encoded by SEQ ED NO: 1327 30 aa SEQ ED NO: 1329 PRAME segment 4 90 nts SEQ DD NO: 1330 Polypeptide encoded by SEQ ED NO: 1329 30 aa SEQ DD NO: 1331 PRAME segment 5 90 nts SEQ DD NO: 1332 Polypeptide encoded by SEQ ED NO: 1331 30 aa SEQ DD NO: 1333 PRAME segment 6 90 nts SEQ ED NO: 1334 Polypeptide encoded by SEQ ED NO: 1333 30 aa SEQ ED NO: 1335 PRAME segment 7 90 nts SEQ DD NO: 1336 Polypeptide encoded by SEQ ED NO: 1335 30 aa SEQ ED NO: 1337 PRAME segment 8 90 nts SEQ ED NO: 1338 Polypeptide encoded by SEQ ED NO: 1337 30 aa SEQ DD NO: 1339 PRAME segment 9 90 nts SEQ DD NO: 1340 Polypeptide encoded by SEQ ED NO: 1339 30 aa SEQ ED NO: 1341 PRAME segment 10 90 nts SEQ DD NO: 1342 Polypeptide encoded by SEQ ED NO: 1341 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ ED NO: 1343 PRAME segment 11 90 nts SEQ ED NO: 1344 Polypeptide encoded by SEQ DD NO: 1343 30 aa SEQ DD NO: 1345 PRAME segment 12 90 nts SEQ DD NO: 1346 Polypeptide encoded by SEQ ED NO: 1345 30 aa SEQ DD NO: 1347 PRAME segment 13 90 nts SEQ ED NO: 1348 Polypeptide encoded by SEQ DD NO: 1347 30 aa SEQ ED NO: 1349 PRAME segment 14 90 nts SEQ ED NO: 1350 Polypeptide encoded by SEQ ED NO: 1349 30 aa SEQ ED NO: 1351 PRAME segment 15 90 nts SEQ ED NO: 1352 Polypeptide encoded by SEQ ED NO: 1351 30 aa SEQ ED NO: 1353 PRAME segment 16 90 nts SEQ ED NO: 1354 Polypeptide encoded by SEQ ED NO: 1353 30 aa SEQ ID NO: 1355 PRAME segment 17 90 nts SEQ ED NO: 1356 Polypeptide encoded by SEQ ED NO: 1355 30 aa SEQ ED NO: 1357 PRAME segment 18 90 nts SEQ ED NO: 1358 Polypeptide encoded by SEQ ED NO: 1357 30 aa SEQ ED NO: 1359 PRAME segment 19 90 nts SEQ ED NO: 1360 Polypeptide encoded by SEQ DD NO: 1359 30 aa SEQ DD NO: 1361 PRAME segment 20 90 nts SEQ ED NO: 1362 Polypeptide encoded by SEQ ED NO: 1361 30 aa SEQ ED NO: 1363 PRAME segment 21 90 nts SEQ ED NO: 1364 Polypeptide encoded by SEQ ED NO: 1363 30 aa SEQ DD NO: 1365 PRAME segment 22 90 nts SEQ DD NO: 1366 Polypeptide encoded by SEQ DD NO: 1365 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ DD NO: 1367 PRAME segment 23 90 nts SEQ DD NO: 1368 Polypeptide encoded by SEQ ED NO: 1367 30 aa SEQ DD NO: 1369 PRAME segment 24 90 nts SEQ ED NO: 1370 Polypeptide encoded by SEQ ED NO: 1369 30 aa SEQ ED NO: 1371 PRAME segment 25 90 nts SEQ ED NO: 1372 Polypeptide encoded by SEQ ED NO: 1371 30 aa SEQ ED NO: 1373 PRAME segment 26 90 nts SEQ DD NO: 1374 Polypeptide encoded by SEQ ED NO: 1373 30 aa SEQ DD NO: 1375 PRAME segment 27 90 nts SEQ DD NO: 1376 Polypeptide encoded by SEQ DD NO: 1375 30 aa SEQ DD NO: 1377 PRAME segment 28 90 nts SEQ ED NO: 1378 Polypeptide encoded by SEQ ED NO: 1377 30 aa SEQ ED NO: 1379 PRAME segment 29 90 nts SEQ ED NO: 1380 Polypeptide encoded by SEQ ED NO: 1379 30 aa SEQ ED NO: 1381 PRAME segment 30 90 nts SEQ ED NO: 1382 Polypeptide encoded by SEQ ED NO: 1381 30 aa SEQ ED NO: 1383 PRAME segment 31 90 nts SEQ ED NO: 1384 Polypeptide encoded by SEQ ID NO: 1383 30 aa SEQ ED NO: 1385 PRAME segment 32 90 nts SEQ ED NO: 1386 Polypeptide encoded by SEQ ED NO: 1385 30 aa SEQ ED NO: 1387 PRAME segment 33 90 nts SEQ ED NO: 1388 Polypeptide encoded by SEQ ED NO: 1387 30 aa SEQ ED NO: 1389 PRAME segment 34 54 nts SEQ ED NO: 1390 Polypeptide encoded by SEQ ED NO: 1389 18 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ DD NO: 1391 TRP21N2 segment 1 90 nts SEQ ED NO: 1392 Polypeptide encoded by SEQ ED NO: 1391 30 aa SEQ ED NO: 1393 TRP21N2 segment 2 90 nts SEQ DD NO: 1394 Polypeptide encoded by SEQ DD NO: 1393 30 aa SEQ ED NO: 1395 TRP21N2 segment 3 84 nts SEQ ED NO: 1396 Polypeptide encoded by SEQ DD NO: 1395 28 aa SEQ DD NO: 1397 NYNSOla segment 1 90 nts SEQ ED NO: 1398 Polypeptide encoded by SEQ ED NO: 1397 30 aa SEQ ED NO: 1399 NYNSOla segment 2 90 nts SEQ ED NO: 1400 Polypeptide encoded by SEQ ED NO: 1399 30 aa SEQ DD NO: 1401 NYNSOla segment 3 90 nts SEQ DD NO: 1402 Polypeptide encoded by SEQ ED NO: 1401 30 aa SEQ ED NO: 1403 NYNSOla segment 4 90 nts SEQ DD NO: 1404 Polypeptide encoded by SEQ ED NO: 1403 30 aa SEQ ED NO: 1405 NYNSOla segment 5 90 nts SEQ HD NO: 1406 Polypeptide encoded by SEQ ED NO: 1405 30 aa SEQ ED NO: 1407 NYNSOla segment 6 90 nts SEQ ED NO: 1408 Polypeptide encoded by SEQ ED NO: 1407 30 aa SEQ ED NO: 1409 NYNSOla segment 7 90 nts SEQ DD NO: 1410 Polypeptide encoded by SEQ ED NO: 1409 30 aa SEQ DD NO: 1411 NYNSOla segment 8 90 nts SEQ DD NO: 1412 Polypeptide encoded by SEQ ED NO: 1411 30 aa SEQ DD NO: 1413 NYNSOla segment 9 90 nts SEQ ED NO: 1414 Polypeptide encoded by SEQ ED NO: 1413 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ DD NO: 1415 NYNSOla segment 10 90 nts SEQ DD NO: 1416 Polypeptide encoded by SEQ DD NO: 1415 30 aa SEQ ED NO: 1417 NYNSOla segment 11 90 nts SEQ DD NO: 1418 Polypeptide encoded by SEQ ED NO: 1417 30 aa SEQ ED NO: 1419 NYNSOla segment 12 57 nts SEQ ED NO: 1420 Polypeptide encoded by SEQ ED NO: 1419 19 aa SEQ DD NO: 1421 NYNSOlb segment 1 90 nts SEQ ED NO: 1422 Polypeptide encoded by SEQ DD NO: 1421 30 aa SEQ ED NO: 1423 NYNSOlb segment 2 90 nts SEQ ED NO: 1424 Polypeptide encoded by SEQ DD NO: 1423 30 aa SEQ DD NO: 1425 NYNSOlb segment 3 90 nts SEQ DD NO: 1426 Polypeptide encoded by SEQ ED NO: 1425 30 aa SEQ DD NO: 1427 NYNSOlb segment 4 51 nts SEQ DD NO: 1428 Polypeptide encoded by SEQ ED NO: 1427 SEQ DD NO: 1429 LAGEl segment 1 90 nts SEQ ED NO: 1430 Polypeptide encoded by SEQ DD NO: 1429 30 aa SEQ ED NO: 1431 LAGEl segment 2 90 nts SEQ ED NO: 1432 Polypeptide encoded by SEQ ED NO: 1431 30 aa SEQ ED NO: 1433 LAGEl segment 3 90 nts SEQ ED NO: 1434 Polypeptide encoded by SEQ ED NO: 1433 30 aa SEQ DD NO: 1435 LAGEl segment 4 90 nts SEQ DD NO: 1436 Polypeptide encoded by SEQ ED NO: 1435 30 aa SEQ ED NO: 1437 LAGEl segment 5 90 nts SEQ ED NO: 1438 Polypeptide encoded by SEQ ED NO: 1437 30 aa SEQUENCEID SEQUENCE LENGTH NUMBER SEQ ED NO: 1439 LAGEl segment 6 90 nts SEQ ED NO: 1440 Polypeptide encoded by SEQ ED NO: 1439 30 aa SEQ ED NO: 1441 LAGEl segment 7 90 nts SEQ ED NO: 1442 Polypeptide encoded by SEQ ED NO: 1441 30 aa SEQ ED NO: 1443 LAGEl segment 8 90 nts SEQ DD NO: 1444 Polypeptide encoded by SEQ ID NO: 1443 30 aa SEQ ED NO: 1445 LAGEl segment 9 90 nts SEQ ED NO: 1446 Polypeptide encoded by SEQ ED NO: 1445 30 aa SEQ ED NO: 1447 LAGEl segment 10 90 nts SEQ ED NO: 1448 Polypeptide encoded by SEQ ED NO: 1447 30 aa SEQ ED NO: 1449 LAGEl segment 11 90 nts SEQ ED NO: 1450 Polypeptide encoded by SEQ ED NO: 1449 30 aa SEQ H NO: 1451 LAGEl segment 12 57 nts SEQ ED NO: 1452 Polypeptide encoded by SEQ ED NO: 1451 19 aa SEQ DD NO: 1453 Melanoma cancer specific Savine 10623 nts SEQ DD NO: 1454 Polypeptide encoded by SEQ ED NO: 1453 3541 aa SEQ ED NO: 1455 Figure 16 A1S1 99mer 99 nts SEQ DD NO: 1456 Figure 16 A1S2 lOOmer 100 nts SEQ DD NO: 1457 Figure 16 Al S3 lOOmer 100 nts SEQ DD NO: 1458 Figure 16 A1S4 lOOmer 100 nts SEQ DD NO: 1459 Figure 16 A1S5 lOOmer 100 nts SEQ ED NO: 1460 Figure 16 A1S6 99mer 99 nts SEQ ED NO: 1461 Figure 16 AlS7 97mer 99 nts SEQ DD NO: 1462 Figure 16 A1S8 lOOmer 100 nts DETAILED DESCRIPTION OF THE INVENTION 1. Definitions The articles "a" and "an " are used herein to refer to one or to more than one (i.e., to at least one) of the grammatical object of the article. By way of example, "an element" means one element or more than one element. As used herein, the term "about" refers to a quantity, level, value, dimension, size, or amount that varies by as much as 30%, preferably by as much as 20%, and more preferably by as much as 10% to a reference quantity, level, value, dimension, size, or amount. By "antigen-binding molecule " is meant a molecule that has binding affinity for a target antigen. It will be understood that this term extends to immunoglobulins, immunoglobulin fragments and non-immunoglobulin derived protein frameworks that exhibit antigen-binding activity. The term "clade " as used herein refers to a hypothetical species of an organism and its descendants or a monophyletic group of organisms. Clades carry a definition, based on ancestry, and a diagnosis, based on synapomorphies. It should be noted that diagnoses of clades could change while definitions do not. Throughout this specification, unless the context requires otherwise, the words "comprise ", "comprises " and "comprising" will be understood to imply the inclusion of a stated step or element or group of steps or elements but not the exclusion of any other step or element or group of steps or elements. By "expression vector" is meant any autonomous genetic element capable of directing the synthesis of a protein encoded by the vector. Such expression vectors are known by practitioners in the art. As used herein, the term "function " refers to a biological, enzymatic, or therapeutic function. "Homology " refers to the percentage number of amino acids that are identical or constitute conservative substitutions as defined in Table B infra. Homology may be determined using sequence comparison programs such as GAP (Deveraux et al. 1984, Nucleic Acids Research 12, 387-395). In this way, sequences of a similar or substantially different length to those cited herein might be compared by insertion of gaps into the alignment, such gaps being determined, for example, by the comparison algorithm used by GAP. To enhance an immune response ("immunoenhancement"), as is well-known in the art, means to increase an animal's capacity to respond to foreign or disease-specific antigens (e.g., cancer antigens) i.e., those cells primed to attack such antigens are increased in number, activity, and ability to detect and destroy the those antigens. Strength of immune response is measured by standard tests including: direct measurement of peripheral blood lymphocytes by means known to the art; natural killer cell cytotoxicity assays (see, e.g., Provinciali M. et al (1992, J. Immunol Meth. 155: 19-24), cell proliferation assays (see, e.g., Vollenweider, I. and Groseurth, P. J. (1992, J. Immunol Meth. 149: 133-135), immunoassays of immune cells and subsets (see, e.g., Loeffler, D. A., et al. (1992, Cytom. 13: 169-174); Rivoltini, L., et al. (1992, Can. Immunol. Immunother. 34: 241-251); or skin tests for cell-mediated immunity (see, e.g., Chang, A. E. et al (1993, Cancer Res. 53: 1043-1050). Any statistically significant increase in strength of immune response as measured by the foregoing tests is considered "enhanced immune response" "immunoenhancement" or "immunopotentiation" as used herein. Enhanced immune response is also indicated by physical manifestations such as fever and inflammation, as well as healing of systemic and local infections, and reduction of symptoms in disease, i.e., decrease in tumour size, alleviation of symptoms of a disease or condition including, but not restricted to, leprosy, tuberculosis, malaria, naphthous ulcers, herpetic and papillomatous warts, gingivitis, artherosclerosis, the concomitants of AEDS such as Kaposi's sarcoma, bronchial infections, and the like. Such physical manifestations also define "enhanced immune response" "immunoenhancement" or "immunopotentiation " as used herein. Reference herein to "immuno-interactive" includes reference to any interaction, reaction, or other form of association between molecules and in particular where one of the molecules is, or mimics, a component of the immune system. By "isolated" is meant material that is substantially or essentially free from components that normally accompany it in its native state. By "modulating" is meant increasing or decreasing, either directly or indirectly, an immune response against a target antigen of a member selected from the group consisting of a cancer and an organism, preferably a pathogenic organism. By "natural gene " is meant a gene that naturally encodes a protein. The term "natural polypeptide" as used herein refers to a polypeptide that exists in nature. By "obtained from " is meant that a sample such as, for example, a polynucleotide extract or polypeptide extract is isolated from, or derived from, a particular source of the host. For example, the extract can be obtained from a tissue or a biological fluid isolated directly from the host. The term "oligonucleotide" as used herein refers to a polymer composed of a multiplicity of nucleotide residues (deoxyribonucleotides or ribonucleotides, or related structural variants or synthetic analogues thereof) linked via phosphodiester bonds (or related structural variants or synthetic analogues thereof). Thus, while the term "oligonucleotide" typically refers to a nucleotide polymer in which the nucleotide residues and linkages between them are naturally occurring, it will be understood that the term also includes within its scope various analogues including, but not restricted to, peptide nucleic acids (PNAs), phosphoramidates, phosphorothioates, methyl phosphonates, 2-O-methyl ribonucleic acids, and the like. The exact size of the molecule can vary depending on the particular application. An oligonucleotide is typically rather short in length, generally from about 10 to 30 nucleotide residues, but the term can refer to molecules of any length, although the term "polynucleotide" or "nucleic acid" is typically used for large oligonucleotides. By "operably linked" is meant that transcriptional and translational regulatory polynucleotides are positioned relative to a polypeptide-encoding polynucleotide in such a manner that the polynucleotide is transcribed and the polypeptide is translated. The term "parent polypeptide " as used herein typically refers to a polypeptide encoded by a natural gene. However, it is possible that the parent polypeptide corresponds to a protein that is not naturally-occurring but has been engineered using recombinant techniques. In this instance, a polynucleotide encoding the parent polypeptide may comprise different but synonymous codons relative to a natural gene encoding the same polypeptide. Alternatively, the parent polypeptide may not correspond to a natural polypeptide sequence. For example, the parent polypeptide may comprise one or more consensus sequences common to a plurality of polypeptides. The term "patient" refers to patients of human or other mammal and includes any individual it is desired to examine or treat using the methods of the invention. However, it will be understood that "patient" does not imply that symptoms are present. Suitable mammals that fall within the scope of the invention include, but are not restricted to, primates, livestock animals (e.g., sheep, cows, horses, donkeys, pigs), laboratory test animals (e.g., rabbits, mice, rats, guinea pigs, hamsters), companion animals (e.g., cats, dogs) and captive wild animals (e.g., foxes, deer, dingoes). By "pharmaceutically-acceptable carrier" is meant a solid or liquid filler, diluent or encapsulating substance that can be safely used in topical or systemic administration to a mammal. "Polypeptide", "peptide" and "protein" are used interchangeably herein to refer to a polymer of amino acid residues and to variants and synthetic analogues of the same. Thus, these terms apply to amino acid polymers in which one or more amino acid residues is a synthetic non-narurally occurring amino acid, such as a chemical analogue of a corresponding naturally occurring amino acid, as well as to naturally-occurring amino acid polymers. The term "polynucleotide" or "nucleic acid ' ' as used herein designates mRNA, RNA, cRNA, cDNA or DNA. The term typically refers to oligonucleotides greater than 30 nucleotide residues in length. By "primer" is meant an oligonucleotide which, when paired with a strand of DNA, is capable of initiating the synthesis of a primer extension product in the presence of a suitable polymerising agent. The primer is preferably single-stranded for maximum efficiency in amplification but can alternatively be double-stranded. A primer must be sufficiently long to prime the synthesis of extension products in the presence of the polymerisation agent. The length of the primer depends on many factors, including application, temperature to be employed, template reaction conditions, other reagents, and source of primers. For example, depending on the complexity of the target sequence, the oligonucleotide primer typically contains 15 to 35 or more nucleotide residues, although it can contain fewer nucleotide residues. Primers can be large polynucleotides, such as from about 35 nucleotides to several kilobases or more. Primers can be selected to be "substantially complementary" to the sequence on the template to which it is designed to hybridise and serve as a site for the initiation of synthesis. By "substantially complementary", it is meant that the primer is sufficiently complementary to hybridise with a target polynucleotide. Preferably, the primer contains no mismatches with the template to which it is designed to hybridise but this is not essential. For example, non- complementary nucleotide residues can be attached to the 5' end of the primer, with the remainder of the primer sequence being complementary to the template. Alternatively, non-complementary nucleotide residues or a stretch of non-complementary nucleotide residues can be interspersed into a primer, provided that the primer sequence has sufficient complementarity with the sequence of the template to hybridise therewith and thereby form a template for synthesis of the extension product of the primer. "Probe " refers to a molecule that binds to a specific sequence or sub-sequence or other moiety of another molecule. Unless otherwise indicated, the term "probe" typically refers to a polynucleotide probe that binds to another polynucleotide, often called the "target polynucleotide", through complementary base pairing. Probes can bind target polynucleotides lacking complete sequence complementarity with the probe, depending on the stringency of the hybridisation conditions. Probes can be labelled directly or indirectly. By "recombinant polypeptide " is meant a polypeptide made using recombinant techniques, i.e., through the expression of a recombinant or synthetic polynucleotide. Terms used to describe sequence relationships between two or more polynucleotides or polypeptides include "reference sequence", "comparison window", "sequence identity", "percentage of sequence identity" and "substantial identity". A "reference sequence" is at least 12 but frequently 15 to 18 and often at least 25 monomer units, inclusive of nucleotides and amino acid residues, in length. Because two polynucleotides may each comprise (1) a sequence (i.e., only a portion of the complete polynucleotide sequence) that is similar between the two polynucleotides, and (2) a sequence that is divergent between the two polynucleotides, sequence comparisons between two (or more) polynucleotides are typically performed by comparing sequences of the two polynucleotides over a "comparison window" to identify and compare local regions of sequence similarity. A "comparison window" refers to a conceptual segment of at least 50 contiguous positions, usually about 50 to about 100, more usually about 100 to about 150 in which a sequence is compared to a reference sequence of the same number of contiguous positions after the two sequences are optimally aligned. The comparison window may comprise additions or deletions (i.e., gaps) of about 20% or less as compared to the reference sequence (which does not comprise additions or deletions) for optimal alignment of the two sequences. Optimal alignment of sequences for aligning a comparison window may be conducted by computerised implementations of algorithms (GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package Release 7.0, Genetics Computer Group, 575 Science Drive Madison, WI, USA) or by inspection and the best alignment (i.e., resulting in the highest percentage homology over the comparison window) generated by any of the various methods selected. Reference also may be made to the BLAST family of programs as for example disclosed by Altschul et al, 1997, Nucl. Acids Res. 25:3389. A detailed discussion of sequence analysis can be found in Unit 19.3 of Ausubel et al, "Current Protocols in Molecular Biology", John Wiley & Sons Inc, 1994-1998, Chapter 15. The term "sequence identity" as used herein refers to the extent that sequences are identical on a nucleotide-by-nucleotide basis or an amino acid-by-amino acid basis over a window of comparison. Thus, a "percentage of sequence identity" is calculated by comparing two optimally aligned sequences over the window of comparison, determining the number of positions at which the identical nucleic acid base (e.g., A, T, C, G, I) or the identical amino acid residue (e.g., Ala, Pro, Ser, Thr, Gly, Val, Leu, lie, Phe, Tyr, Tip, Lys, Arg, His, Asp, Glu, Asn, Gin, Cys and Met) occurs in both sequences to yield the number of matched positions, dividing the number of matched positions by the total number of positions in the window of comparison (i.e., the window size), and multiplying the result by 100 to yield the percentage of sequence identity. For the purposes of the present invention, "sequence identity" will be understood to mean the "match percentage" calculated by the DNASIS computer program (Version 2.5 for windows; available from Hitachi Software engineering Co., Ltd., South San Francisco, California, USA) using standard defaults as used in the reference manual accompanying the software. The term "synthetic polynucleotide" as used herein refers to a polynucleotide formed in vitro by the manipulation of a polynucleotide into a form not normally found in nature. For example, the synthetic polynucleotide can be in the form of an expression vector. Generally, such expression vectors include transcriptional and translational regulatory polynucleotide operably linked to the polynucleotide. The term "synonymous codon " as used herein refers to a codon having a different nucleotide sequence than another codon but encoding the same amino acid as that other codon. By "translational efficiency" is meant the efficiency of a cell's protein synthesis machinery to incorporate the amino acid encoded by a codon into a nascent polypeptide chain. This efficiency can be evidenced, for example, by the rate at which the cell is able to synthesise the polypeptide from an RNA template comprising the codon, or by the amount of the polypeptide synthesised from such a template. By "vector" is meant a polynucleotide molecule, preferably a DNA molecule derived, for example, from a plasmid, bacteriophage, yeast or virus, into which a polynucleotide can be inserted or cloned. A vector preferably contains one or more unique restriction sites and can be capable of autonomous replication in a defined host cell including a target cell or tissue or a progenitor cell or tissue thereof, or be integrable with the genome of the defined host such that the cloned sequence is reproducible. Accordingly, the vector can be an autonomously replicating vector, i.e., a vector that exists as an extrachromosomal entity, the replication of which is independent of chromosomal replication, e.g., a linear or closed circular plasmid, an extrachromosomal element, a minichromosome, or an artificial chromosome. The vector can contain any means for assuring self-replication. Alternatively, the vector can be one which, when introduced into the host cell, is integrated into the genome and replicated together with the chromosome(s) into which it has been integrated. A vector system can comprise a single vector or plasmid, two or more vectors or plasmids, which together contain the total DNA to be introduced into the genome of the host cell, or a transposon. The choice of the vector will typically depend on the compatibility of the vector with the host cell into which the vector is to be introduced. In the present case, the vector is preferably a viral or viral-derived vector, which is operably functional in animal and preferably mammalian cells. Such vector may be derived from a poxvirus, an adenovirus or yeast. The vector can also include a selection marker such as an antibiotic resistance gene that can be used for selection of suitable transformants. Examples of such resistance genes are known to those of skill in the art and include the nptll gene that confers resistance to the antibiotics kanamycin and G418 (Geneticin®) and the hph gene which confers resistance to the antibiotic hygromycin B. 2. Synthetic polypeptides The inventors have surprisingly discovered that the structure of a parent polypeptide can be disrupted sufficiently to impede, abrogate or otherwise alter at least one function of the parent polypeptide, while simultaneously minimising the destruction of potentially useful epitopes that are present in the parent polypeptide, by fusing, coupling or otherwise linking together different segments of the parent polypeptide in a different relationship relative to their linkage in the parent polypeptide. As a result of this change in relationship, the sequence of the linked segments in the resulting synthetic polypeptide is different to a sequence contained within the parent polypeptide. The synthetic polypeptides of the invention are useful as immunopotentiating agents, and are referred to elsewhere in the specification as scrambled antigen vaccines, super attenuated vaccines or "Savines ". Thus, the invention broadly resides in a synthetic polypeptide comprising a plurality of different segments of at least one parent polypeptide, wherein said segments are linked together in a different relationship relative to their linkage in the at least one parent polypeptide. It is preferable but not essential that the segments in said synthetic polypeptide are linked sequentially in a different order or arrangement relative to that of corresponding segments in said at least one parent polypeptide. For example, in the case of a parent polypeptide that comprises three contiguous or overlapping segments A-B-C-D, these segments may be linked in 23 other possible orders to form a synthetic polypeptide. These orders may be selected from the group consisting of: A-B-D-C, A-C-B-D, A-C-D-B, A-D- B-C, A-D-C-B, B-A-C-D, B-A-D-C, B-C-A-D, B-C-D-A, B-D-A-C, B-D-C-A, C-A-B-D, C-A-D-B, C-B-A-D, C-B-D-A, C-D-A-B, C-D-B-A, D-A-B-C, D-A-C-B, D-B-A-C, D-B- C-A, D-C-A-B, and D-C-B-A. Although the rearrangement of the segments is preferably random, it is especially preferable to exclude or otherwise minimise rearrangements that result in complete or partial reassembly of the parent sequence (e.g., ADBC, BACD, DABC). It will be appreciated, however, that the probability of such complete or partial reassembly diminishes as the number of segments for rearrangement increases. The order of the segments is suitably shuffled, reordered or otherwise rearranged relative to the order in which they exist in the parent polypeptide so that the structure of the polypeptide is disrupted sufficiently to impede, abrogate or otherwise alter at least one function associated with the parent polypeptide. Preferably, the segments of the parent polypeptide are randomly rearranged in the synthetic polypeptide. The parent polypeptide is suitably a polypeptide that is associated with a disease or condition. For example, the parent polypeptide may be a polypeptide expressed by a pathogenic organism or a cancer. Alternatively, the parent polypeptide can be a self peptide related to an autoimmune disease including, but are not limited to, diseases such as diabetes (e.g., juvenile diabetes), multiple sclerosis, rheumatoid arthritis, myasthenia gravis, atopic dermatitis, and psoriasis and ankylosing spondylitis. Accordingly, the synthetic molecules of the present invention may also have utility for the induction of tolerance in a subject afflicted with an autoimmune disease or condition or with an allergy or other condition to which tolerance is desired. For example tolerance may be induced by contacting an immature dendritic cell of the individual to be treated with a synthetic polypeptide of the invention or by expressing in an immature dendritic cell a synthetic polynucleotide of the invention. Tolerance may also be induced against antigens causing allergic responses (e.g., asthma, hay fever). In this case, the parent polypeptide is suitably an allergenic protein including, but not restricted to, house-dust-mite allergenic proteins as for example described by Thomas and Smith (1998, Allergy, 53(9): 821-832). The pathogenic organism includes, but is not restricted to, yeast, a virus, a bacterium, and a parasite. Any natural host of the pathogenic organism is contemplated by the present invention and includes, but is not limited to, mammals, avians and fish. In a preferred embodiment, the pathogenic organism is a virus, which may be an RNA virus or a DNA virus. Preferably, the RNA virus is Human Immunodeficiency Virus (HJV), Poliovirus, and Influenza virus, Rous sarcoma virus, or a Flavivirus such as Japanese encephalitis virus. In a preferred embodiment, the RNA virus is a Hepatitis virus including, but not limited to, Hepatitis strains A, B and C. Suitably, the DNA virus is a Herpesvirus including, but not limited to, Herpes simplex virus, Epstein-Barr virus, Cytomegalovirus and Parvovirus. In a preferred embodiment, the virus is HJV and the parent polypeptide is suitably selected from env, gag, pol, vif, vpr, tat, rev, vpu and nef, or combination thereof. In an alternate preferred embodiment, the virus is Hepatitis Cla virus and the parent polypeptide is the Hepatitis Cla virus polyprotein. In another embodiment, the pathogenic organism is a bacterium, which includes, but is not restricted to, Neisseria species, Meningococcal species, Haemophilus species Salmonella species, Streptococcal species, Legionella species and Mycobacterium species. In yet another embodiment, the pathogenic organism is a parasite, which includes, but is not restricted to, Plasmodium species, Schistosoma species, Leishmania species, Trypanosoma species, Toxoplasma species and Giardia species. Any cancer or tumour is contemplated by the present invention. For example, the cancer or tumour includes, but is not restricted to, melanoma, lung cancer, breast cancer, cervical cancer, prostate cancer, colon cancer, pancreatic cancer, stomach cancer, bladder cancer, kidney cancer, post transplant lymphoproliferative disease (PTLD), Hodgkin's Lymphoma and the like. Preferably, the cancer or tumour relates to melanoma. In a preferred embodiment of this type, the parent polypeptide is a melanocyte differentiation antigen which is suitably selected from gplOO, MART, TRP-1, Tyros, TRP2, MC1R, MUCIF, MUCIR or a combination thereof. In an alternate preferred embodiment of this type, the parent polypeptide is a melanoma-specific antigen which is suitably selected from BAGE, GAGE-1, gpl00In4, MAGE-1, MAGE-3, PRAME, TRP2IN2, NYNSOla, NYNSOlb, LAGEl or a combination thereof. In a preferred embodiment, the segments are selected on the basis of size. A segment according to the invention may be of any suitable size that can be utilised to elicit an immune response against an antigen encoded by the parent polypeptide. A number of factors can influence the choice of segment size. For example, the size of a segment should be preferably chosen such that it includes, or corresponds to the size of, T cell epitopes and their processing requirement. Practitioners in the art will recognise that class I-restricted T cell epitopes can be between 8 and 10 amino acids in length and if placed next to unnatural flanking residues, such epitopes can generally require 2 to 3 natural flanking amino acids to ensure that they are efficiently processed and presented. Class Il-restricted T cell epitopes can range between 12 and 25 amino acids in length and may not require natural flanking residues for efficient proteolytic processing although it is believed that natural flanking residues may play a role. Another important feature of class π-restricted epitopes is that they generally contain a core of 9-10 amino acids in the middle which bind specifically to class E MHC molecules with flanking sequences either side of this core stabilising binding by associating with conserved structures on either side of class II MHC antigens in a sequence independent manner (Brown et al, 1993). Thus the functional region of class H-restricted epitopes is typically less than 15 amino acids long. The size of linear B cell epitopes and the factors effecting their processing, like class H-restricted epitopes, are quite variable although such epitopes are frequently smaller in size than 15 amino acids. From the foregoing, it is preferable, but not essential, that the size of the segment is at least 4 amino acids, preferably at least 7 amino acids, more preferably at least 12 amino acids, more preferably at least 20 amino acids and more preferably at least 30 amino acids. Suitably, the size of the segment is less than 2000 amino acids, more preferably less than 1000 amino acids, more preferably less than 500 amino acids, more preferably less than 200 amino acids, more preferably less than 100 amino acids, more preferably less than 80 amino acids and even more preferably less than 60 amino acids and still even more preferably less than 40 amino acids. In this regard, it is preferable that the size of the segments is as small as possible so that the synthetic polypeptide adopts a functionally different structure relative to the structure of the parent polypeptide. It is also preferable that the size of the segments is large enough to minimise loss of T cell epitopes. In an especially preferred embodiment, the size of the segment is about 30 amino acids. An optional spacer may be utilised to space adjacent segments relative to each other. Accordingly, an optional spacer may be interposed between some or all of the segments. The spacer suitably alters proteolytic processing and/or presentation of adjacent segment(s). In a preferred embodiment of this type, the spacer promotes or otherwise enhances proteolytic processing and/or presentation of adjacent segment(s). Preferably, the spacer comprises at least one amino acid. The at least one amino acid is suitably a neutral amino acid. The neutral amino acid is preferably alanine. Alternatively, the at least one amino acid is cysteine. In a preferred embodiment, segments are selected such that they have partial sequence identity or homology with one or more other segments. Suitably, at one or both ends of a respective segment there is comprised at least 4 contiguous amino acids, preferably at least 7 contiguous amino acids, more preferably at least 10 contiguous amino acids, more preferably at least 15 contiguous amino acids and even more preferably at least 20 contiguous amino acids that are identical to, or homologous with, an amino acid sequence contained within one or more other of said segments. Preferably, at the or each end of a respective segment there is comprised less than 500 contiguous amino acids, more preferably less than 200 contiguous amino acids, more preferably less than 100 contiguous amino acids, more preferably less than 50 contiguous amino acids, more preferably less than 40 contiguous amino acids, and even more preferably less than 30 contiguous amino acids that are identical to, or homologous with, an amino acid sequence contained within one or more other of said segments. Such sequence overlap (also referred to elsewhere in the specification as "overlapping fragments" or "overlapping segments") is preferable to ensure potential epitopes at segment boundaries are not lost and to ensure that epitopes at or near segment boundaries are processed efficiently if placed beside or near amino acids that inhibit processing. Preferably, the segment size is about twice the size of the overlap. Jh a preferred embodiment, when segments have partial sequence homology therebetween, the homologous sequences suitably comprise conserved and/or non- conserved amino acid differences. Exemplary conservative substitutions are listed in the following table. TABLE B Conserved or non-conserved differences may correspond to polymorphisms in corresponding parent polypeptides. Polymorphic polypeptides are expressed by various pathogenic organisms and cancers. For example, the polymorphic polypeptides may be expressed by different viral strains or clades or by cancers in different individuals. Sequence overlap between respective segments is preferable to minimise destruction of any epitope sequences that may result from any shuffling or rearrangement of the segments relative to their existing order in the parent polypeptide. If overlapping segments as described above are employed to form a synthetic polypeptide, it may not be necessary to change the order in which those segments are linked together relative to the order in which corresponding segments are normally present in the parent polypeptide. In this regard, such overlapping segments when linked together in the synthetic polypeptide can adopt a different structure relative to the structure of the parent polypeptide, wherein the different structure does not provide for one or more functions associated with the parent polypeptide. For example, in the case of four segments A-B-C-D each spanning 30 contiguous amino acids of the parent polypeptide and having a 10-amino acid overlapping sequence with one or more adjacent segments, the synthetic polypeptide will have duplicated 10-amino acid sequences bridging segments A-B, B-C and C-D. The presence of these duplicated sequences may be sufficient to render a different structure and to abrogate or alter function relative to the parent polypeptide. fri a preferred embodiment, segment size is about 30 amino acids and sequence overlap at one or both ends of a respective segment is about 15 amino acids. However, it will be understood that other suitable segment sizes and sequence overlap sizes are contemplated by the present invention, which can be readily ascertained by persons of skill in the art. It is preferable but not necessary to utilise all the segments of the parent polypeptide in the construction of the synthetic polypeptide. Suitably, at least 30%, preferably at least 40%, more preferably at least 50%, even more preferably at least 60%, even more preferably at least 70%, even more preferably at least 80% and still even more preferably at least 90% of the parent polypeptide sequence is used in the construction of the synthetic polypeptide. However, it will be understood that the more sequence infoπnation from a parent polypeptide that is utilised to construct the synthetic polypeptide, the greater the population coverage will be of the synthetic polypeptide as an immunogen. Preferably, no sequence information from the parent polypeptide is excluded (e.g. , because of an apparent lack of immunological epitopes). Persons of skill in the art will appreciate that when preparing a synthetic polypeptide against a pathogenic organism (e.g., a virus) or a cancer, it may be preferable to use sequence information from a plurality of different polypeptides expressed by the organism or the cancer. Accordingly, in a preferred embodiment, segments from a plurality of different polypeptides are linked together to form a synthetic polypeptide according to the invention. It is preferable in this respect to utilise as many parent polypeptides as possible from, or in relation to, a particular source in the construction of the synthetic polypeptide. The source of parent polypeptides includes, but is not limited to, a pathogenic organism and a cancer. Suitably, at least about 30%, preferably at least 40%, more preferably at least 50%, even more preferably at least 60%, even more preferably at least 70%, even more preferably at least 80% and still even more preferably at least 90% of the parent polypeptides expressed by the source is used in the construction of the synthetic polypeptide. Preferably, parent polypeptides from a virus include, but are not restricted to, latent polypeptides, regulatory polypeptides or polypeptides expressed early during their replication cycle. Suitably, parent polypeptides from a parasite or bacterium include, but are not restricted to, secretory polypeptides and polypeptides expressed on the surface of the parasite or bacteria. It is preferred that parent polypeptides from a cancer or tumour are cancer specific polypeptides. Suitably, hypervariable sequences within the parent polypeptide are excluded from the construction of the synthetic polypeptide. The synthetic polypeptides of the inventions may be prepared by any suitable procedure known to those of skill in the art. For example, the polypeptide may be synthesised using solution synthesis or solid phase synthesis as described, for example, in Chapter 9 of Atherton and Shephard (1989, Solid Phase Peptide Synthesis: A Practical Approach. IRL Press, Oxford) and in Roberge et al (1995, Science 269: 202). Syntheses may employ, for example, either t-butyloxycarbonyl (t-Boc) or 9- fluorenylmethyloxycarbonyl (Fmoc) chemistries (see Chapter 9.1, of Coligan et al, CURRENT PROTOCOLS IN PROTEIN SCIENCE, John Wiley & Sons, Inc. 1995-1997; Stewart and Young, 1984, Solid Phase Peptide Synthesis, 2nd ed. Pierce Chemical Co., Rockford, 111; and Atherton and Shephard, supra). Alternatively, the polypeptides may be prepared by a procedure including the steps of: (a) preparing a synthetic construct including a synthetic polynucleotide encoding a synthetic polypeptide wherein said synthetic polynucleotide is operably linked to a regulatory polynucleotide, wherein said synthetic polypeptide comprises a plurality of different segments of a parent polypeptide, wherein said segments are linked together in a different relationship relative to their linkage in the parent polypeptide; (b) introducing the synthetic construct into a suitable host cell; (c) culturing the host cell to express the synthetic polypeptide from said synthetic construct; and (d) isolating the synthetic polypeptide. The synthetic construct is preferably in the form of an expression vector. For example, the expression vector can be a self-replicating extra-chromosomal vector such as a plasmid, or a vector that integrates into a host genome. Typically, the regulatory polynucleotide may include, but is not limited to, promoter sequences, leader or signal sequences, ribosomal binding sites, transcriptional start and stop sequences, translational start and termination sequences, and enhancer or activator sequences. Constitutive or inducible promoters as known in the art are contemplated by the invention. The promoters may be either naturally occurring promoters, or hybrid promoters that combine elements of more than one promoter. The regulatory polynucleotide will generally be appropriate for the host cell used for expression. Numerous types of appropriate expression vectors and suitable regulatory polynucleotides are known in the art for a variety of host cells. In a preferred embodiment, the expression vector contains a selectable marker gene to allow the selection of transformed host cells. Selection genes are well known in the art and will vary with the host cell used. The expression vector may also include a fusion partner (typically provided by the expression vector) so that the synthetic polypeptide of the invention is expressed as a fusion polypeptide with said fusion partner. The main advantage of fusion partners is that they assist identification and/or purification of said fusion polypeptide. In order to express said fusion polypeptide, it is necessary to ligate a polynucleotide according to the invention into the expression vector so that the translational reading frames of the fusion partner and the polynucleotide coincide. Well known examples of fusion partners include, but are not limited to, glutathione-S-transferase (GST), Fc portion of human IgG, maltose binding protein (MBP) and hexahistidine (HIS 6 ), which are particularly useful for isolation of the fusion polypeptide by affinity chromatography. For the purposes of fusion polypeptide purification by affinity chromatography, relevant matrices for affinity chromatography are glutathione-, amylose-, and nickel- or cobalt-conjugated resins respectively. Many such matrices are available in "kit" form, such as the QIAexpress™ system (Qiagen) useful with (HIS 6 ) fusion partners and the Pharmacia GST purification system. In a preferred embodiment, the recombinant polynucleotide is expressed in the commercial vector pFLAG™. Another fusion partner well known in the art is green fluorescent protein (GFP). ' This fusion partner serves as a fluorescent "tag" which allows the fusion polypeptide of the invention to be identified by fluorescence microscopy or by flow cytometry. The GFP tag is useful when assessing subcellular localisation of a fusion polypeptide of the invention, or for isolating cells which express a fusion polypeptide of the invention. Flow cytometric methods such as fluorescence activated cell sorting (FACS) are particularly useful in this latter application. Preferably, the fusion partners also have protease cleavage sites, such as for Factor X a , Thrombin and inteins (protein introns), which allow the relevant protease to partially digest the fusion polypeptide of the invention and thereby liberate the recombinant polypeptide of the invention therefrom. The liberated polypeptide can then be isolated from the fusion partner by subsequent chromatographic separation. Fusion partners according to the invention also include within their scope "epitope tags", which are usually short peptide sequences for which a specific antibody is available. Well known examples of epitope tags for which specific monoclonal antibodies are readily available include c-Myc, influenza virus, haemagglutinin and FLAG tags. Alternatively, a fusion partner may be provided to promote other forms of immunity. For example, the fusion partner may be an antigen-binding molecule that is immuno-interactive with a conformational epitope on a target antigen or to a post-translational modification of a target antigen (e.g., an antigen-binding molecule that is immuno-interactive with a glycosylated target antigen). The step of introducing the synthetic construct into the host cell may be effected by any suitable method including transfection, and transformation, the choice of which will be dependent on the host cell employed. Such methods are well known to those of skill in ' the art. Synthetic polypeptides of the invention may be produced by culturing a host cell transformed with the synthetic construct. The conditions appropriate for protein expression will vary with the choice of expression vector and the host cell. This is easily ascertained by one skilled in the art through routine experimentation. Suitable host cells for expression may be prokaryotic or eukaryotic. One preferred host cell for expression of a polypeptide according to the invention is a bacterium. The bacterium used may be Escherichia coli. Alternatively, the host cell may be an insect cell such as, for example, SF9 cells that may be utilised with a baculovirus expression system. The synthetic polypeptide may be conveniently prepared by a person skilled in the art using standard protocols as for example described in Sambrook, et al, MOLECULAR CLONING. A LABORATORY MANUAL (Cold Spring Harbor Press, 1989), in particular Sections 16 and 17; Ausubel et al, CURRENT PROTOCOLS IN MOLECULAR BIOLOGY (John Wiley & Sons, Inc. 1994-1998), in particular Chapters 10 and 16; and Coligan et al, CURRENT PROTOCOLS IN PROTEIN SCIENCE (John Wiley & Sons, Inc. 1995-1997), in particular Chapters 1, 5 and 6. The amino acids of the synthetic polypeptide can be any non-naturally occurring or any naturally occurring amino acid. Examples of unnatural amino acids and derivatives during peptide synthesis include but are not limited to, use of 4-amino butyric acid, 6- aminohexanoic acid, 4-amino-3-hydroxy-5-phenylpentanoic acid, 4-amino-3-hydroxy-6- methylheptanoic acid, t-butylglycine, norleucine, norvaline, phenylglycine, ornithine, sarcosine, 2-thienyl alanine and/or D-isomers of amino acids. A list of unnatural amino acids contemplated by the present invention is shown in TABLE C. TABLE C Non-conventional amino acid Non-conventional amino acid D-histidine L-N-methylphenylalanine D-isoleucine L-N-methylproline D-leucine L-N-medlylserine D-lysine L-N-methylthreonine D-methionine L-N-methyltryptophan D-ornithine L-N-methyltyrosine D-phenylalanine L-N-methylvaline D-proline L-N-methylethylglycine D-serine L-N-methyl-t-butylglycine D-threonine L-norleucine D-tryptophan L-norvaline D-tyrosine α-methyl-aminoisobutyrate D-valine α-methyl-γ-aminobutyrate D-α-methylalanine α-methylcyclohexylalanine D-α-methylarginine α-methylcylcopentylalanine D-α-methylasparagine α-methyl-α-napthylalanine D-c-methylaspartate α-methylpenicillamine D-α-methylcysteine N-(4-aminobutyl)glycine D-θ!-methylglutamine N-(2-aminoethyl)glycine D-α-methylhistidine N-(3-aminopropyl)glycine D-c-methylisoleucine N-amino-o!-methylbutyrate D-α-methylleucine α-napthylalanine D-α-methyllysine N-benzylglycine D-c-methyhnethionine N-(2-carbamylediyl)glycine D-α-methylornithiine N-(carbamylmethyl)glycine Non-conventional amino acid Non-conventional amino acid D-α-methylphenylalanine N-(2-carboxyethyl)glycine D-α-methylproline N-(carboxymethyl)glycine D-α-methylserine N-cyclobutylglycine D-θ!-methylthreonine N-cycloheptylglycine D-α-methyltryptophan N-cyclohexylglycine D-α-methyltyrosine N-cyclodecylglycine L-α-methylleucine L-α-methyllysine L-α-methylmethionine L-α-methylnorleucine L-α-methylnorvatine L-α-methylornithine L-α-methylphenylalanine L-c-methylproline L-α-methylserine L-cϋ-methylthreonine L-α-methyltryptophan L-α-methyltyrosine L-o;-methylvaline L-N-methylhomophenylalanine N-(N-(2,2-diphenylethyl N-(N-(3,3-diphenylpropyl carbamylmethyl)glycine carbamylmethyl)glycine 1 -carboxy- 1 -(2,2-diρhenyl-ethyl amino)cyclopropane The invention also contemplates modifying the synthetic polypeptides of the invention using ordinary molecular biological techniques so as to alter their resistance to proteolytic degradation or to optimise solubility properties or to render them more suitable as an immunogenic agent. 3. Preparation of synthetic polynucleotides of the invention The invention contemplates synthetic polynucleotides encoding the synthetic polypeptides as for example described in Section 2 supra. Polynucleotides encoding segments of a parent polypeptide can be produced by any suitable technique. For example, such polynucleotides can be synthesised de novo using readily available machinery. Sequential synthesis of DNA is described, for example, in U.S. Patent No 4,293,652. Instead of de novo synthesis, recombinant techniques may be employed including use of restriction endonucleases to cleave a polynucleotide encoding at least a segment of the parent polypeptide and use of ligases to ligate together in frame a plurality of cleaved polynucleotides encoding different segments of the parent polypeptide. Suitable recombinant techniques are described for example in the relevant sections of Ausubel, et al. (supra) and of Sambrook, et al, (supra) which are incorporated herein by reference. Preferably, the synthetic polynucleotide is constructed using splicing by overlapping extension (SOEing) as for example described by Horton et al. (1990, Biotechniques 8(5): 528-535; 1995, Mol Biotechnol. 3(2): 93-99; and 1997, Methods Mol Biol. 67: 141-149). However, it should be noted that the present invention is not dependent on, and not directed to, any one particular technique for constructing the synthetic construct. Various modifications to the synthetic polynucleotides may be introduced as a means of increasing intracellular stability and half-life. Possible modifications include but are not limited to the addition of flanking sequences of ribo- or deoxy- nucleotides to the 5' and/or 3' ends of the molecule or the use of phosphorothioate or 2' O-methyl rather than phosphodiesterase linkages within the oligodeoxyribonucleotide backbone. The invention therefore contemplates a method of producing a synthetic polynucleotide as broadly described above, comprising linking together in the same reading frame at least two nucleic acid sequences encoding different segments of a parent polypeptide to form a synthetic polynucleotide, which encodes a synthetic polypeptide according to the invention. Suitably, nucleic acid sequences encoding at least 10 segments, preferably at least 20 segments, more preferably at least 40 segments and more preferably at least 100 segments of a parent polypeptide are employed to produce the synthetic polynucleotide. Preferably, the method further comprises selecting segments of the parent polypeptide, reverse translating the selected segments and preparing nucleic acid sequences encoding the selected segments. It is preferred that the method further comprises randomly linking the nucleic acid sequences together to form the synthetic polynucleotide. The nucleic acid sequences may be oligonucleotides or polynucleotides. Suitably, segments are selected on the basis of size. Additionally, or in the alternative, segments are selected such that they have partial sequence identity or homology (i.e., sequence overlap) with one or more other segments. A number of factors can influence segment size and sequence overlap as mentioned above. In the case of sequence overlap, large amounts of duplicated nucleic acid sequences can sometimes result in sections of nucleic acid being lost during nucleic acid amplification (e.g., polymerase chain reaction, PCR) of such sequences, recombinant plasmid propagation in a bacterial host or during amplification of recombinant viruses containing such sequences. Accordingly, in a preferred embodiment, nucleic acid sequences encoding segments having sequence identity or homology with one or more other encoded segments are not linked together in an arrangement in which the identical or homologous sequences are contiguous. Also, it is preferable that different codons are used to encode a specific amino acid in a duplicated region. In this context, an amino acid of a parent polypeptide sequence is preferably reverse translated to provide a codon which, in the context of adjacent or local sequence elements, has a lower propensity of forming an undesirable sequence (e.g., a duplicated sequence or a palindromic sequence) that is refractory to the execution of a task (e.g., cloning or sequencing). Alternatively, segments may be selected such that they contain a carboxyl terminal leucine residue or such that reverse translated sequences encoding the segments contain restriction enzyme sites for convenient splicing of the reverse translated sequences. The method optionally further comprises linking a spacer oligonucleotide encoding at least one spacer residue between segment-encoding nucleic acids. Such spacer residue(s) may be advantageous in ensuring that epitopes within the segments are processed and presented efficiently. Preferably, the spacer oligonucleotide encodes 2 to 3 spacer residues. The spacer residue is suitably a neutral amino acid, which is preferably alanine. Optionally, the method further comprises linking in the same reading frame as other segment-containing nucleic acid sequences at least one variant nucleic acid sequence which encodes a variant segment having a homologous but not identical amino acid sequence relative to other encoded segments. Suitably, the variant segment comprises conserved and/or non-conserved amino acid differences relative to one or more other encoded segments. Such differences may correspond to polymorphisms as discussed above. In a preferred embodiment, degenerate bases are designed or built in to the at least one variant nucleic acid sequence to give rise to all desired homologous sequences. When a large number of polymorphisms is intended to be covered, it is preferred that multiple synthetic polynucleotides are constructed rather than a single synthetic polynucleotide, which encodes all variant segments. For example, if there is less than 85% homology between polymorphic polypeptides, then it is preferred that more than one synthetic polynucleotide is constructed. Preferably, the method further comprises optimising the codon composition of the synthetic polynucleotide such that it is translated efficiently by a host cell. In this regard, it is well known that the translational efficiency of different codons varies between organisms and that such differences in codon usage can be utilised to enhance the level of protein expression in a particular organism. In this regard, reference may be made to Seed et al. (International Application Publication No WO 96/09378) who disclose the replacement of existing codons in a parent polynucleotide with synonymous codons to enhance expression of viral polypeptides in mammalian host cells. Preferably, the first or second most frequently used codons are employed for codon optimisation. Preferably, gene splicing by overlap extension or "gene SOEing" (supra) is employed for the construction of the synthetic polynucleotide which is a PCR-based method of recombining DNA sequences without reliance on restriction sites and of directly generating mutated DNA fragments in vitro. By modifying the sequences incorporated into the 5 '-ends of the primers, any pair of PCR products can be made to share a common sequence at one end. Under PCR conditions, the common sequence allows strands from two different fragments to hybridise to one another, forming an overlap. Extension of this overlap by DNA polymerase yields a recombinant molecule. However, a problem with long synthetic constructs is that mutations generally incorporate into amplified products during synthesis, hi this instance, it is preferred that resolvase treatment is employed at various steps of the synthesis. Resolvases are bacteriophage-encoded endonucleases which recognise disruptions or mispairing of double stranded DNA and are primarily used by bacteriophages to resolve Holliday junctions (Mizuuchi, 1982; Youil et al, 1995). For example, T7 endonuclease I can be employed in synthetic DNA constructions to recognise mutations and cleave corrupted dsDNA. The mutated DNA strands are then hybridised to non-mutant or correct DNA sequences, which results in a mispairing of DNA bases. The mispaired bases are recognised by the resolvase, which then cleaves the DNA nearby leaving only correctly hybridised sequences intact. Preferably a thermostable resolvase enzyme is employed during splicing or amplification so that errors are not incorporated in downstream synthesis products. Synthetic polynucleotides according to the invention can be operably linked to a regulatory polynucleotide in the form a synthetic construct as for example described in Section 2 supra. Synthetic constructs of the invention have utility inter alia as nucleic acid vaccines. The choice of regulatory polynucleotide and synthetic construct will depend on the intended host. Exemplary expression vectors for expression of a synthetic polypeptide according to the invention include, but are not restricted to, modified Ankara Vaccinia virus as for example described by Allen et al. (2000, J. Immunol. 164(9): 4968-4978), fowlpox virus as for example described by Boyle and Coupar (1988, Virus Res. 10: 343-356) and the herpes simplex amplicons described for example by Fong et al. in U.S. Patent No. 6,051,428. Alternatively, Adenovirus and Epstein-Barr virus vectors, which are preferably capable of accepting large amounts of DNA or RNA sequence information, can be used. Preferred promoter sequences that can be utilised for expression of synthetic polypeptides include the P7.5 or PE/L promoters as for example disclosed by Kumar and Boyle. (1990, Virology 179: 151-158), CMV and RSV promoters. The synthetic construct optionally further includes a nucleic acid sequence encoding an immunostimulatory molecule. The immunostimulatory molecule may be fusion partner of the synthetic polypeptide. Alternatively, the immunostimulatory molecule may be translated separately from the synthetic polypeptide. Preferably, the immunostimulatory molecule comprises a general immunostimulatory peptide sequence. For example, the immunostimulatory peptide sequence may comprise a domain of an invasin protein (Inv) from the bacteria Yersinia spp as for example disclosed by Brett et al (1993, Eur. J. Immunol. 23: 1608-1614). This immune stimulatory property results from the capability of this invasin domain to interact with the ^1 integrin molecules present on T cells, particularly activated immune or memory T cells. A preferred embodiment of the invasin domain (Inv) for linkage to a synthetic polypeptide has been previously described in U.S. Pat. No. 5,759,551. The said Inv domain has the sequence: Thr-Ala-Lys-Ser-Lys- Lys-Phe-Pro-Ser-Tyr-Thr-Ala-Thr-Tyr-Gln-Phe [SEQ ED NO; 1467] or is an immune stimulatory homologue thereof from the corresponding region in another Yersinia species invasin protein. Such homologues thus may contain substitutions, deletions or insertions of amino acid residues to accommodate strain to strain variation, provided that the homologues retain immune stimulatory properties. The general immunostimulatory sequence may optionally be linked to the synthetic polypeptide by a spacer sequence. hi an alternate embodiment, the immunostimulatory molecule may comprise an immunostimulatory membrane or soluble molecule, which is suitably a T cell co- stimulatory molecule. Preferably, the T cell co-stimulatory molecule is a B7 molecule or a biologically active fragment thereof, or a variant or derivative of these. The B7 molecule includes, but is not restricted to, B7-1 and B7-2. Preferably, the B7 molecule is B7-1. Alternatively, the T cell co-stimulatory molecule may be an ICAM molecule such as ICAM-1 and ICAM-2. In another embodiment, the immunostimulatory molecule can be a cytokine, which includes, but is not restricted to, an interleukin, a lymphokine, tumour necrosis factor and an interferon. Alternatively, the immunostimulatory molecule may comprise an immunomodulatory oligonucleotide as for example disclosed by Krieg in U.S. Patent No. 6,008,200. Suitably, the size of the synthetic polynucleotide does not exceed the ability of host cells to transcribe, translate or proteolytically process and present epitopes to the immune system. Practitioners in the art will also recognise that the size of the synthetic polynucleotide can impact on the capacity of an expression vector to express the synthetic polynucleotide in a host cell. In this connection, it is known that the efficacy of DNA vaccination reduces with expression vectors greater that 20-kb. In such situations it is preferred that a larger number of smaller synthetic constructs is utilised rather than a single large synthetic construct. 4. Immunopotentiating compositions The invention also contemplates a composition, comprising an immunopotentiating agent selected from the group consisting of a synthetic polypeptide as described in Section 2, and a synthetic polynucleotide or a synthetic construct as described in Section 3, together with a pharmaceutically acceptable carrier. One or more immunopotentiating agents can be used as actives in the preparation of immunopotentiating compositions. Such preparation uses routine methods known to persons skilled in the art. Typically, such compositions are prepared as injectables, either as liquid solutions or suspensions; solid forms suitable for solution in, or suspension in, liquid prior to injection may also be prepared. The preparation may also be emulsified. The active immunogenic ingredients are often mixed with excipients that are pharmaceutically acceptable and compatible with the active ingredient. Suitable excipients are, for example, water, saline, dextrose, glycerol, ethanol, or the like and combinations thereof. In addition, if desired, the vaccine may contain minor amounts of auxiliary substances such as wetting or emulsifying, agents, pH buffering agents, and/or adjuvants that enhance the effectiveness of the vaccine. Examples of adjuvants which may be effective include but are not limited to: aluminium hydroxide, N-acetyl-muramyl-L-threonyl-D-isoglutamine (thur-MDP), N- acetyl-nor-muramyl-L-alanyl-D-isoglutamine (CGP 11637, referred to as nor-MDP), N- acetylmuramyl-L-alanyl-D-isoglutaminyl-L-alanine-2-(l'-2'-dipalmitoyl-sn-glycero-3- hydroxyphosphoryloxy)-ethylamine (CGP 1983 A, referred to as MTP-PE), and RIB I, which contains three components extracted from bacteria, monophosphoryl lipid A, trehalose dimycolate and cell wall skeleton (MPL+TDM+CWS) in a 2% squalene/Tween 80 emulsion. For example, the effectiveness of an adjuvant may be determined by measuring the amount of antibodies resulting from the administration of the composition, wherein those antibodies are directed against one or more antigens presented by the treated cells of the composition. The immunopotentiating agents may be formulated into a composition as neutral or salt forms. Pharmaceutically acceptable salts include the acid addition salts (formed with free amino groups of the peptide) and which are formed with inorganic acids such as, for example, hydrochloric or phosphoric acids, or such organic acids such as acetic, oxalic, tartaric, maleic, and the like. Salts formed with the free carboxyl groups may also be derived from inorganic basis such as, for example, sodium, potassium, ammonium, calcium, or ferric hydroxides, and such organic basis as isopropylamine, trimethylamine, 2-ethylamino ethanol, histidine, procaine, and the like. If desired, devices or compositions containing the immunopotentiating agents suitable for sustained or intermittent release could be, in effect, implanted in the body or topically applied thereto for the relatively slow release of such materials into the body. The compositions are conventionally administered parenterally, by injection, for example, either subcutaneously or intramuscularly. Additional formulations which are suitable for other modes of administration inc 1- " ^ suppositories and, in some cases, oral formulations. For suppositories, traditional binders and carriers may include, for example, polyalkylene glycols or triglycerides; such suppositories may be formed from mixtures containing the active ingredient in the range of 0.5% to 10%, preferably l%-2%. Oral formulations include such normally employed excipients as, for example, pharmaceutical grades of mannitol, lactose, starch, magnesium carbonate, and the like. These compositions take the form of solutions, suspensions, tablets, pills, capsules, sustained release formulations or powders and contain 10%-95% of active ingredient, preferably 25%-70%. Administration of the gene therapy construct to said mammal, preferably a human, may include delivery via direct oral intake, systemic injection, or delivery to selected tissue(s) or cells, or indirectly via delivery to cells isolated from the mammal or a compatible donor. An example of the latter approach would be stem cell therapy, wherein isolated stem cells having potential for growth and differentiation are transfected with the vector comprising the Soxl8 nucleic acid. The stem cells are cultured for a period and then transferred to the mammal being treated. With regard to nucleic acid based compositions, all modes of delivery of such compositions are contemplated by the present invention. Delivery of these compositions to cells or tissues of an animal may be facilitated by microprojectile bombardment, liposome mediated transfection (e.g., lipofectin or lipofectamine), electroporation, calcium phosphate or DEAE-dextran-mediated transfection, for example. In an alternate embodiment, a synthetic construct may be used as a therapeutic or prophylactic composition in the form of a "naked DNA" composition as is known in the art. A discussion of suitable delivery methods may be found in Chapter 9 of CURRENT PROTOCOLS EST MOLECULAR BIOLOGY (Eds. Ausubel et al; John Wiley & Sons Inc., 1997 Edition) or on the Internet site DNAvaccine.com. The compositions may be administered by intradermal (e.g., using panjet™ delivery) or intramuscular routes. The step of introducing the synthetic polynucleotide into a target cell will differ depending on the intended use and species, and can involve one or more of non- viral and viral vectors, cationic liposomes, retroviruses, and adenoviruses such as, for example, described in Mulligan, R.C., (1993 Science 260 926-932) which is hereby incorporated by reference. Such methods can include, for example: A. Local application of the synthetic polynucleotide by injection (Wolff et al, 1990, Science 247 1465-1468, which is hereby incorporated by reference), surgical implantation, instillation or any other means. This method can also be used in combination with local application by injection, surgical implantation, instillation or any other means, of cells responsive to the protein encoded by the synthetic polynucleotide so as to increase the effectiveness of that treatment. This method can also be used in combination with local application by injection, surgical implantation, instillation or any other means, of another factor or factors required for the activity of said protein. B. General systemic delivery by injection of DNA, (Calabretta et al, 1993, Cancer Treat. Rev. 19 169-179, which is incorporated herein by reference), or RNA, alone or in combination with liposomes (Zhu et al, 1993, Science 261 209-212, which is incorporated herein by reference), viral capsids or nanoparticles (Bertling et al, 1991, Biotech. Appl. Biochem. 13 390-405, which is incorporated herein by reference) or any other mediator of delivery. Improved targeting might be achieved by linking the synthetic polynucleotide to a targeting molecule (the so-called "magic bullet" approach employing, for example, an antibody), or by local application by injection, surgical implantation or any other means, of another factor or factors required for the activity of the protein encoding said synthetic polynucleotide , or of cells responsive to said protein. C. Injection or implantation or delivery by any means, of cells that have been modified ex vivo by transfection (for example, in the presence of calcium phosphate: Chen et al, 1987, Mole. Cell Biochem. 1 2745-2752, or of cationic lipids and polyamines: Rose et al, 1991, BioTech. 10 520-525, which articles are incorporated herein by reference), infection, injection, electroporation (Shigekawa et al, 1988, BioTech. 6 742-751, which is incorporated herein by reference) or any other way so as to increase the expression of said synthetic polynucleotide in those cells. The modification can be mediated by plasmid, bacteriophage, cosmid, viral (such as adenoviral or retroviral; Mulligan, 1993, Science 260 926-932; Miller, 1992, Nature 357 455-460; Salmons et al, 1993, Hum. Gen. Ther. 4 129-141, which articles are incorporated herein by reference) or other vectors, or other agents of modification such as liposomes (Zhu et al, 1993, Science 261 209-212, which is incorporated herein by reference), viral capsids or nanoparticles (Bertling et al, 1991, Biotech. Appl. Biochem. 13 390-405, which is incorporated herein by reference), or any other mediator of modification. The use of cells as a delivery vehicle for genes or gene products has been described by Barr et al, 1991, Science 254 1507-1512 and by Dhawan et al, 1991, Science 254 1509- 1512, which articles are incorporated herein by reference. Treated cells can be delivered in combination with any nutrient, growth factor, matrix or other agent that will promote their survival in the treated subject. Also encapsulated by the present invention is a method for treatment and/or prophylaxis of a disease or condition, comprising administering to a patient in need of such treatment a therapeutically effective amount of a composition as broadly described above. The disease or condition may be caused by a pathogenic organism or a cancer as for example described above. In a preferred embodiment, the immunopotentiating composition of the invention is suitable for treatment of, or prophylaxis against, a cancer. Cancers which could be suitably treated in accordance with the practices of this invention include cancers of the lung, breast, ovary, cervix, colon, head and neck, pancreas, prostate, stomach, bladder, kidney, bone liver, oesophagus, brain, testicle, uterus, melanoma and the various leukemias and lymphomas. In an alternate embodiment, the immunopotentiating composition is suitable for treatment of, or prophylaxis against, a viral, bacterial or parasitic infection. Viral infections contemplated by the present invention include, but are not restricted to, infections caused by HJV, Hepatitis, Influenza, Japanese encephalitis virus, Epstein-Barr virus and respiratory syncytial virus. Bacterial infections include, but are not restricted to, those caused by Neisseria species, Meningococcal species, Haemophilus species Salmonella species, Streptococcal species, Legionella species and Mycobacterium species. Parasitic infections encompassed by the invention include, but are not restricted to, those caused by Plasmodium species, Schistosoma species, Leishmania species, Trypanosoma species, Toxoplasma species and Giardia species. The above compositions or vaccines may be administered in a manner compatible with the dosage formulation, and in such amount as is therapeutically effective to alleviate patients from the disease or condition or as is prophylactically effective to prevent incidence of the disease or condition in the patient. The dose administered to a patient, in the context of the present invention, should be sufficient to effect a beneficial response in a patient over time such as a reduction or cessation of blood loss. The quantity of the composition or vaccine to be administered may depend on the subject to be treated inclusive of the age, sex, weight and general health condition thereof. In this regard, precise amounts of the composition or vaccine for administration will depend on the judgement of the practitioner. In determining the effective amount of the composition or vaccine to be administered in the treatment of a disease or condition, the physician may evaluate the progression of the disease or condition over time. In any event, those of skill in the art may readily determine suitable dosages of the composition or vaccine of the invention. hi a preferred embodiment, DNA-based immunopotentiating agent (e.g., 100 μg) is delivered intradermally into a patient at day 1 and at week 8 to prime the patient. A recombinant poxvirus (e.g., at 10 7 pfu/mL) from which substantially the same immunopotentiating agent can be expressed is then delivered intradermally as a booster at weeks 16 and 24, respectively. The effectiveness of the immunisation may be assessed using any suitable technique. For example, CTL lysis assays may be employed using stimulated splenocytes or peripheral blood mononuclear cells (PBMC) on peptide coated or recombinant virus infected cells using 51 Cr labelled target cells. Such assays can be performed using for example primate, mouse or human cells (Allen et al, 2000, J Immunol. 164(9): 4968-4978 also Woodberry et al, infra). Alternatively, the efficacy of the immunisation may be monitored using one or more techniques including, but not limited to, HLA class I Tetramer staining - of both fresh and stimulated PBMCs (see for example Allen et al, supra), proliferation assays (Allen et al, supra), Elispot™ Assays and intracellular INF- ga ma staining (Allen et al, supra), ELISA Assays - for linear B cell responses; and Western blots of cell sample expressing the synthetic polynucleotides. 5. Computer related embodiments The design or construction of a synthetic polypeptide sequence or a synthetic polynucleotide sequence according to the invention is suitably facilitated with the assistance of a computer programmed with software, which inter alia fragments a parent sequence into fragments, and which links those fragments together in a different relationship relative to their linkage in the parent sequence. The ready use of a parent sequence for the construction of a desired synthetic molecule according to the invention requires that it be stored in a computer-readable format. Thus, in accordance with the present invention, sequence data relating to a parent molecule (e.g., a parent polypeptide) is stored in a machine-readable storage medium, which is capable of processing the data to fragment the sequence of the parent molecule into fragments and to link together the fragments in a different relationship relative to their linkage in the parent molecule. Therefore, another embodiment of the present invention provides a machine- readable data storage medium, comprising a data storage material encoded with machine readable data which, when used by a machine programmed with instructions for using said data, fragments a parent sequence into fragments, and links those fragments together in a different relationship relative to their linkage in the parent sequence. In a preferred embodiment of this type, a machine-readable data storage medium is provided that is capable of reverse translating the sequence of a respective fragment to provide a nucleic acid sequence encoding the fragment and to link together in the same reading frame each of the nucleic acid sequences to provide a polynucleotide sequence that codes for a polypeptide sequence in which said fragments are linked together in a different relationship relative to their linkage in a parent polypeptide sequence. In another embodiment, the invention encompasses a computer for designing the sequence of a synthetic polypeptide and/or a synthetic polynucleotide of the invention, wherein the computer comprises wherein said computer comprises: (a) a machine readable data storage medium comprising a data storage material encoded with machine readable data, wherein said machine readable data comprises the sequence of a parent polypeptide; (b) a working memory for storing instructions for processing said machine-readable data; - Ill - (c) a central-processing unit coupled to said working memory and to said machine-readable data storage medium, for processing said machine-readable data into said synthetic polypeptide sequence and/or said synthetic polynucleotide; and (d) an output hardware coupled to said central processing unit, for receiving said synthetic polypeptide sequence and/or said synthetic polynucleotide. hi yet another embodiment, the invention contemplates a computer program product for designing the sequence of a synthetic polynucleotide of the invention, comprising code that receives as input the sequence of a parent polypeptide, code that fragments the sequence of the parent polypeptide into fragments, code that reverse translates the sequence of a respective fragment to provide a nucleic acid sequence encoding the fragment, code that links together in the same reading frame each said nucleic acid sequence to provide a polynucleotide sequence that codes for a polypeptide sequence in which said fragments are linked together in a different relationship relative to their linkage in the parent polypeptide sequence, and a computer readable medium that stores the codes. A version of these embodiments is presented in Figure 23, which shows a system 10 including a computer 11 comprising a central processing unit ("CPU") 20, a working memory 22 which may be, e.g., RAM (random- access memory) or "core" memory, mass storage memory 24 (such as one or more disk drives or CD-ROM drives), one or more cathode-ray tube ("CRT") display terminals 26, one or more keyboards 28, one or more input lines 30, and one or more output lines 40, all of which are interconnected by a conventional bidirectional system bus 50. Input hardware 36, coupled to computer 11 by input lines 30, may be implemented in a variety of ways. For example, machine-readable data of this invention may be inputted via the use of a modem or modems 32 connected by a telephone line or dedicated data line 34. Alternatively or additionally, the input hardware 36 may comprise CD. Alternatively, ROM drives or disk drives 24 in conjunction with display terminal 26, keyboard 28 may also be used as an input device. Output hardware 46, coupled to computer 11 by output lines 40, may similarly be implemented by conventional devices. By way of example, output hardware 46 may include CRT display terminal 26 for displaying a synthetic polynucleotide sequence or a synthetic polypeptide sequence as described herein. Output hardware might also include a printer 42, so that hard copy output may be produced, or a disk drive 24, to store system output for later use. In operation, CPU 20 coordinates the use of the various input and output devices 36,46 coordinates data accesses from mass storage 24 and accesses to and from working memory 22, and determines the sequence of data processing steps. A number of programs may be used to process the machine readable data of this invention. Exemplary programs may use for example the steps outlined in the flow diagram illustrated in Figure 24. Broadly, these steps include (1) inputting at least one parent polypeptide sequence; (2) optionally adding to alanine spacers at the ends of each polypeptide sequence; (3) fragmenting the polypeptide sequences into fragments (e.g., 30 amino acids long), which are preferably overlapping (e.g., by 15 amino acids); (4) reverse translating the fragment to provide a nucleic acid sequence for each fragment and preferably using for the reverse translation first and second most translationally efficient codons for a cell type, wherein the codons are preferably alternated out of frame with each other in the overlaps of consecutive fragments; (5) randomly rearranging the fragments; (6) checking whether rearranged fragments recreate at least a portion of a parent polypeptide sequence; (7) repeating randomly rearranging the fragments when rearranged fragments recreate said at least a portion; or otherwise (8) linking the rearranged fragments together to produce a synthetic polypeptide sequence and/or a synthetic polynucleotide sequence; and (9) outputting said synthetic polypeptide sequence and/or a synthetic polynucleotide sequence. An example of an algorithm which uses inter alia the aforementioned steps is shown in Figure 25. By way of example, this algorithm has been used for the design of synthetic polynucleotides and synthetic polypeptides according to the present invention for Hepatitis C la and for melanoma, as illustrated in Figures 26 and 27. Figure 28 shows a cross section of a magnetic data storage medium 100 which can be encoded with machine readable data, or set of instructions, for designing a synthetic molecule of the invention, which can be carried out by a system such as system 10 of Figure 23. Medium 100 can be a conventional floppy diskette or hard disk, having a suitable substrate 101, which may be conventional, and a suitable coating 102, which may be conventional, on one or both sides, containing magnetic domains (not visible) whose polarity or orientation can be altered magnetically. Medium 100 may also have an opening (not shown) for receiving the spindle of a disk drive or other data storage device 24. The magnetic domains of coating 102 of medium 100 are polarised or oriented so as to encode in manner which may be conventional, machine readable data such as that described herein, for execution by a system such as system 10 of Figure 23. Figure 29 shows a cross section of an optically readable data storage medium 110 which also can be encoded with such a machine-readable data, or set of instructions, for designing a synthetic molecule of the invention, which can be carried out by a system such as system 10 of Figure 23. Medium 110 can be a conventional compact disk read only memory (CD-ROM) or a rewritable medium such as a magneto-optical disk, which is optically readable and magneto-optically writable. Medium 100 preferably has a suitable substrate 111, which may be conventional, and a suitable coating 112, which may be conventional, usually of one side of substrate 111. In the case of CD-ROM, as is well known, coating 112 is reflective and is impressed with a plurality of pits 113 to encode the machine-readable data. The arrangement of pits is read by reflecting laser light off the surface of coating 112. A protective coating 114, which preferably is substantially transparent, is provided on top of coating 112. In the case of a magneto-optical disk, as is well known, coating 112 has no pits 113, but has a plurality of magnetic domains whose polarity or orientation can be changed magnetically when heated above a certain temperature, as by a laser (not shown). The orientation of the domains can be read by measuring the polarisation of laser light reflected from coating 112. The arrangement of the domains encodes the data as described above. In order that the invention may be readily understood and put into practical effect, particular preferred non-limiting embodiments will now be described as follows. EXAMPLES EXAMPLE 1 Preparation of an HIV Savine Experimental Protocol Plasmids The plasmid pDNAVacc is ampicillin resistant and contains an expression cassette comprising a CMV promoter and enhancer, a synthetic intron, a multiple cloning site (MCS) and a SV40poly A signal sequence (Thomson et al, 1998). The plasmid pTK7.5 and contains a selection cassette, a pox virus 7.5 early/late promoter and a MCS flanked on either side by Vaccinia virus TK gene sequences. Recombinant Vaccinia Viruses Recombinant Vaccinia viruses expressing the gag, env (IEB) and pol (LAI) genes of HJV-l were used as previously described and denoted VV-GAG, VV-POL, VV-ENV (Woodberry et al, 1999; Kent et al, 1998). Marker Rescue Recombination Recombinant Vaccinia viruses containing Savine constructs were generated by marker rescue recombination, using protocols described previously (Boyle et al, 1985). Plaque purified viruses were tested for the TK phenotype and for the appropriate genome arrangement by Southern blot and PCR. Oligonucleotides Oligonucleotides 50 nmol scale and desalted were purchased from Life Technologies. Short oligonucleotides were resuspended in 100 μL of water, their concentration determined, then diluted to 20 μM for use in PCR or sequencing reactions. Long oligonucleotides for splicing reactions were denatured for 5 minutes at 94°C in 20 μL of formamide loading buffer then 0.5 μL gel purified on a 6% polyacrylamide gel. Gel slices containing full-length oligonucleotides were visualised with ethidium bromide, excised, placed in Eppendorf™ tubes, combined with 200 μL of water before being crushed using the plunger of a 1 mL syringe. Before being used in splicing reactions the crushed gel was resuspended in an appropriate volume of buffer and 1-2 μL of the resuspendate used directly in the splicing reactions. Sequencing Sequencing was performed using Dye terminator sequencing reactions and analyzed by the Biomedical Resource Facility at the John Curtin School of Medical Research using an ABI automated sequencer. Restimulation of Lymphocytes from HIV Infected Patients Two pools of recombinant Vaccinia viruses containing W-AC1 + VV-BC1 (Pool 1) or VV-AC2 + VV-BC2 + W-CC2 (Pool 2) were used to restimulate lymphocytes from the blood samples of HJV-infected patients. Briefly CTL lines were generated from HIV- infected donor PBMC. A fifth of the total PBMC were infected with either Pool 1 or Pool 2 Vaccinia viruses then added back to the original cell suspension. The infected cell suspension was then cultured with IL-7 for 1 week. CTL Assays Restimulated PBMCs were used as effectors in a standard 51 Cr-release CTL assay. Targets were autologous EBV-transformed lymphoblastoid cell lines (LCLs) infected with the following viruses : Pool 1, Pool 2,W-GAG, VV-POL or VV-ENV. Assay controls included uninfected targets, targets infected with VV-lacZ (virus control) and K562 cells. Results HIV Savine Design A main goal of the Savine strategy is to include as much protein sequence information from a pathogen or cancer as possible in such a way that potential T cell epitopes remain intact and so that the vaccine or therapy is extremely safe. An HIV Savine is described herein not only to compare this strategy to other strategies but also, to produce an HIV vaccine that would provide the maximum possible population coverage as well as catering for the major HIV clades. A number of design criteria was first determined to exploit the many advantages of using a synthetic approach. One advantage is that it is possible to use consensus protein sequences to design these vaccines. Using consensus sequences for a highly variable virus like HJV should provide better vaccine coverage because individual viral isolate sequences may have lost epitopes which induce CTL against the majority of other viral isolates. Thus, using the ' consensus sequences of each HIV clade rather than individual isolate sequences should provide better vaccine coverage. Taking this one step further, a consensus sequence that covers all HIV clades should theoretically provide better coverage than using just the consensus sequences for individual clades. Before designing such a sequence however, it was decided that a more appropriate and focussed HJV vaccine might be constructed if the various clades were first ranked according to their relative importance. To establish such a ranking the following issues were considered, current prevalence of each clade, the rate at which each clade is increasing and the capacity of various regions of the world to cope with the HIV pandemic (Figures 1 and 2). These criteria produced the following ranking, Clade E > clade A > clade C > clade B > clade D > other clades. Clades E and A were considered to almost equal since they are very similar except in their envelope protein sequences, which differ considerably. Another advantage of synthesising a designed sequence is that it is possible to incorporate degenerate sequences into their design. In the case of HJV, this means that more than one amino acid can be included at various positions to improve the ability of the vaccine to cater for the various HIV clades and isolates. Coverage is improved because mutations in different HJV clades and also in individual isolate sequences, while mostly destroying specific T cell epitopes, can result in the formation of new potentially useful epitopes nearby (Goulder et al, 1997). Incorporating degenerate amino acid sequences, however, also means that more than one construct must be made and mixed together. The number of constructs required depends on the frequency with which mutations are incorporated into the design. While this approach requires the construction of additional constructs, these constructs can be prepared from the same set of degenerate long oligonucleotides, significantly reducing the cost of providing such considerable interclade coverage. A set of degeneracy rules was developed for the incorporation of amino acid mutations into the design which meant that a maximum of eight constructs would be required so that theoretically all combinations were present, as follows: 1) Two amino acids at three positions (or less) within any group of nine amino acids (i.e., present in a CTL epitope); 2) Three amino acids at one position and two at another (or not) within any group of nine amino acids; 3) Four amino acids at one position and two at another (or not) within any group of nine amino acids. The reason why these rules were applied to nine amino acids (the average CTL epitope size) and not to larger stretches of amino acid sequence to cater for class II restricted epitopes, is because class H-restricted epitopes generally have a core sequence of nine amino acids in the middle which bind specifically to class II MHC molecules with the extra flanking sequences stabilising binding, by associating with either side of class II MHC antigens in a largely sequence independent manner (Brown et al, 1993). Using the HIV clade ranking described above, the amino acid degeneracy rules and in some situations the similarity between amino acids, a degenerate consensus protein sequence was designed for each HJV protein using the consensus protein sequences for each HIV clade compiled by the Los Alamos HJV sequence database (Figures 3-11) (HIV Molecular Immunology Database, 1997). It is important to note that in some situations the order with which each of the above design criteria was applied was altered. Each time this was done the primary goal however was to increase the ability of the Savine to cater for interclade differences. Two isolate sequences, GenBank accession U51189 and U46016, for clade E and clade C, respectively, were used when a consensus sequence for some HJV proteins from these two clades was unavailable (Gao et al, 1996; Salminen et al, 1996). The design of a consensus sequence for the hypervariable regions of the HTV envelope protein and in some cases between these regions (hypervariable regions 1-2 and 3-5) was difficult and so these regions were excluded from the vaccine design. Once a degenerate consensus sequence was designed for each HIV protein, an approach was then determined for incorporating all the protein sequences safely into the vaccine. One convenient approach to ensure that a vaccine will be safe is to systematically fragment and randomly rearrange the protein sequences together thus abrogating or otherwise altering their structure and function. The protein sequences still have to be immunologically functional however, meaning that the process used to fragment the sequences should not destroy potential epitopes. To decide on the best approach for systematically fragmenting protein sequences, the main criteria used was the size of T epitopes and their processing requirements. Class I-restricted T cell epitopes are 8-10 amino acids long and generally require 2-3 natural flanking amino acids to ensure their efficient processing and presentation if placed next to unnatural flanking residues (Del Val et al, 1991; Thomson et al, 1995). Class H-restricted T cell epitopes range between 12-25 amino acids long and do appear to require natural flanking residues for processing however, it is difficult to rule out a role for natural flanking residues in all cases due to the complexity of their processing pathways (Thomson et al, 1998). Also class Il-resrricted epitopes despite being larger than CTL epitopes generally have a core sequence of 9-10 amino acids, which binds to MHC molecules in a sequence specific fashion. Thus, based on current knowledge, it was decided that an advantageous approach was to overlap the fragments by at least 15 amino acids to ensure that potential epitopes which might lie across fragment boundaries are not lost and to ensure that CTL epitopes near fragment boundaries, that are placed beside or near inhibitory amino acids in adjacent fragments, are processed efficiently. In deciding the optimal fragment size, the main criteria used were that size had to be small enough to cause the maximum disruption to the structure and function of proteins but large enough to cover the sequence information as efficiently as possible without any further unnecessary duplication. Based on these criteria the fragments would be twice the overlap size, in this case 30 amino acids long. The designed degenerate protein sequences were then separated into fragments 30 amino acid long and overlapping by fifteen amino acids. Two alanine amino acids were also added to the start and end of the first and last fragment for each protein or envelop protein segment to ensure these fragments were not placed directly adjacent to amino acids capable of blocking epitope processing (Del Val et al, 1991). The next step was to reverse translate each protein sequence back into DNA. Duplicating DNA sequences was avoided when constructing DNA sequences encoding a tandem repeat of identical or homologous amino acid sequences to maximise expression of the Savine. In this regard, the first and second most commonly used mammalian codons (shown in Figure 12) were assigned to amino acids in these repeat regions, wherein a first codon was used to encode an amino acid in one of the repeated sequences and wherein a second but synonymous codon was used for the other repeated sequence (e.g., see the gag HJV protein in Figure 13). To cater for the designed amino acid mutations more than one base was assigned to some positions using the IUPAC DNA codes without exceeding more than three base variations (eight possible combinations) in any group of 27 bases (Figure 12). Where a particular combination of amino acids could not be incoφorated, because too many degenerate bases would be required, some or all of the amino acid degeneracy was removed according to the protein consensus design rules outlined above. Also the degenerate codons were checked to determine if they could encode a stop codon, if stop codons could not be avoided then the amino acid degeneracy was also simplified again according to the protein consensus design rules outlined above. The designed DNA segments were then scrambled randomly and joined to create twenty-two subcassettes approximately 840 bp in size. Extra DNA sequences incorporating sites for one of the cohesive restriction enzymes Xbal, Spel, Avrϋ or el and 3 additional base pairs (to cater for premature Taq polymerase termination) were then added to each end of each subcassette (Figure 14). Some of these extra DNA sequences also contained, the cohesive restriction sites for Sail or Xhol, Kozak signal sequences and start or stop codons to enable the subcassettes to be joined and expressed either as three large cassettes or one full length protein (Figures 14 and 15). hi designing the HJV Savine one issue that required investigation was whether such a large DNA molecule would be fully expressed and whether epitopes encoded near the end of the molecule would be efficiently presented to the immune system. The inventors also wished to show that mixing two or more degenerate Savine constructs together could induce T cell responses that recognise mutated sequences. To examine both issues DNA coding for a degenerate murine influenza nucleoprotein CTL epitope, NP365- 373, which differs by two amino acids at positions 71 and 72 in influenza strain A/PR/8/34 compared to the A/NT/60/68strain and restricted by H2-Db, was inserted before the last stop codon at the end of the HIV Savine design (Figure 15). An important and unusual characteristic of both of these naturally occurring NP365-373 sequences, which enabled the present inventors to examine the effectiveness of incorporating mutated sequences, is that they generate CTL responses which do not cross react with the alternate sequence (Townsend et. al, 1986). This is an unusual characteristic because epitopes not destroyed by mutation usually induce CTL responses that cross-react. Up to ten long oligonucleotides up to 100 bases long and two short amplification oligonucleotides were synthesised to enable construction of each subcassette (Life Technologies). In designing each oligonucleotide the 3' end and in most cases also the 5' end had to be either a 'c' or a 'g' to ensure efficient extension during PCR splicing. The overlap region for each long oligonucleotide was designed to be at least 16 bp with approximately 50% G/C content. Also oligonucleotide overlaps were not placed where degenerate DNA bases coded for degenerate amino acids to avoid splicing difficulties later. Where this was too difficult some degenerate bases were removed according to the protein consensus design rules outlined above and indicated in Figure 12. Figure 16 shows an example of the oligonucleotides design for each subcassette. Construction of the HIV Savine Five of each group of ten designed oligonucleotides were spliced together using stepwise asymmetric PCR (Sandhu et al, 1992) and Splicing by Overlap Extension (SOEing) (Figure 17a). Each subcassette was then PCR amplified, cloned into pBluescript™ π KS " using BamHI/EcoRI and 16 individual clones sequenced. Mutations, deletions and insertions were present in the large majority of the clones for each subcassette, despite acrylamide gel purification of the long oligonucleotides. In order to construct a functional Savine with minimal mutations, two clones for each subcassette with no insertions or deletions and hence a complete open reading frame and with minimal numbers of non-designed mutations, were selected from the sixteen available. The subcassettes were then excised from their plasmids and joined by stepwise PCR-amplified ligation using the polymerase blend Elongase™ (Life Technology), T4 DNA ligase and the cohesive restriction enzymes Xball Spell AvrWNhel, to generate two copies of cassettes A, B and C as outlined in Figure 14 and shown in Figure 17b. Predicted sequences for these cassettes are shown in Figure 30. Each cassette was then reamplified by PCR with Elongase™, cloned into pBluescript™ H KS" and 3 of the resulting plasmid clones sequenced using 12 of the 36 sequencing primers designed to cover the full length construct. Clones with minimal or no further mutations were selected for transfer into plasmids for DNA vaccination or used to make recombinant poxviruses. A summary of the number of designed and non-designed mutations in each Savine construct is presented in Table 1. TABLE 1 Summary of mutations Summary of the mutations present in the two full-length clones constructed as determined by sequencing. Includes the number of mutations designed, expected and actually present in the 2 clones and the number of non-designed mutations in each cassette and full-length clone. HIV Savine DNA vaccines and Recombinant Vaccinia viruses To test the immunological effectiveness of the HIV Savine constructs the cassette sequences were transferred into DNA vaccine and poxvirus vectors. These vectors when used either separately in immunological assays described below or together in a 'prime- boost' protocol which has been shown previously to generate strong T cell responses in vivo (Kent et al, 1997). DNA Vaccination plasmids were constructed by excising the cassettes from the selected plasmid clones with XbaUXhol (cassette A) or XballSaR (cassettes B and C) and ligating them into pDNAVacc cut with XbaUXhol to create pD VAC 1 , pDVAC2, pDVBC 1 , pDVBC2, pDVCCl, pDVCC2, respectively (Figure 18a). These plasmids were then further modified by cloning into their Xbάl site a DNA fragment excised using XbaJIAvrU from pTUMERA2 and encoding a synthetic endoplasmic reticulum (ER) signal sequence from the Adenovirus El A protein (Persson et al, 1980) (Figure 18a). ER signal sequences have been shown previously to enhance the presentation of both CTL and T helper epitopes in vivo (Ishioka, G.Y., 1999; Thomson et al, 1998). The plasmids pDVERACl, pDVERBCl, pDVERCCl andpDVERAC2, pDVERBC2, pDVERCC2 were then mixed together to create, plasmid pool 1 and pool 2 respectively. Each plasmid pool collectively encodes one copy of the designed full-length HJV Savine. Plasmids to generate recombinant Vaccinia viruses which express HIV Savine sequences were constructed by excising the various HJV Savine cassettes from the selected plasmid clones using BamUJJXhoI (cassette A) or BamHl/Sall (cassettes B and C) and cloned into the marker rescue plasmid, pTK7.5, cleaved with BamFUlSaU. These pTK7.5- derived plasmids were then used to generate recombinant Vaccinia viruses by marker rescue recombination using established protocols (Boyle et al, 1985) to generate VV-AC1, W-AC2, W-BC1, W-BC2, VV-CC1 and W-CC2 (Figure 18b). Two further DNA vaccine plasmids were constructed each encoding a version of the full length HIV Savine (Figure 18c). Briefly, the two versions of cassette B were excised with Xhol and cloned into the corresponding selected plasmid clones containing cassette A sequences that were cut with XhollSaH to generate pBSABl and pBSAB2 respectively. The joined A/B cassettes in pBSABl and pBSAB2 were excised with XbaUXhol and cloned into pDVCCl and pDVCC2, respectively, and cleaved with XbaVXhoJ to generate pDVFLl and pDVFL2. These were then further modified to contain an ER signal sequence using the same cloning strategy as outlined in figure 18 a. Restimulation of HIV specific lymphocytes from HIV infected patients The present inventors examined the capacity of the HIV Savine to restimulate HIV-specific polyclonal CTL responses from HIV-infected patients. PBMCs from three different patients were restimulated in vitro with two HIV Savine Vaccinia virus pools (Pool 1 included VV-AC1 andVV-BCl; Pool 2 included W-AC2, W-BC2 and VV-CC2) then used in CTL lysis assays against LCLs infected either with one of the Savine Vaccinia virus pools or Vaccinia viruses which express gag, env or pol. Figure 19 clearly shows, that in all three assays, both HIV Savine viral pools restimulated HIV-specific CTL responses which could recognise targets expressing whole natural HIV antigens and not targets which were uninfected or infected with the control Vaccinia virus. Furthermore, in all three cases, both pools restimulated responses that recognised all three natural HIV antigens. This result suggests that the combined Savine constructs will provide broader immunological coverage than single antigen based vaccine approaches. The level of lysis in each case of targets infected with Savine viral pools was significantly higher than the lysis recorded for any other infected target. This probably reflects the combined CTL responses to gag, pol, and env plus other HIV antigens not analysed here but whose sequences are also incorporated into the Savine constructs. CTL recognition of each HIV antigen is largely controlled by each patient's HLA background hence the pattern of CTL lysis for whole HJV antigens is different in each patient. Interestingly, this CTL lysis pattern did not change when the second Savine Vaccinia virus pool was used for CTL restimulation. In these assays, therefore, the inventors were unable to demonstrate clear differences between pools 1 and 2, despite pool 1 lacking a Vaccinia virus expressing cassette CC1 and despite the many amino acid differences between the A and B cassettes in each pool (see table 1). From the foregoing, the present inventors have developed a novel vaccine/therapeutic strategy. In one embodiment, pathogen or cancer protein sequences are systemically fragmented, reverse translated back into DNA, rearranged randomly then joined back together. The designed synthetic DNA sequence is then constructed using long oligonucleotides and can be transferred into a range of delivery vectors. The vaccine vectors used here were DNA vaccine plasmids and recombinant poxvirus vectors which have been previously shown to elicit strong T cell responses when used together in a 'prime-boost' protocol (Kent et al, 1997). An important advantage of scrambled antigen vaccines or 'Savines' is that the amount of starting sequence information for the design can be easily expanded to include the majority of the protein sequences from a pathogen or for cancer, thereby providing the maximum possible vaccine or therapy coverage for a given population. An embodiment of the systematic fragmentation approach described herein was based on the size and processing requirements for T cell epitopes and was designed to cause maximal disruption to the structure and function of protein sequences. This fragmentation approach ensures that the maximum possible range of T cell epitopes will be present from any incorporated protein sequence without the protein being functional and able to compromise vaccine safety Another important advantage of Savines is that consensus protein sequences can be used for their design. This feature is only applicable when the design needs to cater for pathogen or cancer antigens whose sequence varies considerably. HIV is a highly mutagenic virus, hence this feature was utilised extensively to design a vaccine which has the potential to cover not only field isolates of HJV but also the major HJV clades involved in the current HJV pandemic. To construct the HIV Savine, one set of long oligonucleotides was synthesised, which included degenerate bases in such a way that 8 constructs are theoretically required for the vaccine to contain all combinations in any stretch of 9 amino acids. The inventors believe that this approach can be improved for the following reasons: 1) While degenerate bases should be theoretically equally represented, in practice some degenerate bases were biased towards one base or the other, leading to a lower than expected frequency of the designed mutations in the two full length HJV Savines which were constructed (see Table 1). 2) Only sequence combinations actually present in the HJV clade consensus sequences are required to get full clade coverage, hence the number of full length constructs needed could be reduced. To reduce the number of constructs however, separate sets of long oligonucleotides would have to be synthesised, significantly increasing the cost, time and effort required to generate a vaccine capable of such considerable vaccine coverage. A significant problem during the construction of the HJV Savine synthetic DNA sequence was the incorporation of non-designed mutations. The most serious types of mutations were insertions, deletions or those giving rise to stop codons, all of which change the frame of the synthesised sequences and/or caused premature truncation of the Savine proteins. These types of mutation were removed during construction of the HIV Savines by sequencing multiple clones after subcassette and cassette construction and selecting functional clones. The major source of these non-designed mutations was in the long oligonucleotides used for Savine synthesis, despite their gel purification. This problem could be reduced by making the initial subcassettes smaller thereby reducing the possibility of corrupted oligonucleotides being incorporated into each subcassette clone. The second major cause of non-designed mutations was the large number of PCR cycles required for the PCR and ligation-mediated joining of the subcassettes. Including extra sequencing and clone selection steps during the subcassette joining process should help to reduce the frequency of non-designed mutations in future constructs. Finally, another method that could help reduce the frequency of such mutations at all stages is to use resolvase treatment. Resolvases are bacteriophage-encoded endonucleases which recognise disruptions to double stranded DNA and are primarily used by bacteriophages to resolve Holliday junctions (Mizuuchi, 1982; Youil et al, 1995). T7 endonuclease I has already been used by the present inventors in synthetic DNA constructions to recognise mutations and cleave corrupted dsDNA to allow gel purification of correct sequences. Cleavage of corrupted sequences occurs because after a simple denaturing and hybridisation step mutated DNA hybridises to correct DNA sequences and results in a mispairing of DNA bases which is able to be recognised by the resolvase. This method resulted in a 50% reduction in the frequency of errors. Further optimisation of this method and the use of a thermostable version of this type of enzyme could further reduce the frequency of errors during long Savine construction. Two pools of Vaccinia viruses expressing Savine cassettes were both shown to restimulate HJV-specific responses from three different patients infected with B clade HJV viruses. These results provide a clear indication that the HJV Savine should provide broad coverage of the population because each patient had a different HLA pattern yet both pools were able to restimulate HJV-specific CTL responses in all three patients against all three natural HIV proteins tested. Also, both pools were shown to restimulate virtually identical CTL patterns in all three patients. This result was unexpected because some responses should have been lost or gained due to the amino acid differences between the two pools and because Pool 1 is only capable of expressing 2/3 of the full length HIV Savine. There are two suggested reasons why the pattern of CTL lysis was not altered between the two viral pools. Firstly, the sequences in the Savine constructs are nearly all duplicated because the fragment sequences overlap. Hence the loss of a third of the Savine may not have excluded sufficient T cell epitopes for differences to be detected in only three patient samples against only three HIV proteins. Secondly, while mutations often destroy T cell epitopes, if they remain functional, then the CTL they generate frequently can recognise alternate epitope sequences. Taken together this finding indirectly suggests that combining only two Savine constructs may provide robust multiclade coverage. Further experiments are being carried out to directly examine the capacity of the HJV Savine to stimulate CTL generated by different strains of HJV virus. The capacity of the two HIV-1 Savine Vaccinia vector pools to stimulate CD4+ T cell HJV-l specific responses from infected patients was also tested (Figure 20). Both patients showed significant proliferation of CD4+ T cells although both pools did not show consistent patterns suggesting that the two pools may provide wider vaccine coverage than using either pool independently. The present inventors have generated a novel vaccine strategy, which has been used to generate what the inventors believe to be the most effective HIV candidate vaccine to date. The inventors have used this vaccine to immunise naive mice. Figure 21 shows conclusively that the HJV-l Savine described above can generate a Gag and Nef CTL response in naϊve mice. It should be noted, however, that the Nef CTL epitope appeared to exist only in Pool 1 since it was not restimulated by Pool 2. This is further proof of the utility of combining HIV-1 Savine Pool 1 and Pool 2 components together to provide broader vaccine coverage. The HJV-l Savine Vaccinia vectors have also been used to restimulate in vivo HJV-l responses in pre-immune M. nemestrina monkeys. These experiments (Figure 22) showed, by ENEF-γ ELISPOT and CD69 expression on both CD4 and CD8 T cells, that the ability of the HIV-1 SAVINE to restimulate HIV-1 specific responses in vivo is equivalent or perhaps better than another HJV-l candidate vaccine. This is a generic strategy able to be applied to many other human infections or cancers where T-cell responses are considered to be important for protection or recovery. With this in mind the inventors have begun constructing Savines for melanoma, cervical cancer and Hepatitis C. In the case of melanoma, the majority of the currently identified melanoma antigens have been divided into two groups, one containing antigens associated with melanoma and one containing differentiation antigens from melanocytes, which are often upregulated in melanomas. Two Savine constructs are presently being constructed to cater for these two groups. The reason for making the distinction is that treatment of melanoma might first proceed using the Savine that incorporates fragments of melanoma specific antigens only. If this Savine fails to control some metastases then the less specific Savine containing the melanocyte-specific antigens can then be used. It is important to point out that other cancers also express many of the antigens specific to melanomas e.g., testicular and breast cancers. Hence the melanoma specific Savine may have therapeutic benefits for other cancers. A small Savine is also being constructed for cervical cancer. This Savine will contain two antigens, E6 and E7, from two strains of human papilloma virus (HPV), HPV- 16 and HPV- 18, directly linked with causing the majority of cervical cancers worldwide. There is a large number of sequence differences in these two antigens between the two strains which would normally require two Savines to be constructed. However since this Savine is small, the antigen fragments from both strains are being scrambled together. While it is normally better for the Savine approach to include all or a majority of the antigens from a virus, in this case only E6 and E7 are expressed during viral latency or in cervical carcinomas. Hence in the interests of simplicity, the rest of the HPV genome will not be included although all HPV antigens would be desirable in a Savine against genital warts. Two Savines have also been constructed for two strains of hepatitis C, a major cause of liver disease in the world. Hepatitis C is similar to HJV in the requirements for a vaccine or therapeutic. However, the major hepatitis C strains share significantly lower homology, 69-79%, with one another than do the various HJV clades. To cater for this the inventors have decided to construct two separate constructs to cater for the two major strains present in Australia, types laand 3a, which together cause approximately 80-95% of hepatitis C infections in this country. Both constructs will be approximately the same size as the HIV Savine but will be blended together into a single vaccine or therapy. Overall it is believed that the Savine vaccine strategy is a generic technology likely to be applied to a wide range of human diseases. It is also believed that because it is not necessary to characterise each antigen, this technology will be actively applied to animal vaccines as well where research into vaccines or therapies is often inhibited by the lack of specific reagents, modest research budgets and poor returns on animal vaccines. EXAMPLE 2 Hepatitis C Savine Synthetic immunomodulatory molecules have also been designed for treating Hepatitis C. In one example, the algorithm of Figure 25 was applied to a consensus polyprotein sequence of Hepatitis C la to facilitate its segmentation into overlapping segments (30 aa segments overlapping by 15 aa), the rearrangement of these segments into a scrambled order and the output of Savine nucleic acid and amino acid sequences, as shown in Figure 26. Exemplary DNA cassettes (A, B and C) are also shown in Figure 26, which contain suitable restriction enzyme sites at their ends to facilitate their joining into a single expressible open reading frame. EXAMPLE 3 Melanoma Savine The algorithm of Figure 25 was also applied to melanocyte differentiation antigens (gplOO, MART, TRP-1, Tyros, Trp-2, MC1R, MUCIF and MUCIR) and to melanoma specific antigens (BAGE, GAGE-1, gpl00In4, MAGE-1, MAGE-3, PRAME, TRP2TN2, NYNSOla, NYNSOlb and LAGEl), as shown in Figure 27, to provide separate Savine nucleic acid and amino acid sequences for treating or preventing melanoma. EXAMPLE 4 Resolvase Repair Experiment A resolvase can be used advantageously to repair errors in polynucleotides. The following procedure outlines resolvase repair of a synthetic 340 bp fragment in which DNA errors were common. Method The 340 bp fragment was PCR amplified and gel purified on a 4% agarose gel. After spin purifying, lOul of the eluate corresponding to approximately 100 ng was subjected to the resolvase repair treatment. The rest of the DNA sample was stored for later cloning as the untreated control. 2 μL of lOxPCR buffer, 2 μL of 20 mM MgCl 2 and 6 μL of MilliQ™ water (MQW) and Taq DNA polymerase were added to the 10 μL DNA sample. The mixture was subjected to the following thermal profile; 95°C for 5min, 65°C for 30min, cooled and held at 37°C. Five μL of 10xT7 endonuclease I buffer, 8 μL of 1/50 μL of T7endoI enzyme stock and 17 μL of MQW were added, mixed and incubated for 30 min. Loading buffer was added to the sample and the sample was electrophoresed on a 4% agarose gel. A faint band corresponding to the full length fragment was excised and subjected to 15 further cycles of PCR. The amplified fragment was agarose gel purified and, along with the untreated DNA sample, cloned into pBluescript. Eleven plasmid clones for each DNA sample were sequenced and the number and type of errors compared (see table) Buffers were as follows: lOx T7endonuclease buffer 2.5ml IM TRIS pH7.8, 0.5ml IM MgCl 2 , 25 μL 1 M DTT, 50 μL lOmg/mL BSA, 2 mL MQW made up to a total of 5 mL. T7 endonuclease I stock Concentrated sample of enzyme prepared by, and obtained from, Jeff Babon (St Vincent's Hospital) was diluted 1/50 using the following dilution buffer: 50 μL 1 M TRIS pH7.8, O.l L IM EDTA pH8, 5 μL 100 mM glutathione, 50 μL lOmg/mL BSA, 2.3 mL MQW, 2.5 mL glycerol made up to a total of 5 mL. Results The results are summarised in Tables 2 and 3. TABLE 2 TABLE S Discussion/Conclusion While overall the number of correct clones obtained was not significantly different, there was a significant difference in the level of errors. This reduction in errors becomes more significant as greater numbers of long oligonucleotides are joined into the one construct i.e., increasing the difference between untreated versus treated samples in the chance of obtaining a correct clone. It is believed that combining another resolvase such as T4 endonuclease VH may further enhance repair or increase the bias against errors. Importantly, this experiment was not optimised e.g., by using proofreading PCR enzymes or optimised conditions. Finally if the repair reaction is carried out during normal PCR, for example, by including a thermostable resolvase, it is believed that amplification of already damaged long oligonucleotides, and the normal accumulation of PCR induced errors, even using error reading polymerases during PCR, could be reduced significantly. The repair of damaged long oligonucleotides is particularly important for synthesis of long DNA fragment such as in Savines because, while the rate of long oligonucleotide damage is typically <5%, after joining 10 oligonucleotides, the error rate approaches 50%. This is true even using the best proofreading PCR enzymes because these enzymes do not verify the sequence integrity using correct oligonucleotide templates that exist as a significant majority (95%) in a joining reaction. The disclosure of every patent, patent application, and publication cited herein is incorporated herein by reference in its entirety. The citation of any reference herein should not be construed as an admission that such reference is available as "Prior Art" to the instant application Throughout the specification the aim has been to describe the preferred embodiments of the invention without limiting the invention to any one embodiment or specific collection of features. Those of skill in the art will therefore appreciate that, in light of the instant disclosure, various modifications and changes can be made in the particular embodiments exemplified without departing from the scope of the present invention. All such modifications and changes are intended to be included within the scope of the appended claims. BIBLIOGRAPHY Ada G.L. Vaccines. In: Paul, WE, Fundamental Immunology, 3rd edition, Raven Press, Ltd, New York 1993, : 1309- 1352. Boyle D.B., Coupar B.E.H., Both G.W.: Multiple-cloning-site plasmids for the rapid construction of recombinant poxviruses. Gene 1985,35:169-177. Brown J.H., Jardetsky T.S., Gorga J.C., Stern L.J., Urban R.G., Strominger J.L., Wiley D.C.: Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1. Nature 1993, 364:33-39. Chicz, R.M., Urban, R.G., Gorga, J.C., Vignali, D.A.A., Lane, W.S. and Strominger, J.L., Specificity and promiscuity among naturally processed peptides bound to HLA-DR alleles., J. Exp. Med, 178, 27-47 (1993). Del Val M., Schlicht H. 5 Ruppert T., Reddehase M.J., Koszinowski U.H.: Efficient processing of an antigenic sequence for presentation by MHC class I molecules depends on its neighboring residues in the protein. Cell 1991, 66:1145-1153. Dyall, R., Vasovic, L.V., Molano, A. and Nikolic-Zugic, J., CD4-independent in vivo priming of murine CTL by optimal MHC class I-restricted peptides derived from intracellular pathogens., Int. Immunol, 7(8), 1205-1212 (1995). 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Claims: WHAT IS CLAIMED IS: 1. A synthetic polypeptide comprising a plurality of different segments of at least one parent polypeptide, wherein the segments are linked together in a different relationship relative to their linkage in the at least one parent polypeptide to impede, abrogate or otherwise alter at least one function associated with the parent polypeptide. 2. The synthetic polypeptide of claim 1, consisting essentially of different segments of a single parent polypeptide. 3. The synthetic polypeptide of claim 1, consisting essentially of different segments of a plurality of different parent polypeptides. 4. The synthetic polypeptide of claim 1, wherein the segments in said synthetic polypeptide are linked sequentially in a different order or arrangement relative to their linkage in said at least one parent polypeptide. 5. The synthetic polypeptide of claim 4, wherein the segments in said synthetic polypeptide are randomly rearranged relative to their order or arrangement in said at least one parent polypeptide. 6. The synthetic polypeptide of claim 1, wherein the size of an individual segment is at least 4 amino acids. 7. The synthetic polypeptide of claim 6, wherein the size of an individual segment is from about 20 to about 60 amino acids. 8. The synthetic polypeptide of claim 7, wherein the size of an individual segment is about 30 amino acids. 9. The synthetic polypeptide of claim 7, comprising at least 30% of the parent polypeptide sequence. 10. The synthetic polypeptide of claim 1, wherein at least one of said segments comprises partial sequence identity or homology to one or more other said segments. 11. The synthetic polypeptide of claim 10, wherein the sequence identity or homology is contained at one or both ends of an individual segment. 12. The synthetic polypeptide of claim 11, wherein one or both ends of said segment comprises at least 4 contiguous amino acids that are identical to, or homologous with, an amino acid sequence contained within one or more other of said segments. 13. The synthetic polypeptide of claim 10, wherein the size of an individual segment is about twice the size of the sequence that is identical or homologous to the or each other said segment. 14. The synthetic polypeptide of claim 13, wherein the size of an individual segment is about 30 amino acids and the size of the sequence that is identical or homologous to the or each other said segment is about 15 amino acids. 15. The synthetic polypeptide of claim 1, wherein an optional spacer is interposed between some or all of the segments. 16. The synthetic polypeptide of claim 15, wherein the spacer alters proteolytic processing and/or presentation of adjacent segment(s). 17. The synthetic polypeptide of claim 16, wherein the spacer comprises at least one neutral amino acid. 18. The synthetic polypeptide of claim 16, wherein the spacer comprises at least one alanine residue. 19. The synthetic polypeptide of claim 1, wherein the at least one parent polypeptide is associated with a disease or condition. 20. The synthetic polypeptide of claim 1, wherein the at least one parent polypeptide is selected from a polypeptide of a pathogenic organism, a cancer-associated polypeptide, an autoimmune disease-associated polypeptide, an allergy-associated polypeptide or a variant or derivative of these. 21. The synthetic polypeptide of claim 1, wherein the at least one parent polypeptide is a polypeptide of a virus. 22. The synthetic polypeptide of claim 21, wherein the virus is selected from a Human Immunodeficiency Virus (HJV) or a Hepatitis virus. 23. The synthetic polypeptide of claim 22, wherein the virus is a Human Immunodeficiency Virus (HIV) and the at least one parent polypeptide is selected from env, gag, pol, vif, vpr, tat, rev, vpu and nef, or a combination thereof. 24. The synthetic polypeptide of claim 1, wherein the at least one parent polypeptide is a cancer-associated polypeptide. 25. The synthetic polypeptide of claim 24, wherein the cancer is melanoma. 26. The synthetic polypeptide of claim 25, wherein the at least one parent polypeptide is a melanocyte differentiation antigen. 27. The synthetic polypeptide of claim 25, wherein the at least one parent polypeptide is a melanocyte differentiation antigen selected from gplOO, MART, TRP-1, Tyros, TRP2, MC1R, MUCIF, MUCIR or a combination thereof. 28. The synthetic polypeptide of claim 25, wherein the at least one parent polypeptide is a melanoma-specific antigen. 29. The synthetic polypeptide of claim 25, wherein the at least one parent polypeptide is a melanoma-specific antigen selected from BAGE, GAGE-1, gpl00In4, MAGE-1, MAGE- 3, PRAME, TRP2IN2, NYNSOla, NYNSOlb, LAGEl or a combination thereof. 30. A synthetic polynucleotide encoding a synthetic polypeptide comprising a plurality of different segments of at least one parent polypeptide, wherein the segments are linked together in a different relationship relative to their linkage in the at least one parent polypeptide to impede, abrogate or otherwise alter at least one function associated with the parent polypeptide. 31. A method for producing the synthetic polynucleotide encoding a synthetic polypeptide comprising a plurality of different segments of at least one parent polypeptide, wherein the segments are linked together in a different relationship relative to their linkage in the at least one parent polypeptide to impede, abrogate or otherwise alter at least one function associated with the parent polypeptide, said method comprising: - linking together in the same reading frame a plurality of nucleic acid sequences encoding different segments of the at least one parent polypeptide to form a synthetic polynucleotide whose sequence encodes said segments linked together in a different relationship relative to their linkage in the at least one parent polypeptide. 32. The method of claim 31, further comprising fragmenting the sequence of a respective parent polypeptide into fragments and linking said fragments together in a different relationship relative to their linkage in a respective parent polypeptide sequence. 33. The method of claim 32, wherein the fragments are randomly linked together. 34. The method of claim 31, further comprising reverse translating the sequence of a respective parent polypeptide or a segment thereof to provide a nucleic acid sequence encoding said parent polypeptide or said segment. 35. The method of claim 34, wherein an amino acid of a respective parent polypeptide sequence is reverse translated to provide a codon, which has higher translational efficiency than other synonymous codons in a cell of interest. 36. The method of claim 35, wherein an amino acid of said parent polypeptide sequence is reverse translated to provide a codon which, in the context of adjacent or local sequence elements, has a lower propensity of forming an undesirable sequence that is refractory to the execution of a task. 37. The method of claim 35, wherein an amino acid of said parent polypeptide sequence is reverse translated to provide a codon which, in the context of adjacent or local sequence elements, has a lower propensity of forming an undesirable sequence selected from a palindromic sequence or a duplicated sequence, which is refractory to the execution of a task selected from cloning or sequencing. 38. The method of claim 31, further comprising linking a spacer oligonucleotide encoding at least one spacer residue between segment-encoding nucleic acids. 39. The method of claim 38, wherein spacer oligonucleotide encodes 2 to 3 spacer residues. 40. The method of claim 38 or claim 39, wherein the spacer residue is a neutral amino acid. 41. The method of claim 38 or claim 39, wherein the spacer residue is alanine. 42. The method of claim 31, further comprising linking in the same reading frame as other segment-containing nucleic acid sequences at least one variant nucleic acid sequence which encodes a variant segment having a homologous but not identical amino acid sequence relative to other encoded segments. 43. The method of claim 42, wherein the variant segment comprises conserved and/or non- conserved amino acid differences relative to one or more other encoded segments. 44. The method of claim 43, wherein the differences correspond to sequence polymorphisms. 45. The method of claim 44, wherein degenerate bases are designed or built in to the at least one variant nucleic acid sequence to give rise to all desired homologous sequences. 46. The method of claim 31, further comprising optimising the codon composition of the synthetic polynucleotide such that it is translated efficiently by a host cell. 47. A synthetic construct comprising a synthetic polynucleotide encoding a synthetic polypeptide comprising a plurality of different segments of at least one parent polypeptide, wherein the segments are linked together in a different relationship relative to their linkage in the at least one parent polypeptide to impede, abrogate or otherwise alter at least one function associated with the parent polypeptide, wherein said synthetic polynucleotide is operably linked to a regulatory polynucleotide. 48. The synthetic construct of claim 47, further including a nucleic acid sequence encoding an immunostimulatory molecule. 49. The synthetic construct of claim 48, wherein the immunostimulatory molecule comprises a domain of an invasin protein (Inv). 50. The synthetic construct of claim 48, wherein the immunostimulatory molecule comprises the sequence set forth in SEQ ED NO: 1467 or an immune stimulatory homologue thereof. 51. The synthetic construct of claim 48, wherein the immunostimulatory molecule is a T cell co-stimulatory molecule. 52. The synthetic construct of claim 48, wherein the immunostimulatory molecule is a T cell co-stimulatory molecule selected from a B7 molecule or an ICAM molecule. 53. The synthetic construct of claim 48, wherein the immunostimulatory molecule is a B7 molecule or a biologically active fragment thereof, or a variant or derivative of these. 54. The synthetic construct of claim 48, wherein the immunostimulatory molecule is a cytokine selected from an interleukin, a lymphokine, tumour necrosis factor or an interferon. 55. The synthetic construct of claim 48, wherein the immunostimulatory molecule is an immunoniodulatory oligonucleotide. 56. An immunopotentiating composition, comprising an immunopotentiating agent selected from the synthetic polypeptide of claim 1, the synthetic polynucleotide of claim 30 or the synthetic construct of claim 47, together with a pharmaceutically acceptable carrier. 57. The composition of claim 56, further comprising an adjuvant. 58. A method for modulating an immune response, which response is preferably directed against a pathogen or a cancer, comprising administering to a patient in need of such treatment an effective amount of an immunopotentiating agent selected from the synthetic polypeptide of claim 1, the synthetic polynucleotide of claim 30, the synthetic construct of claim 47, or the composition of claim 56. 59. A method for treatment and/or prophylaxis of a disease or condition, comprising administering to a patient in need of such treatment an effective amount of an immunopotentiating agent selected from selected from the synthetic polypeptide of claim 1, the synthetic polynucleotide of claim 30, the synthetic construct of claim 47, or the composition of claim 56. 60. A computer program product for designing the sequence of a synthetic polypeptide comprising a plurality of different segments of at least one parent polypeptide, wherein the segments are linked together in a different relationship relative to their linkage in the at least one parent polypeptide to impede, abrogate or otherwise alter at least one function associated with the parent polypeptide, said program product comprising: - code that receives as input the sequence of said at least one parent polypeptide; - code that fragments the sequence of a respective parent polypeptide into fragments; - code that links together said fragments in a different relationship relative to their linkage in said parent polypeptide sequence; and - a computer readable medium that stores the codes. 61. The computer program product of claim 60, further comprising code that randomly rearranges said fragments. 62. The computer program product of claim 60, further comprising code that links the sequence of a spacer residue to the sequence of said at least one parent polypeptide or to said fragments. 63. A computer program product for designing the sequence of a synthetic polynucleotide encoding a synthetic polypeptide comprising a plurality of different segments of at least one parent polypeptide, wherein the segments are linked together in a different relationship relative to their linkage in the at least one parent polypeptide to impede, abrogate or otherwise alter at least one function associated with the parent polypeptide, comprising: - code that receives as input the sequence of at least one parent polypeptide; - code that fragments the sequence of a respective parent polypeptide into fragments; - code that reverse translates the sequence of a respective fragment to provide a nucleic acid sequence encoding said fragment; - code that links together in the same reading frame each said nucleic acid sequence to provide a polynucleotide sequence that codes for a polypeptide sequence in which said fragments are linked together in a different relationship relative to their linkage in the at least one parent polypeptide sequence; and - a computer readable medium that stores the codes. 64. The computer program product of claim 63, further comprising code that randomly rearranges said nucleic acid sequences. 65. The computer program product of claim 64, further comprising code that reverse translates an amino acid of a respective parent polypeptide sequence to provide a codon, which has higher translational efficiency than other synonymous codons in a cell of interest. 66. The computer program product of claim 63, further comprising code that reverse translates an amino acid of a respective parent polypeptide sequence to provide a codon which, in the context of adjacent or local sequence elements, has a lower propensity of forming an undesirable sequence that is refractory to the execution of a task. 67. The computer program product of claim 63, further comprising code that links a spacer oligonucleotide to one or more of said nucleic acid sequences. 68. A computer for designing the sequence of a synthetic polypeptide comprising a plurality of different segments of at least one parent polypeptide, wherein the segments are linked together in a different relationship relative to their linkage in the at least one parent polypeptide to impede, abrogate or otherwise alter at least one function associated with the parent polypeptide, wherein said computer comprises: (a) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein said machine-readable data comprise the sequence of at least one parent polypeptide; (b) a working memory for storing instructions for processing said machine-readable data; (c) a central-processing unit coupled to said working memory and to said machine- readable data storage medium, for processing said machine readable data to provide said synthetic polypeptide. sequence; and (d) an output hardware coupled to said central processing unit, for receiving said synthetic polypeptide sequence. 69. The computer of claim 68, wherein the processing of said machine readable data comprises fragmenting the sequence of a respective parent polypeptide into fragments and linking together said fragments in a different relationship relative to their linkage in the sequence of said parent polypeptide. 70. The computer of claim 68, wherein the processing of said machine readable data comprises randomly rearranging said fragments. 71. The computer of claim 68, wherein the processing of said machine readable data comprises linking the sequence of a spacer residue to the sequence of said at least one parent polypeptide or to said fragments. 72. A computer for designing the sequence of a synthetic polynucleotide encoding a synthetic polypeptide comprising a plurality of different segments of at least one parent polypeptide, wherein the segments are linked together in a different relationship relative to their linkage in the at least one parent polypeptide to impede, abrogate or otherwise alter at least one function associated with the parent polypeptide, wherein said computer comprises: (a) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein said machine-readable data comprise the sequence of at least one parent polypeptide; (b) a working memory for storing instructions for processing said machine-readable data; (c) a central-processing unit coupled to said working memory and to said machine- readable data storage medium, for processing said machine readable data to provide said synthetic polynucleotide sequence; and (d) an output hardware coupled to said central processing unit, for receiving said synthetic polynucleotide sequence. 73. The computer of claim 72, wherein the processing of said machine readable data comprises fragmenting the sequence of a respective parent polypeptide into fragments, reverse translating the sequence of a respective fragment to provide a nucleic acid sequence encoding said fragment and linking together in the same reading frame each said nucleic acid sequence to provide a polynucleotide sequence that codes for a polypeptide sequence in which said fragments are linked together in a different relationship relative to their linkage in the at least one parent polypeptide sequence. 74. The computer of claim 72, wherein the processing of said machine readable data comprises randomly rearranging said nucleic acid sequences. 75. The computer of claim 72, wherein the processing of said machine readable data comprises reverse translating an amino acid of a respective parent polypeptide sequence to provide a codon, which has higher translational efficiency than other synonymous codons in a cell of interest. 76. The computer of claim 72, wherein the processing of said machine readable data comprises reverse translating an amino acid of a respective parent polypeptide sequence to provide a codon which, in the context of adjacent or local sequence elements, has a lower propensity of forming an undesirable sequence that is refractory to the execution of a task. 77. The computer of claim 72, wherein the processing of said machine readable data comprises linking a spacer oligonucleotide to one or more of said nucleic acid sequences.

Inventors: RAMSHAW IAN ALISTAIR, THOMSON SCOTT ANTHONY, RAMSHAW, IAN, ALISTAIR, THOMSON, SCOTT, ANTHONY
Applicants: RAMSHAW IAN ALISTAIR, THOMSON SCOTT ANTHONY, UNIV AUSTRALIAN, RAMSHAW, IAN, ALISTAIR, THE AUSTRALIAN NATIONAL UNIVERSITY, THOMSON, SCOTT, ANTHONY
Application year: 2001
Main classification: C07K19
IPC codes: A61K38, A61K48, A61P31, A61P35, A61P37, C07K14, C07K19, C12N15, G06F17, G06F19