METHOD AND COMPOSITION TO ENHANCE THE EFFICACY OF A VACCINE USING CHEMOKINES

Abstract: The present invention relates to a method to enhance the efficacy of a vaccine in a subject treated with the vaccine comprising administering to the subject in combination with the vaccine a one or more chemokines. The present invention also relates to compositions of vaccines containing chemokines.

Description: METHOD AND COMPOSITION TO ENHANCE THE EFFICACY OF A VACCINE USING CHEMOKINES 1. CROSS-REFERENCE TO RELATED APPLICATIONS This application claims priority to U.S. Application Serial No. 60/069,281 filed December 1 1 , 1997. 2. BACKGROUND OF THE INVENTION The present invention relates to a method to enhance the efficacy of a vaccine by administration of a chemokine, such as macrophage derived chemokine (MDC), in conjunction with the vaccine. The present invention also relates to compositions useful in the method. 2.1. GENERATION OF AN IMMUNE RESPONSE The introduction of a foreign antigen into an individual elicits an immune response consisting of two major components, the cellular and humoral immune responses, mediated by two functionally distinct populations of lymphocytes known as T and B cells, respectively (see generally Coutinho, 1991 , Immune System, Encyclopedia of Human Biology, Vol. 4, Ed. Dulbecco, Academic Press, Inc.). A subset of T cells responds to antigen stimulation by producing lymphokines which "help" or activate various other cell types in the immune system. Another T cell subset is capable of developing into antigen-specific cytotoxic effector cells, which can directly kill antigen-positive target cells. On the other hand, the B cell response is primarily carried out by secretory proteins, antibodies, which directly bind and neutralize antigens. Helper T cells (TH) can be distinguished from classical cytotoxic T lymphocytes (CTL) and B cells by their cell surface expression of the glycoprotein marker CD4. Although the mechanism by which CD4 + TH function has not been fully elucidated, the existence of functionally distinct subsets within the CD4 + T cell compartment has been reported (Mosmann and Coffman, 1989, Ann. Rev. Immunol. 7:145-1 73). In the mouse, type 1 helper T cells (TH1 ) produce interleukin-2 (IL-2) and τ-interferon (τ-IFN) upon activation, while type 2 helper T cells (TH2) produce IL-4 and IL-5. Based on the profile of lymphokine production, TH 1 appear to be involved in promoting the activation and proliferation of other T cell subsets including CTL, whereas TH2 specifically regulate B cell proliferation and differentiation, antibody synthesis, and antibody class switching. A second T cell subpopulation is the classical CTL which express the CD8 surface marker. Unlike most TH, these cells display cytolytic activity upon direct contact with target cells, rather than through the production of lymphokines. In vivo, CTL function is particularly important in situations where an antibody response alone is inadequate. Significant experimental evidence indicates that CTL rather than B cells and their antibody products play a principal role in the defense against viral infections and cancer. A salient feature of both T and B cell responses is their exquisite specificity for the immunizing antigen; however, the mechanisms for antigen recognition differ between these two cell types. B cells recognize antigens by antibodies, either acting as cell surface receptors or as secreted proteins, which bind directly to antigens on a solid surface or in solution, whereas T cells only recognize antigens that have been processed or degraded into small fragments and presented on a solid phase such as the surface of antigen-presenting cells (APC). Additionally, antigenic fragments must be presented to T cells in association with major histocompatibility complex (MHC)- encoded class I or class II molecules. The MHC refers to a cluster of genes that encode proteins with diverse immunological functions. In man, the MHC is known as HLA. Class I gene products are found on all somatic cells, and they were originally discovered as targets of major transplantation rejection responses. Class II gene products are mostly expressed on cells of various hematopoietic lineages, and they are involved in cell-cell interactions in the immune system. Most importantly, MHC- encoded proteins have been shown to function as receptors for processed antigenic fragments on the surface of APC (Bjorkman et al., 1987, Nature 329:506-512). Another level of complexity in the interaction between a T cell and an antigenic fragment is that it occurs only if the MHC molecules involved are the same on the APC and the responding T cells. In other words, a T cell specific for a particular antigenic epitope expresses a receptor having low affinity for self MHC proteins, which when such MHC proteins on APC are occupied by the epitope, engage the T cell in a stronger interaction leading to antigen-specific T cell activation. The phenomenon of a T cell reacting with a processed antigen only when presented by cells expressing a matching MHC is known as MHC-restriction. The specificity of T cell immune responses for antigens is a function of the unique receptors expressed by these cells. The T cell receptor (TCR) is structurally homologous to an antibody; it is a heterodimer composed of disulfide-linked glycoproteins. Four TCR polypeptide chains known as α, β, τ, and δ have been identified, although the vast majority of functional T cells express the αβ heterodimeric TCR. Transfer of α and β genes alone into recipient cells was shown to be both necessary and sufficient to confer antigen specificity and MHC-restriction (Dembic et al., 1986, Nature 320:232-238). Thus, the αβ TCR appears to be responsible for recognizing a combination of antigenic fragment and MHC determinants. The apparent basis of MHC restriction is that CD4 + T cells express αβ TCR which recognize antigenic fragments physically associated with MHC class II proteins, while the TCR on CD8 + CTL recognize MHC class l-associated fragments. Thus, CD4 + T cells can recognize only a restricted class of APC that are class ll + , whereas CD8 + CTL can interact with virtually any antigen-positive cells, since all cells express class I molecules. CD4 + CTL have been identified, and they are MHC class II restricted, and lyse target cells only if the latter express self-MHC class II determinants associated with specific antigenic fragments. Both CD4 and CD8 molecules also contribute to this interaction by binding to monotypic determinants on the MHC class II and I molecules, respectively. A second type of TCR composed of τδ heterodimers is expressed by a small percentage of T cells, but the involvement of τδ T cells in antigen-specific recognition is still poorly understood. Some studies have shown that functionally active τδ T cells can be cytolytic in a MHC non-restricted manner. In summary, the generation of an immune response begins with the sensitization of CD4 + and CD8 + T cell subsets through their interaction with APC that express MHC-class I or class II molecules associated with antigenic fragments. The sensitized or primed CD4 + T cells produce lymphokines that participate in the activation of B cells as well as various T cell subsets. The sensitized CD8 + T cells increase in numbers in response to lymphokines and are capable of destroying any cells that express the specific antigenic fragments associated with matching MHC- encoded class I molecules. For example, in the course of a viral infection, CTL eradicate virally-infected cells, thereby limiting the progression of virus spread and disease development. 2.2. ANTIGEN PRESENTING CELLS The presentation of antigens to T cells is carried out by specialized cell populations referred to as antigen presenting cells (APC). Typically, APC include macrophages/monocytes, B cells, and bone marrow derived dendritic cells (DC). APC are capable of internalizing exogenous antigens, cleaving them into smaller fragments in enzyme-rich vesicles, and coupling the fragments to MHC-encoded products for expression on the cell surface (Goldberg and Rock, 1992, Nature 357:375-379). Since APC express both MHC-encoded class I and class II glycoproteins, they can present antigenic fragments to both CD4 + and CD8 + T cells for the initiation of an immune response. By definition, APC not only can present antigens to T cells with antigen- specific receptors, but can provide all the signals necessary for T cell activation. Such signals are incompletely defined, but probably involve a variety of cell surface molecules as well as cytokines or growth factors. Further, the factors necessary for the activation of naive or unprimed T cells may be different from those required for the reactivation of previously primed memory T cells. The ability of APC to both present antigens and deliver signals for T cell activation is commonly referred to as an accessory cell function. Although monocytes and B cells have been shown to be competent APC, their antigen presenting capacities in vitro appear to be limited to the re-activation of previously sensitized T cells. Hence, they are not capable of directly activating functionally naive or unprimed T cell populations. Although it had been known for a long time that APC process and present antigens to T cells, it was not shown until relatively recently that small antigenic peptides could directly bind to MHC-encoded molecules (Babbit et al., 1 985, Nature 31^:359; Townsend et al., 1986, Cell 44:959). However, it is believed that, normally, complex antigens are proteolytically processed into fragments inside the APC, and become physically associated with the MHC-encoded proteins intracellularly prior to trafficking to the cell surface as complexes. Two distinct pathways for antigen presentation have been proposed (Braciale et al., 1987, Immunol. Rev. 98:95-1 14). It was thought that exogenous antigens were taken up by APC, processed and presented by the exogenous pathway to class II restricted CD4 + T cells, while the endogenous pathway processed intracellularly synthesized proteins, such as products of viral genes in virally-infected cells, for association with MHC class I proteins and presentation to CD8 + CTL. However, although the two pathways in antigen processing and presentation may still be correct in some respects, the distinction is blurred in light of recent findings that exogenously added antigens may also be presented to class I- restricted CTL (Moore et al., 1988, Cell 54:777). The term "dendritic cells" (DC) refers to a diverse population of morphologically similar cell types found in a variety of lymphoid and non-lymphoid tissues (Steinman, 1 991 , Ann. Rev. Immunol. 9:271-296). These cells include lymphoid DC of the spleen, Langerhans cells of the epidermis, and veiled cells in the blood circulation. Although they are collectively classified as a group based on their morphology, high levels of surface MHC-class II expression, and absence of certain other surface markers expressed on T cells, B cells, monocytes, and natural killer cells, it is presently not known whether they derive from a common precursor or can all function as APC in the same manner. Further, since the vast majority of published reports have utilized DC isolated from the mouse spleen, results from these studies may not necessarily correlate with the function of DC obtained from other tissue types. (Inaba et al., 1997, /. Exp. Med. J_66:182-194; Hengel et al., 1987, }. Immunol., 139:4196-4202; Kaut et al., 1988, /. Immunol., 140:3186-3193; Romani et al., 1989 . Exp. Med. 169:1 169-1 1 78; Macatonia et al., 1989, /. Exp. Med. 169: 1255-1264; Inaba et al., 1990, j. Exp. Med. 172:631 -6640). For example, despite high levels of MHC- class II expression, mouse epidermal Langerhans cells, unlike splenic DC, are not active APC in mixed leucocyte reaction (MLR), unless cultured with granulocyte- macrophage colony stimulating factor (GM-CSF) (Witmer-Pock et al., 1987, /. Exp. Med. 166:1484-1498; Heufler et al., 1988, /. Exp. Med. 167:700-705). Most human Langerhans cells express the CD1 and CD4 markers, while blood DC do not. Additionally, it has not been established the extent to which the functional characteristics observed with mouse DC are applicable to human DC, especially the DC obtained from non-splenic tissues; in part, due to inherent differences between the human and murine immune systems. Recently, a few studies have described the isolation of human DC from the peripheral blood, which involves the use of sheep red blood cells and/or fetal calf serum (Young and Steinman, 1990, /. Exp. Med. 1 71 :1315-1332; Freudenthal and Steinman, 1990, Proc. Natl. Acad. Sci. USA 87:7698-7702; Macatonia et al., 1989 Immunol. 67:285-289; Markowicz and Engleman, 1990, /. Clin. Invest. 85:955-961 ). Engleman et al. described a partial purification procedure of DC from human blood, which does not involve the use of sheep red blood cells and/or fetal calf serum, and showed that the partially purified human DC can, in fact, present exogenous antigens to naive T cells (PCT Publication WO 94/02156 dated February 3, 1994 at page 9, lines 5-32). Recent studies have indicated that DCs are superior APCs as compared to other APCs such as macrophages and monocytes. First, the potent accessory cell function of DCs provides for an antigen presentation system for virtually any antigenic epitopes which T and B cells are capable of recognizing through their specific receptors. For example, Engleman et al. demonstrate that human DCs can present both complex protein antigens and small peptides to CD4 + T cells as well as to as CD8 + CTL (PCT Publication WO 94/02156 dated February 3, 1994, Example 7, from page 29, line 10 to page 34, line 16). Engleman et al. also show that the in vitro priming effect of DCs does not require the addition of exogenous lymphokines, indicating that DCs produce all of the necessary signals in antigen presentation leading to the activation of T cells (PCT Publication WO 94/02156 dated February 3, 1994, from page 32, line 36 to page 33, line 2). More importantly, DCs can induce a primary CD4 + T cell-mediated proliferative response when similarly prepared monocytes can not induce such a response (PCT Publication WO 94/02156 dated February 3, 1994 at page 31 , lines 23- 30). Similarly, when DCs and monocytes ware compared for their ability to present antigens for re-activating secondary T cell response, it was observed that DCs were capable of stimulating a stronger response than monocytes (PCT Publication WO 94/02156 dated February 3, 1994 at page 32, lines 12-16). 2.3. CHEMOKINES Chemokines, or chemoattractant cytokines, are a subgroup of immune factors that have been shown to mediate chemotactic and other pro-inflammatory phenomena (see, Schall, 1991 , Cytokine 3 ^ :165-183). Chemokines are small molecules of approximately 70-80 residues in length and can generally be divided into two subgroups, α which have two N-terminal cysteines separated by a single amino acid (CxC) and β which have two adjacent cysteines at the N terminus (CC). RANTES, MIP- 1 α and MIP-1 β are members of the β subgroup (reviewed by Horuk, R., 1994, Trends Pharmacol. Sci. J_5: 159-165; Murphy, P.M., 1994, Annu. Rev. Immunol. 12:593-633; Baggiolini et al. Annu. Rev. Immunol. 1997, J_5:675-705 ). MCP-1 has been shown to attract monocytes but not neutrophils. MCP-1 , MCP- 2, and MCP-3 share a pyroglutamate proline NH 2 -terminal motif and are structurally closely related to each other and to eotaxin (56% to 71 % amino acid sequence identity). MCP-1 , MCP-2, and MCP-3 attract monocytes, CD4 + and CD8 + T lymphocytes (Loetscher et al. FAESB j. 1994, 8:1055-60), as well as basophil leukocytes. MCP-2, MCP-3, and MCP-4 (but not MCP-1 ) attracts eosinophil leukocytes. All four MCPs attract activated T lymphocytes, natural killer (NK) cells, and dendritic cells (see Baggiolini et al. Annu. Rev. Immunol. 1997, 15:675-705). Eotaxin acts on eosinophils and is inactive on neutrophils and monocytes, but has weak-to-moderate chemotactic activity toward IL-2-conditioned T lymphocytes (see Baggiolini et al. Annu. Rev. Immunol. 1997, J_5:675-705). Due to its preferential, powerful action on eosinophils and its occurrence in different species, eotaxin is considered to be an important chemokine in the pathophysiology of allergic conditions and asthma (See Baggiolini et al. Annu. Rev. Immunol. 1997, 15:675-705). IP10 is a CXC chemokine attracts human monocytes, T lymphocytes, and NK cells, and Mig attracts tumor-infiltrating T lymphocytes. It has been suggested that IP10 and Mig may also be involved in the regulation of lymphocyte recruitment and the formation of the lymphoid infiltrates observed in autoimmune inflammatory lesions, delayed-type hypersensitivity, some viral infections, and certain tumors (Baggiolini et al. Annu. Rev. Immunol. 1997, 1^:675-705). SDF-1 (stromal cell-derived factor 1 ), including SDF-1 and SDF-1 β stimulates the proliferation of B cell progenitors, and attracts mature dendritic cells (Finkel et al. Immunobiology 1998, 198:490-500). Synthetic human SDF-1 stimulates monocytes, neutrophils, and peripheral blood lymphocytes, as is indicated by [Ca2 +]i changes and chemotaxis. SDF-1 is also a powerful HIV-suppressive factor (See Baggiolini et al. Annu. Rev. Immunol. 1997, 15:675-705). The amino terminus of the β chemokines RANTES, MCP-1 , and MCP-3 has been implicated in the mediation of cell migration and inflammation induced by these chemokines. This involvement is suggested by the observation that the deletion of the amino terminal 8 residues of MCP-1 , amino terminal 9 residues of MCP-3, and amino terminal 8 residues of RANTES and the addition of a methionine to the amino terminus of RANTES, antagonize the chemotaxis, calcium mobilization and/or enzyme release stimulated by their native counterparts (Gong et al., 1996, /. Biol. Chem. 271 :10521- 10527; Proudfoot et al., 1996 /. Biol. Chem. 271:2599-2603). Additionally, α chemokine-like chemotactic activity has been introduced into MCP-1 via a double mutation of Tyr 28 and Arg 30 to leucine and valine, respectively, indicating that internal regions of this protein also play a role in regulating chemotactic activity (Beall et al., 1992, ). Biol. Chem. 267:3455-3459). The monomeric forms of all chemokines characterized thus far share significant structural homology, although the quaternary structures of α and β groups are distinct. While the monomeric structures of the β and α chemokines are very similar, the dimeric structures of the two groups are completely different. An additional chemokine, lymphotactin, which has only one N terminal cysteine has also been identified and may represent an additional subgroup (γ) of chemokines (Yoshida et al., 1995, FEBS Lett. 360:155-159; and Kelner et al., 1994, Science 266:1395-1399). Receptors for chemokines belong to the large family of G-protein coupled, 7 transmembrane domain receptors (GCR's) (See, reviews by Horuk, R., 1994, Trends Pharmacol. Sci. 15:159-165; and Murphy, P.M., 1994, Annu. Rev. Immunol. J_2:593- 633). Competition binding and cross-desensitization studies have shown that chemokine receptors exhibit considerable promiscuity in ligand binding. Examples demonstrating the promiscuity among β chemokine receptors include: CCR-1 , which binds RANTES and MIP-1 α (Neote et al., 1993, Cell 72:415-425), CCR-4, which binds RANTES, MIP-1 α, and MCP-1 (Power et al., 1995, /. Biol. Chem. 270:19495-19500), and CCR-5, which binds RANTES, MIP-1 α, and MIP-1 β (Alkhatib et al., 1996, Science 272:1955-1958 and Dragic et al., 1996, Nature 381:667-674). Erythrocytes possess a receptor (known as the Duffy antigen) which binds both α and β chemokines (Horuk et al., 1994, j. Biol. Chem. 269:1 7730-1 7733; Neote et al., 1994, Blood 84:44-52; and Neote et al., 1993, /. Biol. Chem. 268:12247-12249). Thus the sequence and structural homologies evident among chemokines and their receptors allow some overlap in receptor-ligand interactions. Godiska et al. identified and described the nucleic acid and amino acid sequences of an additional β chemokine designated macrophage derived chemokine (MDC) (PCT Publication WO 96/40923 dated December 19, 1996, and 1997, /. Exp. Med. 185:1595-1604). PCT publication WO 96/40923 further provides materials and methods for the recombinant production of the chemokine, the purified and isolated chemokine protein, and polypeptide analogues thereof. The PCT publication WO 96/40923 does not disclose that the human MDC has chemotactic activity upon DC. While Godiska et al. (1997, J. Exp. Med. 185:1595-1604) showed that, in a microchamber migration assay, monocyte-derived DC migrated toward the human MDC, the reference fails to teach that MDC can enhance an immune response to an antigen in vivo. Chang et al. (1997, J. Biol. Chem. 272(40):25229-25237), isolated a stimulated T cell chemotactic protein (STCP-1 ) from an activated macrophage cDNA library. The nucleotide sequence of the STCP-1 is identical to that of the MDC isolated by Godiska et al. (PCT Publication WO 96/40923 dated December 19, 1996, and 1997, ). Exp. Med. 185:1595-1604). However, unlike the results observed by Godiska et al. (1997, j. Exp. Med. 185: 1595-1604), Chang et al. (1997, /. Biol. Chem. 272(40) :25229- 25237) showed that although the STCP-1 acted as a mild chemoattractant for primary activated T lymphocytes and a potent chemoattractant for chronically activated T lymphocytes, the STCP-1 has no chemoattractant activity for monocytes, neutrophils, eosinophils and resting T lymphocytes. Chang et al. further showed that the STCP-1 does not induce Ca2 + mobilization in monocytes, dendritic cells, neutrophils, eosinophils, lipopolysaccharide-activated B lymphocytes, and freshly isolated resting T lymphocytes. 2.4. HIV VACCINES Human immunodeficiency virus (HIV) induces a persistent and progressive infection leading, in the vast majority of cases, to the development of the acquired immunodeficiency syndrome (AIDS) (Barre-Sinoussi et al., 1983, Science 220:868-870; Gallo et al., 1984, Science 224:500-503). The HIV envelope surface glycoproteins are synthesized as a single 160 kilodalton precursor protein which is cleaved by a cellular protease during viral budding into two glycoproteins, gp41 and gp120. gp41 is a transmembrane glycoprotein and gp120 is an extracellular glycoprotein which remains non-covalently associated with gp41 , possibly in a trimeric or multimeric form (Hammerskjold, M. and Rekosh, D., 1989, Biochem. Biophys. Ada 989:269-280). The V3 loop of gp120 is the major determinant of sensitivity to chemokine inhibition of infection or replication (Cocchi et al., 1996, Nature Medicine 2:1244-1247; and Oravecz et al., 1996, j. Immunol. 1 57:1329-1332). Although considerable effort is being put into the design of effective therapeutics, currently no curative anti-retroviral drugs against AIDS exist. The HIV-1 envelope proteins (gp160, gp120, gp41 ) have been shown to be the major antigens for neutralizing anti-HIV antibodies present in AIDS patients (Barin et al., 1985, Science 228: 1094-1096). Thus far, therefore, these proteins seem to be the most promising candidates to act as antigens for anti-HIV vaccine development. Several groups have begun to use various portions of gp160, gp120, and/or gp41 as immunogenic targets for the host immune system (see, for example, Ivanoff et al., U.S. Pat. No. 5,141 ,867; Saith et al., PCT publication WO 92/22654; Shafferman, A., PCT publication WO 91/09872; Formoso et al., PCT publication WO 90/071 19). Therefore, methods to increase the efficacy of vaccines against HIV, especially vaccines using gp120 as the antigen, are needed. Additionally a novel vaccine technology, designated genetic vaccination, nucleic acid vaccination or DNA vaccination, has been explored to induce immune responses in vivo. Injection of cDNA expression cassettes results in in vivo expression of the encoded proteins (Dubensky et al., 1984, Proc. Natl. Acad. Sci. USA 81:7529- 7533; Raz et al., 1993, Proc. Natl. Acad. Sci. USA 90:4523; Wolff et al., 1990, Science 247:1465-1468), with the concomitant development of specific cellular and humoral immune responses directed against the encoded antigen(s) (Wang et al., 1995, Hum. Gene Ther. 6:407-418; Ulmer et al., 1993, Science 259:1 745-1 749; Tang et al., 1992, Nature 356:152-154; Michel et al., 1995, Proc. Natl. Acad. Sci. USA 92:5307-531 1 ; and Lowrie et al., 1994, Vaccine 12:1537-1540). Humoral and cellular responses have been induced to HIV-1 and SIV antigens through various applications of this technology in macaques (Wang et al., 1995, Virology 221 : 102-1 12; Wang et al., 1993, Proc. Natl. Acad. Sci. USA 90:4156-4160; and Boyer et al., 1996, ). Med. Primatol. 25:242-250) as well as mice (Wang et al., 1995, Virology 221 :102-1 12; Lu et al., 1995, Virology 209:147-154; Haynes et al., 1994, AIDS Res. Hum. Retrovi ruses U) (Suppl. 2):S43-S45; Okuda et al., 1995, Λ/DS Res. Hum. Retroviruses V :933-943). Recently, Lekutis et al. (1997, /. Immunol. 158:4471 -4477), assessed the TH cell response elicited by an HIV-1 gp120 DNA vaccine in rhesus monkeys by isolation of gp120-specific, MHC class ll-restricted CD4 + T cell lines from the vaccinated animals. Lekutis et al. showed that the isolated cell lines proliferated in response to APC in the presence of recombinant gp120, as well as to APC expressing HIV encoded env protein. Lekutis et al. further showed that these cell lines responded to env by secreting IFN-T and IFN-α without appreciable IL-4 production. These results demonstrate that the animals exhibited a cellular immune response to the DNA vaccine. Boyer et al. (1997, Nature Medicine 3:625-532), inoculated chimpanzees with an HIV-1 DNA vaccine encoding env, rev, and gag/pol, and found that the immunized animals developed specific cellular and humoral immune responses to these proteins. After challenging the immunized animals with a heterologous chimpanzee titered stock of HIV-1 SF2, Boyer et al. further found, using a Reverse Transcriptase- Polymerase Chain Reaction (RT-PCR) assay, that those animals vaccinated with the DNA vaccine were protected against infection whereas the control animals were not so protected. Kim et al., (1997 /. Immunol. 158:816-826), investigated the role of co-delivery of genes for IL-12 and GM-CSF along with DNA vaccine formulation for HIV-1 antigens env and gag/pol in mice. Kim et al. observed a dramatic increase in specific CTL response from the mice immunized with the HIV-1 DNA vaccine and IL-12. Kim et al. also observed that the co-delivery of IL-12 genes resulted in the reduction of specific antibody response, whereas the codelivery of GM-CSF genes resulted in the enhancement of specific antibody response. Kim et al. further observed that codelivery of IL-12 gene with a HIV DNA vaccine results in splenomegaly (Kim et al. 1997, /. Immunol., 158:816-826), which has been shown in mice to have toxic effects such as weight reduction or even death (Eng et al., 1995, /. Exp. Med. 181 :1893; Stevensen et al., 1995, /. Immunol. 155:2545; and Orange et al., 1995, /. Exp. Med. 181 :901). Notwithstanding the recent developments of the HIV DNA vaccine, there still exists a need for a method to enhance the efficacy of a vaccine, especially an HIV DNA vaccine. For instance, for efficacious vaccine against HIV-1 one preferably induces both cellular and humoral immune responses to control the infection (Boyer et al., 1997, Nature Medicine 3:625-532). The induction of both cellular and humoral immune response by the Berjer et al. method is still quite low because only one of the three immunized chimpanzees developed both cellular and humoral responses. Similarly, although co-delivery of an IL-12 encoding gene with a HIV DNA vaccine, as described in Kim et al. (1997, /. Immun. 158:816-826), may have enhanced the cellular immune response, this co-delivery also decreased the humoral response. Citation of a reference hereinabove shall not be construed as an admission that such reference is prior art to the present invention. 3. SUMMARY OF THE INVENTION. SUMMARY OF THE INVENTION. . SUMMARY OF THE INVENTION The present invention is based upon the ability of chemokines, such as MDC, Rantes, MIP-1 d, MIP-1 B, and I-309, to enhance the immune response to an antigen, particularly a vaccine. Accordingly, in a first aspect, the present invention provides a method for enhancing the efficacy of a vaccine, which method comprises administration to a subject of one or more purified chemokines, or biologically active fragments, analogues or derivatives thereof, either concurrently with one or more purified antigens against which an immune response is desired or within a time period either before or after administration of the antigens such that the immune response against the antigens is enhanced. In a second aspect, the present invention provides a method to enhance the efficacy of a vaccine, which method comprises administration to a subject of a first set of one or more purified nucleic acids comprising one or more nucleotide sequences encoding one or more chemokines, or fragments, derivatives, analogues, and/or truncation isoforms thereof, and a second purified nucleic acid comprising a nucleotide sequence encoding one or more antigens against which an immune response is desired, such that, the one or more chemokine(s) and the antigen(s) are expressed in a coordinated manner upon introduction into a suitable cell. Alternatively, the nucleotide sequences encoding one or more chemokines, or fragments, derivatives, and/or analogues thereof, and the antigens against which an immune response is desired are present on the same nucleic acid. In a preferred embodiment, the invention provides a method to enhance the efficacy of an HIV vaccine. In yet another aspect, the present invention provides a composition comprising an immunogenic amount of one or more purified antigens, an amount of one or more purified chemokines, or a fragments, derivatives, analogues and/or truncation isoforms thereof, effective to enhance the immune response to the antigen. In another aspect, the present invention provides a composition comprising a first set of one or more purified nucleic acids comprising one or more nucleotide sequences encoding one or more chemokines, fragments, derivatives analogues and or truncation isoforms thereof, and a second set of purified nucleic acids comprising one or more nucleotide sequences encoding one or more antigens against which an immune response is desired, such that, the chemokine(s) and the antigen are expressed in a coordinated manner upon introduction into a suitable cell. In a preferred embodiment, the antigen is an HIV antigen. In another preferred embodiment, the chemokine is selected from the group consisting of: Macrophage-derived chemokine, Monocyte chemotactic protein 1 , Monocyte chemotactic protein 2, Monocyte chemotactic protein 3, Monocyte chemotactic protein 4, activated macrophage specific chemokine 1 , Macrophage inflammatory protein 1 alpha, Macrophage inflammatory protein 1 beta, Macrophage inflammatory protein 1 gamma, Macrophage inflammatory protein 1 delta, Macrophage inflammatory protein 2 alpha, Macrophage inflammatory protein 3 alpha, Macrophage inflammatory protein 3 beta, Regulated upon activation, normal T cell expressed and secreted (and its variants), I-309, EBM-ligand chemokine, Pulmonary and activation regulated chemokine, Liver and activation-regulated chemokine, Thymus and activation regulated chemokine, Eotaxin (and variants), Human CC chemokine 1 , Human CC chemokine 2, Human CC chemokine 3, IL-10- inducible chemokine, liver-expressed chemokine, 6Ckine, Exodus 1 , Exodus 2, Exodus 3, thymus-expressed chemokine, Secondary Lymphoid tissue chemokine, Lymphocyte and Monocyte chemoattractant; Monotactin, Activation-induced, chemokine-related molecule, Myeloid progenitor inhibitory factor-1 , Myeloid progenitor inhibitory factor- 2, Stromal cell-derived factor 1 alpha, Stromal cell-derived factor 1 beta, B-cell- attracting chemokine 1 , HuMIG, H1 74, Interferon-stimulated T-cell alpha chemoattractant, lnterleukin-8, IP-10, platelet factor 4, growth-regulated gene-alpha, growth-regulated gene-beta, growth-regulated gene-gamma, Neutrophil-activating protein 2, ENA-78, granulocyte chemotactic protein 2, LYMPHOTACTIN, and Fractalkine/neurotactin. 4. DESCRIPTION OF FIGURES Figures 1 A and 1 B. The nucleotide and amino acid sequences of MDC. 1 A depicts the nucleotide sequence of MDC (SEQ ID NO:1 ), with the coding region indicated by the appearance of the amino acid sequence in the line below; and 1 B depicts the amino acid of MDC (SEQ ID NO:2) from GenBank accession no. U83171 (Godiska et al., 1997, /. Exp. Med. 185:1595-1 604). 5. DETAILED DESCRIPTION OF THE INVENTION The present invention relates to a method for enhancing the efficacy of a vaccine in a subject comprising administering to the subject one or more purified antigens in conjunction with one or more purified chemokines, or more purified fragments, derivatives or analogues and/or truncation isoforms thereof. While any chemokine may be employed according to the present invention, the chemokine is preferably selected from the following table: Chemokine Class Chemokines Abbreviations Accession Number CC Chemokines Macrophage inflammatory protein MIP-1 β j04130; d90145 (continued) 1 beta Macrophage inflammatory protein MIP-1γ 1 gamma Macrophage inflammatory protein MIP-15 AF031587 1 delta Macrophage inflammatory protein MIP-2α AF043340 2 alpha Macrophage inflammatory protein MIP-3α U77035 3 alpha Macrophage inflammatory protein MIP-3β u77180 3 beta Regulated upon activation, normal RANTES M2121 1 T cell expressed and secreted (and its variants) I-309 M57502 EBI1 -ligand chemokine ELC AB000887 Pulmonary and activation PARC/DC-CK- AB000221 regulated chemokine 1/MIP4 Liver and activation-regulated LARC D86955 chemokine Thymus and activation regulated TARC D43767 chemokine Eotaxin (and variants) D49372; Z69291 ; Z75669; Z75668 Human chemokine 1 HCC1 ; NCC2 Z49270; Z49269 Human chemokine 2 HCC2; NCC3, MIP- Z70292 5, MlP-lδ Human chemokine 3 HCC3 Z70293 IL-10-inducible chemokine HCC4 U91 46 liver-expressed chemokine. LEC; HCC4;NCC4 AB007454 6Ckine AF001979 Exodus 1 U64197 Exodus 2 U88320 Exodus 3 U88321 thymus-expressed chemokine TECK U86358 Secondary Lymphoid tissue SLC AB002409 chemokine The present invention also relates to the use of fragments, analogues and derivatives of the foregoing chemokines, as well as truncation isoforms of such chemokines which are known in the art. The present invention also relates to therapeutic compositions comprising one or more chemokines, nucleic acids encoding one or more chemokines, derivatives, analogues, and/or truncation isoforms thereof, and nucleic acids encoding the same, that are effective to enhance the immune response of a subject to a vaccine. In another preferred embodiment of the invention, nucleic acids comprising nucleotide sequences encoding one or more chemokines or fragments or derivatives, including truncation isoforms, thereof, and encoding one or more antigens against which an immune response is desired, which coding sequences are operatively linked to gene regulatory sequences capable of directing the expression of the one or more chemokines and the one or more antigens upon introduction into a suitable cell, for example, but not limited to, the cell (of a subject), are administered to a subject such that the one or more chemokines, or fragments or derivatives, including truncation isoforms, thereof, and one or more antigens, are expressed in the subject. For clarity of disclosure, and not by way of limitation, the detailed description of the invention is divided into the subsections which follow. 5.1. METHODS AND COMPOSITIONS TO ENHANCE THE EFFICACY OF A VACCINE The present invention provides methods for enhancing the efficacy of a vaccine in a subject, which methods comprise administering to a subject an immunogenic amount of one or more purified antigens against which an immune response is desired in the subject in conjunction with an amount of one or more purified chemokines, or fragments, derivatives, analogues and/or truncation isoforms thereof, effective to enhance the immune response against the antigen. In one aspect, the purified chemokine(s), or fragment(s), derivative(s), analogue(s) and/or truncation isoforms thereof, are administered to the subject concurrently with (e.g., in the same composition with) the purified antigen or antigens against which an immune response is desired. In another, aspect, the purified chemokine(s), or fragment(s), derivative(s), analogue(s) and/or truncation isoforms thereof, are administered either before or after the administration of one or more purified antigens against which immunity is desired in the subject, but is administered within such time that the chemokine(s) enhance the immune response to the one or more antigens. For example, but not by way of limitation, the purified chemokine(s) are administered during the time that the subject mounts an immune response against the administered one or more antigens, or, the purified MDC is administered within, for example, but not limited to, 30 minutes, 1 hour, 5 hours, 10 hours, 1 day, 2 days of (preferably, after) administration of the one or more purified antigens against which immunity is desired. In a preferred embodiment, the present invention provides compositions comprising an immunogenic amount of one or more purified antigens and an amount of purified MDC, or one or more fragments, derivatives or analogues thereof, effective to enhance the immune response to said antigen and, preferably, the composition further comprises a pharmaceutically acceptable carrier. A preferred chemokine for use in the methods and compositions of the present invention is any MDC protein, fragment or derivative thereof, that is capable of enhancing the efficacy of a vaccine (for example, but not limited to, as determined by the assays described in Section 5.4, infra). In one specific embodiment, the MDC is purified full length MDC, preferably full length MDC having the amino acid sequence of SEQ ID NO: 2 (Figure 1 B). In another embodiment, the MDC is a purified protein, the amino acid sequence of which consists of amino acid numbers 2-69 of SEQ ID NO: 2 (Figure 1 B). In another specific embodiment, the MDC is a purified protein, the amino acid sequence of which consists of amino acid numbers 3-69 of SEQ ID NO: 2 (Figure 1 B). In still another specific embodiment, the MDC is a purified protein, the N-terminal amino acid sequence of which consists of the amino acid sequence Tyr- Gly-Ala-Asn-Met-Glu-Asp-Ser-Val-Cys-Cys-Arg-Asp-Tyr-Val-Arg-Tyr-Arg-Leu (portion of SEQ ID NO: 2). In yet another specific embodiment, the MDC is a purified protein, the N-terminal amino acid sequence of which consists of the amino acid sequence Pro-Tyr-Gly-Ala-Asn-Met-Glu-Asp-Ser-Val-Cys-Cys-Arg (portion of SEQ ID NO: 2). In yet another specific embodiment, the MDC is a purified derivative of a protein, the N- terminal amino acid sequence of which protein consists of the amino acid sequence Tyr-Gly-Ala-Asn-Met-Glu-Asp-Ser-Val-Cys-Cys-Arg-Asp-Tyr-Val-Arg-Tyr-Arg-Leu (SEQ ID NO:2), which derivative has activity to enhance the efficacy of the vaccine. In yet another specific embodiment, the MDC is a purified derivative of a protein, the N- terminal amino acid sequence of which protein consists of the amino acid sequence Pro-Tyr-Gly-Ala-Asn-Met-Glu-Asp-Ser-Val-Cys-Cys-Arg (SEQ ID NO:2), which derivative has activity to enhance the efficacy of the vaccine. In yet another specific embodiment, the chemokine is a purified derivative of the protein, which derivative has one or more insertions of or substitutions with one or more non-classical amino acids relative to a corresponding wildtype chemokine, which derivative will enhance the efficacy of the vaccine. In yet another specific embodiment, the chemokine is a purified derivative of the protein that has only one or more conservative substitutions in sequence relative a corresponding wildtype chemokine, which derivative will enhance the efficacy of the vaccine. The chemokines useful in the present invention may be derived from any suitable source and obtained by any method known in the art, for example but not limited to the methods described in Section 5.2 infra. Preferably, the chemokine(s) are of the same species as the subject to which the vaccine is administered. In a preferred embodiment, one or more human chemokines are administered to a human subject, e.g., human MDC is administered to a human subject, alone or in combination with another chemokine. The present invention also provides a method to enhance the efficacy of a vaccine in a subject, which method comprises administering to a subject a purified first nucleic acid comprising a nucleotide sequence encoding an antigen against which an immune response is desired in a subject and a purified second nucleic acid comprising a nucleotide sequence encoding one or more chemokines, or fragment(s), derivative(s) or analogue(s) thereof, where the expression of the encoded antigen(s) and chemokine(s), or fragment(s), derivative(s) or analogue(s) thereof, are under control of one or more appropriate gene regulatory elements (which regulatory elements can be any regulatory element known in the art, for example, but not limited to, those regulatory elements described in Section 5.2 supra), such that, upon introduction of said first and second nucleic acids into a suitable cell (e.g., a cell of the subject), the antigen and chemokine(s), or fragment(s), derivative(s) or analogue(s) thereof, are coordinately expressed, i.e., are expressed either at the same time or within an appropriate time period (i.e., sufficient for the chemokine(s) to enhance the immune response against the antigen relative to a corresponding immune response in the absence of the chemokine) and the antigen(s) are expressed in an immunogenic amount and the chemokine(s), or fragment(s), derivative(s) or analogue(s) thereof, are expressed in an amount sufficient to enhance the immune response against the antigen(s). In a specific embodiment, the nucleotide sequences encoding the chemokine(s) and the antigen are present on separate nucleic acids. In another embodiment, the nucleotide sequences encoding the chemokine(s) and the antigen(s) are present on the same nucleic acid. The present invention also provides compositions to enhance the efficacy of a vaccine in a subject, which compositions comprise a purified first nucleic acid comprising a nucleotide sequence encoding one or more antigen(s) and a purified second nucleic acid comprising a nucleotide sequence encoding one or more chemokines, or fragments or derivatives, including truncation isoforms, thereof, wherein the nucleotide sequences encoding the antigens and the chemokine(s) are operably linked to one or more gene regulatory elements such that, upon introduction of said first and second nucleic acids into a suitable cell (e.g., a cell of the subject), the antigen(s) and chemokine(s) are expressed in a coordinated manner and the antigen(s) are expressed in an immunogenic amount and the chemokine(s) are expressed in an amount effective to enhance the immune response against the antigen, relative to a corresponding immune response in the absence of such chemokine(s). The present invention also provides compositions to enhance the efficacy of a vaccine in a subject, which compositions comprise a purified first set of one or more purified nucleic acids comprising one or more nucleotide sequences encoding one or more antigens and a purified second set of one or more purified nucleic acids comprising a nucleotide sequence encoding one or more chemokines, or fragments, analogues, derivatives, (including truncation isoforms) thereof, wherein the nucleotide sequence(s) encoding the antigen(s) and the chemokine(s) are operably linked to one or more gene regulatory elements such that, upon introduction of said first and second sets of nucleic acids into a suitable cell (e.g., a cell of the subject), the antigen(s) and chemokine(s) are expressed in a coordinated manner and the antigen(s) are expressed in an immunogenic amount and the chemokine(s) are expressed in an amount effective to enhance the immune response against the antigen, relative to a corresponding immune response in the absence of such chemokine(s). The present invention also provides compositions to enhance the efficacy of a vaccine in a subject, which compositions comprise a purified nucleic acid comprising a first set of one or more nucleotide sequences encoding one or more antigens and a second set of one ore more nucleotide sequence encoding one or more chemokines, or fragments, derivatives, or analogues thereof (including truncation isoforms), wherein the first and second sets of nucleotide sequences are operably linked to one or more gene regulatory elements such that, upon introduction into a suitable cell, the antigen(s) and the chemokine(s) are expressed in a coordinated manner and the antigen(s) are expressed in an immunogenic amount and the chemokine(s) are expressed in an amount effective to enhance the immune response against the antigen(s). Any nucleic acid comprising a nucleotide sequence encoding one or more chemokine proteins, or fragments or derivatives, thereof (including truncation isoforms), that are capable of enhancing the immune response to the antigen (for example, but not limited to, as determined by any of the assays described in Section 5.2., infra) can be used in the methods and compositions of the present invention. In a preferred embodiment, the nucleotide sequence encodes MDC. In another embodiment, the MDC-encoding nucleotide consists of the nucleotide sequence of SEQ ID NO:1 (Figure 1 A). In another specific embodiment, the method or composition of the invention uses a nucleic acid encoding an MDC derivative having deletional, insertional or substitutional mutations and combination thereof, which derivative has activity to enhance the immune response against an antigen in a subject. Such compositions of nucleic acids encoding an antigen are often referred to as DNA vaccines. Such DNA vaccines are produced by any method known in the art for constructing an expression plasmid vector containing the nucleotide sequences of the antigen(s) and/or chemokine(s) to be expressed which vector is suitable for expression of the encoded proteins in the subject or in cells recombinant for the expression vector, which cells are to be provided to the subject. Such expression vectors may contain various promoters, terminators and polyadenylation coding regions to control the expression of the encoded protein. The DNA vaccine can be administered by any method known in the art for administration of DNA. The DNA vaccine may be delivered either directly, in which case the subject is directly exposed to the DNA vaccine such that the DNA enters and is expressed in cells of the subject, or indirectly, in which case, the DNA vaccine is first introduced into suitable cells by any method known in the art in vitro, then the cells containing the DNA vaccine are transplanted into the subject. In a specific embodiment, the DNA vaccine is directly administered in vivo, where it is expressed to produce the encoded antigens and chemokine(s). This can be accomplished by any of numerous methods known in the art, e.g., by constructing it as part of an appropriate nucleic acid expression vector and administering it so that it becomes intracellular, e.g., by infection using a defective or attenuated retroviral or other viral vector (see U.S. Patent No. 4,980,286), or by direct injection of naked DNA, or by use of microparticle bombardment (e.g., a gene gun; Biolistic, Dupont), or coating with lipids or cell-surface receptors or transfecting agents, encapsulation in liposomes, microparticles, or microcapsules, or by administering it in linkage to a peptide which is known to enter the nucleus, by administering it in linkage to a ligand subject to receptor-mediated endocytosis (see e.g., Wu and Wu, /. Biol. Chem. 262:4429-4432 (1987)) (which can be used to target cell types specifically expressing the receptors), etc. In another embodiment, a nucleic acid-ligand complex can be formed in which the ligand comprises a fusogenic viral peptide to disrupt endosomes, allowing the nucleic acid to avoid lysosomal degradation. In a preferred embodiment, the nucleic acid of a DNA vaccine is injected into the muscle of the subject to be immunized. Another approach is to introduce the nucleic acid of the DNA vaccine into a cell prior to administration in vivo of the resulting recombinant cell. Such introduction can be carried out by any method known in the art, including but not limited to transfection, electroporation, microinjection, infection with a viral or bacteriophage vector containing the nucleic acid sequences, cell fusion, chromosome-mediated gene transfer, microcell-mediated gene transfer, spheroplast fusion, etc. Numerous techniques are known in the art for the introduction of foreign nucleic acid into cells (see e.g., Loeffler and Behr, Meth. Enzymol. 217:599-618 (1993); Cohen et al., Meth. Enzymol. 217:618-644 (1993); Cline, Pharmac. Ther. 29:69-92 (1985)) and may be used in accordance with the present invention. Usually, the method of transfer includes the transfer of a selectable marker to the cells. The cells are then placed under selection to isolate those cells that have taken up and are expressing the transferred gene. Cells into which a DNA vaccine can be introduced for purposes of immunization encompass any desired, available cell type, and include but are not limited to epithelial cells, endothelial cells, keratinocytes, fibroblasts, muscle cells, hepatocytes; blood cells such as T lymphocytes, B lymphocytes, monocytes, macrophages, neutrophils, eosinophils, megakaryocytes, granulocytes; various stem or progenitor cells, in particular hematopoietic stem or progenitor cells, e.g., as obtained from bone marrow, umbilical cord blood, peripheral blood, fetal liver, etc. The resulting recombinant cells can be delivered to a subject by various methods known in the art. In a preferred embodiment, the recombinant cells are injected, e.g., subcutaneously. In another embodiment, recombinant skin cells may be applied as a skin graft onto the patient. Recombinant blood cells (e.g., hematopoietic stem or progenitor cells) are preferably administered intravenously. The cells can also be encapsulated in a suitable vehicle and then implanted in the subject (see, e.g., Dionne et al. PCT Publication WO 92/19195, dated November 12, 1992). The amount of cells envisioned for use depends on the desired effect, subject state, etc., and can be determined by one skilled in the art. By way of example, and not by way of limitation a DNA vaccine may be generated as described by Lekutis et al. for an HIV DNA vaccine (1997, /. Immunol. 158:4471-4477). Briefly, an expression vector is constructed with the promoter, enhancer and intron A of human cytomegalovirus (CMV) and the termination and polyadenylation sequences of bovine growth hormone in a plasmid backbone. Additionally, the nucleotide sequence for signal sequence of tissue plasminogen activator is either substituted for the signal sequence of the antigen, if the antigen has a signal sequence or is added onto the amino-terminus of the antigen, thereby eliminating the dependence on viral proteins for expression (e.g., in the case of gp120 expression, rev and env proteins are required unless the HIV-1 signal sequence is so substituted). The resulting formulation is then injected intra-muscularly. Further examples of DNA vaccines are set forth in Boyer et al. (1996, /. Med. Primatol., 25:242-250), which describes the construction of a plasmid encoding the HIV-1 gp160 envelope glycoprotein as well as the rev-tax region cloned into pMAMneoBlue vector (Clonetech, Inc., Palo Alto, CA), and a vector encoding the envelope glycoprotein and rev from HIV-1 strain MN under the control of the CMV promoter. Another vector which can be used in the present invention is as described in Boyer et al. (1997, Nature Medicine 3:526-532) and contains expression cassettes encoding the envelope and Rev proteins of HIV-1 strain MN, and encoding the Gag/Pol proteins of HIV-1 strain 1MB. For the practice of the present invention, the nucleotide sequence for the one or more chemokines, or fragments, derivatives, or analogues thereof, can either be incorporated into the same expression vector containing the nucleotide sequence encoding the antigen in such a manner that the chemokine(s) are expressed. Alternatively, the nucleotide sequence encoding the chemokine(s), or fragment(s), derivative(s) or analogue(s) thereof, can be cloned into a separate expression vector (e.g., as described above for the expression vector containing the sequences coding for antigen) and the expression vector that expresses the antigen(s) mixed with the expression vector that expresses the chemokine(s). The mixture of the two expression vectors can then be administered to the subject. The methods and compositions of the present invention may be used as a vaccine in a subject in which immunity for the antigen(s) is desired. Such antigens can be any antigen known in the art to be useful in a vaccine formulation. The methods and compositions of the present invention can be used to enhance the efficacy of any vaccine known in the art. The vaccine of the present invention may be used to enhance an immune response to infectious agents and diseased or abnormal cells, such as but not limited to bacteria, parasites, fungi, viruses, tumors and cancers. The compositions of the invention may be used to either treat or prevent a disease or disorder amenable to treatment or prevention by generating an immune response to the antigen provided in the composition. In one preferred embodiment, the antigen(s) are proteins, fragments or derivatives, including truncation isoforms, thereof, encoded by any genes of the HIV genome including the env, gag, pol, nef, vif, rev, and tat genes. In a more preferred embodiment, the antigen is an HIV-associated gp120 protein. The methods and compositions of the present invention may be used to elicit a humoral and/or a cell-mediated response against the antigen(s) of the vaccine in a subject. In one specific embodiment, the methods and compositions elicit a humoral response against the administered antigen in a subject. In another specific embodiment, the methods and compositions elicit a cell-mediated response against the administered antigen in a subject. In a preferred embodiment, the methods and compositions elicit both a humoral and a cell-mediated response. The subjects to which the present invention is applicable may be any mammalian or vertebrate species, which include, but are not limited to, cows, horses, sheep, pigs, fowl (e.g., chickens), goats, cats, dogs, hamsters, mice and rats, monkeys, rabbits, chimpanzees, and humans. In a preferred embodiment, the subject is a human. The compositions and methods of the invention can be used to either prevent a disease or disorder, or to treat a particular disease or disorder, where an immune response against a particular antigen or antigens is effective to treat or prevent the disease or disorder. Such diseases and disorders include, but are not limited to, viral infections, such as HIV, CMV, hepatitis, herpes virus, measles, etc, bacterial infections, fungal and parasitic infections, cancers, and any other disease or disorder amenable to treatment or prevention by eliciting an immune response against a particular antigen or antigens. In another preferred embodiment, the subject is infected or at risk of being infected with HIV virus. In another preferred embodiment the invention provides methods and compositions to enhance the efficacy of an HIV vaccine, such a vaccine can be administered to either prevent or treat HIV. 5.2. CHEMOKINE GENES AND PROTEINS Chemokine proteins and nucleic acids can be obtained by any method known in the art. Chemokine nucleotide and amino acid sequences are available in public databases such as Genbank and are also published in various references known to those of skill in the art. The gene bank accession numbers for the preferred chemokines of the present invention are provided in Table I, in Section 5 above. The ensuing discussion uses MDC by way of example, but applies equally to other chemokines as well. The MDC nucleotide and amino acid sequences for, inter alia, human, are available in the public databases (e.g. Genbank accession No. U83171) also published in Godiska et al., 1997, /. Exp. Med. 185:1595-1604. The nucleotide sequence and the amino acid sequence for the human MDC are provided in Figures 1 A and B (SEQ ID NOS:1 and 2, respectively). Chemokines used herein include, but are not limited to, chemokines from mice, hamsters, dogs, cats, monkeys, rabbits, chimpanzees, and human. In one preferred embodiment, the chemokine is of human origin. Any vertebrate cell potentially can serve as the nucleic acid source for the isolation of chemokine nucleic acids. The nucleic acid sequences encoding the chemokine(s) can be isolated from vertebrate, mammalian, human, porcine, bovine, feline, avian, equine, canine, as well as additional primate sources, etc. The DNA may be obtained by standard procedures known in the art from cloned DNA (e.g., a DNA "library"), by chemical synthesis, by cDNA cloning, or by the cloning of genomic DNA, or fragments thereof, purified from the desired cell (see, for example, Sambrook et al., 1989, Molecular Cloning, A Laboratory Manual, 2d Ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York; Glover, D.M. (ed.), 1985, DNA Cloning: A Practical Approach, MRL Press, Ltd., Oxford, U.K. Vol. I, II.) Clones derived from genomic DNA may contain regulatory and intron DNA regions in addition to coding regions; clones derived from cDNA will contain only exon sequences. Whatever the source, the gene should be molecularly cloned into a suitable vector for propagation of the gene. In the molecular cloning of the gene from cDNA, cDNA is generated from totally cellular RNA or mRNA by methods that are well known in the art. The gene may also be obtained from genomic DNA, where DNA fragments are generated (e.g. using restriction enzymes or by mechanical shearing), some of which will encode the desired gene. The linear DNA fragments can then be separated according to size by standard techniques, including but not limited to, agarose and polyacrylamide gel electrophoresis and column chromatography. Once the DNA fragments are generated, identification of the specific DNA fragment containing all or a portion of the chemokine gene may be accomplished in a number of ways. A preferred method for isolating a chemokine gene is by the polymerase chain reaction (PCR), which can be used to amplify the desired chemokine sequence in a genomic or cDNA library or from genomic DNA or cDNA that has not been incorporated into a library. Oligonucleotide primers which would hybridize to chemokine sequences can be used as primers in PCR. Additionally, a portion of the chemokine (of any species) gene or its specific RNA, or a fragment thereof, can be purified (or an oligonucleotide synthesized) and labeled, the generated DNA fragments may be screened by nucleic acid hybridization to the labeled probe (Benton, W. and Davis, R., 1977, Science 196: 180; Grunstein, M. And Hogness, D., 1975, Proc. Natl. Acad. Sci. U.S.A. 72:3961 ). Those DNA fragments with substantial homology to the probe will hybridize. Chemokine nucleic acids can be also identified and isolated by expression cloning using, for example, anti-chemokine antibodies for selection. Alternatives to obtaining the chemokine DNA by cloning or amplification include, but are not limited to, chemically synthesizing the gene sequence itself from the known chemokine sequence or making cDNA to the mRNA which encodes the chemokine protein. Other methods are possible and within the scope of the invention. Once a clone has been obtained, its identity can be confirmed by nucleic acid sequencing (by any method well known in the art) and comparison to known chemokine sequences. DNA sequence analysis can be performed by any techniques known in the art, including but not limited to the method of Maxam and Gilbert (1980, Meth. Enzymol. 65:499-560), the Sanger dideoxy method (Sanger, F., et al., 1977, Proc. Natl. Acad. Sci. U.S.A. 74:5463), the use of T7 DNA polymerase (Tabor and Richardson, U.S. Patent No. 4,795,699), use of an automated DNA sequenator (e.g., Applied Biosystems, Foster City, CA) or the method described in PCT Publication WO 97/ 15690. Nucleic acids which are hybridizable to a chemokine nucleic acid, or to a nucleic acid encoding a chemokine derivative can be isolated, by nucleic acid hybridization under conditions of low, high, or moderate stringency (see also Shilo and Weinberg, 1981 , Proc. Natl. Acad. Sci. USA 78:6789-6792). For example, the nucleic acid of SEQ ID No: 1 is hybridizable to an MDC nucleic acid. Chemokine proteins and derivatives, analogs and fragments of chemokine proteins can be obtained by any method known in the art, including but not limited to recombinant expression methods, purification from natural sources, and chemical synthesis. For example, chemokines can be obtained by recombinant protein expression techniques. For recombinant expression, the chemokine gene or portion thereof is inserted into an appropriate cloning vector for expression in a particular host cell. A large number of vector-host systems known in the art may be used. Possible vectors include, but are not limited to, plasmids or modified viruses, but the vector system must be compatible with the host cell used. Such vectors include, but are not limited to, bacteriophages such as lambda derivatives, or plasmids such as pBR322 or pUC plasmid derivatives or the Bluescript vector (Stratagene). The insertion into a cloning vector can, for example, be accomplished by ligating the DNA fragment into a cloning vector which has complementary cohesive termini. However, if the complementary restriction sites used to fragment the DNA are not present in the cloning vector, the ends of the DNA molecules may be enzymatically modified. Alternatively, any site desired may be produced by ligating nucleotide sequences (linkers) onto the DNA termini; these ligated linkers may comprise specific chemically synthesized oligonucleotides encoding restriction endonuclease recognition sequences. In an alternative method, the cleaved vector and chemokine gene may be modified by homopolymeric tailing. Recombinant molecules can be introduced into host cells via transformation, transfection, infection, electroporation, etc., so that many copies of the gene sequence are generated. In an alternative method, the desired gene may be identified and isolated after insertion into a suitable cloning vector in a "shot gun" approach. Enrichment for the desired gene, for example, by size fractionation, can be done before insertion into the cloning vector. In specific embodiments, transformation of host cells with recombinant DNA molecules that incorporate the isolated chemokine gene, cDNA, or synthesized DNA sequence enables generation of multiple copies of the gene. Thus, the gene may be obtained in large quantities by growing transformants, isolating the recombinant DNA molecules from the transformants and, when necessary, retrieving the inserted gene from the isolated recombinant DNA. The nucleotide sequence coding for a chemokine protein or a functionally active analog or fragment or other derivative thereof, can be inserted into an appropriate expression vector, i.e., a vector which contains the necessary elements for the transcription and translation of the inserted protein-coding sequence. The necessary transcriptional and translational signals can also be supplied by the native chemokine gene and/or its flanking regions. A variety of host-vector systems may be utilized to express the protein-coding sequence. These include but are not limited to mammalian cell systems infected with virus (e.g., vaccinia virus, adenovirus, etc.); insect cell systems infected with virus (e.g., baculovirus); microorganisms such as yeast containing yeast vectors, or bacteria transformed with bacteriophage, DNA, plasmid DNA, or cosmid DNA. The expression elements of vectors vary in their strengths and specificities. Depending on the host-vector system utilized, any one of a number of suitable transcription and translation elements may be used. Any of the methods previously described for the insertion of DNA fragments into a vector may be used to construct expression vectors containing a chimeric gene consisting of appropriate transcriptional/translational control signals and the protein coding sequences. These methods may include in vitro recombinant DNA and synthetic techniques and in vivo recombinants (genetic recombination). Expression of nucleic acid sequence encoding a chemokine protein or peptide fragment may be regulated by a second nucleic acid sequence so that the chemokine protein or peptide is expressed in a host transformed with the recombinant DNA molecule. For example, expression of a chemokine protein may be controlled by any promoter/enhancer element known in the art. Promoters which may be used to control chemokine expression include, but are not limited to, the SV40 early promoter region (Bernoist and Chambon, 1981 , Nature 290:304-310), the promoter contained in the 3' long terminal repeat of Rous sarcoma virus (Yamamoto, et al., 1980, Cell 22:787-797), the herpes thymidine kinase promoter (Wagner et al., 1981 , Proc. Natl. Acad. Sci. U.S.A. 78:1441-1445), the regulatory sequences of the metallothionein gene (Brinster et al., 1982, Nature 296:39-42); prokaryotic expression vectors such as the β-lactamase promoter (Villa-Kamaroff, et al., 1978, Proc. Natl. Acad. Sci. U.S.A. 75:3727-3731 ), or the tac promoter (DeBoer, et al., 1983, Proc. Natl. Acad. Sci. U.S.A. 80:21-25); see also "Useful proteins from recombinant bacteria" in Scientific American, 1980, 242:74-94; promoter elements from yeast or other fungi such as the Gal 4 promoter, the ADC (alcohol dehydrogenase) promoter, PGK (phosphoglycerol kinase) promoter, alkaline phosphatase promoter, and the following animal transcriptional control regions, which exhibit tissue specificity and have been utilized in transgenic animals: elastase I gene control region which is active in pancreatic acinar cells (Swift et al., 1984, Cell 38:639-646; Ornitz et al., 1986, Cold Spring Harbor Symp. Quant. Biol. 50:399-409; MacDonald, 1987, Hepatology 7:425-515); insulin gene control region which is active in pancreatic beta cells (Hanahan, 1985, Nature 315:1 15-122), immunoglobulin gene control region which is active in lymphoid cells (Grosschedl et al., 1984, Cell 38:647-658; Adames et al., 1985, Nature 318:533-538; Alexander et al., 1987, Mol. Cell. Biol. 7:1436-1444), mouse mammary tumor virus control region which is active in testicular, breast, lymphoid and mast cells (Leder et al., 1986, Cell 45:485-495), albumin gene control region which is active in liver (Pinkert et al., 1987, Genes and Devel. 1 :268-276), alpha-fetoprotein gene control region which is active in liver (Krumlauf et al., 1985, Mol. Cell. Biol. 5:1639-1648; Hammer et al., 1987, Science 235:53-58; alpha 1-antitrypsin gene control region which is active in the liver (Kelsey et al., 1987, Genes and Devel. 1 :161 -1 71 ), beta-globin gene control region which is active in myeloid cells (Mogram et al., 1985, Nature 315:338-340; Kollias et al., 1986, Cell 46:89-94), myelin basic protein gene control region which is active in oligodendrocyte cells in the brain (Readhead et al., 1987, Cell 48:703-712), myosin light chain-2 gene control region which is active in skeletal muscle (Sani, 1985, Nature 314:283-286), and gonadotropic releasing hormone gene control region which is active in the hypothalamus (Mason et al., 1986, Science 234:1372-1378). For example, a vector can be used that comprises a promoter operably linked to an chemokine-encoding nucleic acid, one or more origins of replication, and, optionally, one or more selectable markers (e.g., an antibiotic resistance gene). In a specific embodiment, an expression construct is made by subcloning a chemokine coding sequence into the EcoRI restriction site of each of the three pGEX vectors (Glutathione S-Transferase expression vectors; Smith and Johnson, 1988, Gene 7:31 -40). This allows for the expression of the chemokine protein product from the subclone in the correct reading frame. Expression vectors containing chemokine gene inserts can be identified by three general approaches: (a) nucleic acid hybridization, (b) presence or absence of "marker" gene functions, and (c) expression of inserted sequences. In the first approach, the presence of a chemokine gene inserted in an expression vector can be detected by nucleic acid hybridization using probes comprising sequences that are homologous to an inserted chemokine gene. In the second approach, the recombinant vector/host system can be identified and selected based upon the presence or absence of certain "marker" gene functions (e.g., thymidine kinase activity, resistance to antibiotics, transformation phenotype, occlusion body formation in baculovirus, etc.) caused by the insertion of a chemokine gene in the vector. For example, if the chemokine gene is inserted within the marker gene sequence of the vector, recombinants containing the chemokine insert can be identified by the absence of the marker gene function. In the third approach, recombinant expression vectors can be identified by assaying the product expressed by the recombinant. Such assays can be based, for example, on the physical or functional properties of the chemokine protein in in vitro assay systems, e.g., binding with anti-chemokine antibody or the chemokine's receptor. Once a particular recombinant DNA molecule is identified and isolated, several methods known in the art may be used to propagate it. Once a suitable host system and growth conditions are established, recombinant expression vectors can be propagated and prepared in quantity. As previously explained, the expression vectors which can be used include, but are not limited to, the following vectors or their derivatives: human or animal viruses such as vaccinia virus or adenovirus; insect viruses such as baculovirus; yeast vectors; bacteriophage vectors (e.g., lambda), and plasmid and cosmid DNA vectors, to name but a few. In addition, a host cell strain may be chosen which modulates the expression of the inserted sequences, or modifies and processes the gene product in the specific fashion desired. Expression from certain promoters can be elevated in the presence of certain inducers; thus, expression of the genetically engineered protein may be controlled. Furthermore, different host cells have characteristic and specific mechanisms for the translational and post-translational processing and modification (e.g., glycosylation, phosphorylation of proteins. Appropriate cell lines or host systems can be chosen to ensure the desired modification and processing of the foreign protein expressed. For example, expression in a bacterial system can be used to produce an unglycosylated core protein product. Expression in yeast will produce a glycosylated product. Expression in mammalian cells can be used to ensure "native" glycosylation of a heterologous protein. Furthermore, different vector/host expression systems may effect processing reactions to different extents. In other specific embodiments, the chemokine protein(s), fragment(s), analogue(s), or derivative(s) may be expressed as a fusion, or chimeric protein product (comprising the protein, fragment, analog, or derivative joined via a peptide bond to a heterologous protein sequence (of a different protein)). Such a chimeric product can be made by ligating the appropriate nucleic acid sequences encoding the desired amino acid sequences to each other by methods known in the art, in the proper coding frame, and expressing the chimeric product by methods commonly known in the art. Alternatively, such a chimeric product may be made by protein synthetic techniques, e.g., by use of a peptide synthesizer. In a specific embodiment, a chimeric protein containing all or a portion of the chemokine is joined via a peptide bond to all or a portion of an antigen against which immunity is desired. Both cDNA and genomic sequences can be cloned and expressed. The chemokine protein(s) may also be isolated and purified by standard methods including chromatography (e.g., ion exchange, affinity, and sizing column chromatography), centrifugation, differential solubility, or by any other standard technique for the purification of proteins. The functional properties may be evaluated using any suitable assay (see Section 5.5). Alternatively, the protein can be synthesized by standard chemical methods known in the art (e.g., see Hunkapiller, M., et al., 1984, Nature 310:105-1 1 1). The chemokine-encoding nucleic acid sequence(s) can be mutated in vitro or in vivo, to create and/or destroy translation, initiation, and/or termination sequences, or to create variations in coding regions. Any technique for mutagenesis known in the art can be used, including, but not limited to, in vitro site-directed mutagenesis (Hutchinson et al., 1978, /. Biol. Chem 253:6551 ), use of TAB linkers (Pharmacia), mutation-containing PCR primers, etc. The experimentation involved in mutagenesis consists primarily of site-directed mutagenesis followed by phenotypic testing of the altered gene product. Some of the more commonly employed site-directed mutagenesis protocols take advantage of vectors that can provide single stranded as well as double stranded DNA, as needed. Generally, the mutagenesis protocol with such vectors is as follows. A mutagenic primer, i.e., a primer complementary to the sequence to be changed, but consisting of one or a small number of altered, added, or deleted bases, is synthesized. The primer is extended in vitro by a DNA polymerase and, after some additional manipulations, the now double-stranded DNA is transfected into bacterial cells. Next, by a variety of methods, the desired mutated DNA is identified, and the desired protein is purified from clones containing the mutated sequence. For longer sequences, additional cloning steps are often required because long inserts (longer than 2 kilobases) are unstable in those vectors. Protocols are known to these skilled in the art and kits for site-directed mutagenesis are widely available from biotechnology supply companies, for example from Amersham Life Science, Inc. (Arlington Heights, IL) and Stratagene Cloning Systems (La Jolla, CA). In other specific embodiments, the chemokine derivative(s) or analogue(s) may be expressed as a fusion, or chimeric protein product (comprising the protein, fragment, analogue, or derivative joined via a peptide bond to a heterologous protein sequence (of a different protein)). Such a chimeric product can be made by ligating the appropriate nucleic acid sequences encoding the desired amino acid sequences to each other by methods known in the art, in the proper coding frame, and expressing the chimeric product by methods commonly known in the art. In addition, chemokine proteins, derivatives (including fragments and chimeric proteins), and analogues can be chemically synthesized. See, e.g., Clark-Lewis et al., 1991 , Biochem. 30:3128-3135 and Merrifield, 1963, /. Amer. Chem. Soc. 85:2149- 2156. For example, chemokines, derivatives and analogues can be synthesized by solid phase techniques, cleaved from the resin, and purified by preparative high performance liquid chromatography (e.g., see Creighton, 1983, Proteins, Structures and Molecular Principles, W.H. Freeman and Co., N.Y., pp. 50-60). Chemokines, derivatives and analogues that are proteins can also be synthesized by use of a peptide synthesizer. The composition of the synthetic peptides may be confirmed by amino acid analysis or sequencing (e.g., the Edman degradation procedure; see Creighton, 1983, Proteins, Structures and Molecular Principles, W.H. Freeman and Co., N.Y., pp. 34-49). The chemokine proteins, derivatives, or analogues of the invention may be synthesized in their entirety by the sequential addition of amino acid residues or alternatively as fragment subcomponents which may be combined using techniques well known in the art, such as, for example, fragment condensation (Shin et al., 1992, Biosci. Biotech. Biochem. 56:404-408; Nyfeler et al., 1992, Peptides, Proc. 12th Amer. Pep. Soc, Smith and Rivier (eds), Leiden, pp 661 -663); and Nokihara et al., 1990, Protein Research Foundation, Yanaihara (ed), Osaka, pp 315-320). In a less preferred embodiment, chemokine derivatives can be obtained by proteolysis of the protein followed by purification using standard methods such as those described above (e.g., immunoaffinity purification). In another alternate embodiment, native chemokine proteins can be purified from natural sources, by standard methods such as those described above (e.g., immunoaffinity purification). 5.3. COMPOSITION FORMULATIONS AND METHODS OF ADMINISTRATION The composition formulations of the invention comprise an effective immunizing amount of an immunologically active ingredient, i.e., one or more antigens, and an amount of one or more chemokine(s), or fragment(s) or derivative thereof, effective to enhance the immune response against the antigen in a subject, and a pharmaceutically acceptable carrier or excipient. In a specific embodiment, the chemokines are selected from the group consisting of Macrophage-derived chemokine, Monocyte chemotactic protein 1 , Monocyte chemotactic protein 2, Monocyte chemotactic protein 3, Monocyte chemotactic protein 4, activated macrophage specific chemokine 1 , Macrophage inflammatory protein 1 alpha, Macrophage inflammatory protein 1 beta, Macrophage inflammatory protein 1 gamma, Macrophage inflammatory protein 1 delta, Macrophage inflammatory protein 2 alpha, Macrophage inflammatory protein 3 alpha, Macrophage inflammatory protein 3 beta, Regulated upon activation, normal T cell expressed and secreted (and its variants), I-309, EBI1- ligand chemokine, Pulmonary and activation regulated chemokine, Liver and activation-regulated chemokine, Thymus and activation regulated chemokine, Eotaxin (and variants), Human CC chemokine 1 , Human CC chemokine 2, Human CC chemokine 3, IL-10-inducible chemokine, liver-expressed chemokine, 6Ckine, Exodus 1 , Exodus 2, Exodus 3, thymus-expressed chemokine, Secondary Lymphoid tissue chemokine, Lymphocyte and Monocyte chemoattractant; Monotactin, Activation- induced, chemokine-related molecule, Myeloid progenitor inhibitory factor-1 , Myeloid progenitor inhibitory factor-2, Stromal cell-derived factor 1 alpha, Stromal cell-derived factor 1 beta, B-cell-attracting chemokine 1 , HuMIG, H 1 74, Interferon-stimulated T- cell alpha chemoattractant, lnterleukin-8, IP-10, platelet factor 4, growth-regulated gene-alpha, growth-regulated gene-beta, growth-regulated gene-gamma, Neutrophil- activating protein 2, ENA-78, granulocyte chemotactic protein 2, LYMPHOTACTIN, and Fractalkine/neurotactin. Pharmaceutically acceptable carriers or excipients are well known in the art and include but are not limited to saline, buffered saline, dextrose, water, glycerol, ethanol, sterile isotonic aqueous buffer, and combinations thereof. One example of such an acceptable carrier is a physiologically balanced culture medium containing one or more stabilizing agents such as stabilized, hydrolyzed proteins, lactose, etc. The carrier is preferably sterile. The formulation should suit the mode of administration. In addition, if desired, the vaccine or composition preparation may also include minor amounts of auxiliary substances such as wetting or emulsifying agents, pH buffering agents, and/or adjuvants which enhance the effectiveness of the vaccine or composition. Suitable adjuvants may include, but are not limited to: mineral gels, e.g., aluminum hydroxide; surface active substances such as lysolecithin, pluronic polyols; polyanions; peptides; oil emulsions; alum, MDP, N-acetyl-muramyl-L- threonyl-D-isoglutamine (thr-MDP), N-acetyl-nor-muramyl-L-alanyl-D-isoglutamine, and N-acetylmuramyl-L-alanyl-D-isoglutaminyl-L-alanine-2-(1 '-2'-dipalmitoyl-sn- glycero-3-hydroxyphosphoryloxy)-ethylamine. The effectiveness of an adjuvant may be determined by comparing the induction of antibodies directed against a MDC- containing composition in the presence and in the absence of various adjuvants. In instances where the recombinant antigen is a hapten, i.e., a molecule that is antigenic in that it can react selectively with cognate antibodies, but not immunogenic in that it cannot elicit an immune response, the hapten may be covalently bound to a carrier or immunogenic molecule; for instance, a large protein such as serum albumin will confer immunogenicity to the hapten coupled to it. The hapten-carrier may be formulated for use as a vaccine. The composition can be a liquid solution, suspension, emulsion, tablet, pill, capsule, sustained release formulation, or powder. Oral formulation can include standard carriers such as pharmaceutical grades of mannitol, lactose, starch, magnesium stearate, sodium saccharine, cellulose, magnesium carbonate, etc. The chemokine(s), or fragment(s) or derivative(s) thereof, and/or the antigen(s) may be formulated into the 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 organic acids such as acetic, oxalic, tartaric, maleic, and the like. Salts formed with free carboxyl groups may also be derived from inorganic bases, such as, for example, sodium potassium, ammonium, calcium, or ferric hydroxides, and such organic bases as isopropylamine, trimethylamine, 2- ethylamino ethanol, histidine, procaine and the like. The vaccines of the invention may be multivalent or univalent. Multivalent vaccines are made from recombinant viruses that direct the expression of more than one antigen. An effective dose (immunizing amount) is that amount sufficient to produce an immune response to the antigen(s) in the host to which the vaccine preparation is administered. The precise dose of the composition to be employed in the formulation will depend on the route of administration, and the nature of the subject to be immunized, and should be decided by the practitioner according to standard clinical techniques. Effective doses of the vaccines or compositions of the present invention may also be extrapolated from dose-response curves derived from animal model test systems. The invention also provides a pharmaceutical pack or kit comprising one or more containers comprising one or more of the ingredients of the composition formulations of the invention. Associated with such container(s) can be a notice in the form prescribed by a governmental agency regulating the manufacture, use or sale of pharmaceuticals or biological products, which notice reflects approval by the agency of manufacture, use or sale for human administration. Generally, the ingredients are supplied either separately or mixed together in unit dosage form, for example, as a dry lyophilized powder or water free concentrate in a hermetically sealed container such as an ampoule or sachette indicating the quantity of active agent. Where the composition is administered by injection, an ampoule of sterile diluent can be provided so that the ingredients may be mixed prior to administration. In a specific embodiment, a lyophilized immunologically active ingredient and one or more chemokine polypeptide(s) of the invention are provided in a first container; a second container comprises diluent consisting of an aqueous solution of 507o glycerin, 0.25% phenol, and an antiseptic (e.g., 0.005% brilliant green). Many methods may be used to introduce the composition formulations of the invention; these include but are not limited to oral, intradermal, intramuscular, intraperitoneal, intravenous, subcutaneous, intranasal routes, and via scarification (scratching through the top layers of skin, e.g., using a bifurcated needle). The DNA vaccines of the invention can be administered by any method known in the art for delivery of DNA to subject (for example, as described in Section 5.3 supra) 5.4. DETERMINATION OF COMPOSITION EFFICACY The activity of one or more chemokines, or a fragment, derivative or analogue thereof, to enhance immune response to an antigen can be determined by monitoring the immune response in test animals following immunization with a composition containing the chemokine(s) and an antigen and comparing the response to that following immunization with the antigen in the absence of the chemokine(s). Generation of a humoral (antibody) response and/or cell-mediated immunity, may be taken as an indication of an immune response. Test animals may include mice, hamsters, dogs, cats, monkeys, rabbits, chimpanzees, etc., and eventually human subjects. Assays for humoral and cell-mediated immunity are well known in the art. Methods of introducing the composition may include oral, intracerebral, intradermal, intramuscular, intraperitoneal, intravenous, subcutaneous, intranasal or any other standard routes of immunization. The immune response of the test subjects can be analyzed by various approaches well known in the art, such as but not limited to: testing the reactivity of the resultant immune serum to the antigen of the chemokine-containing vaccine, as assayed by known techniques, e.g., immunosorbant assay (ELISA), immunoblots, radioimmunoprecipitations, etc. As one example of suitable animal testing, a composition of the present invention may be tested in mice for the ability to enhance an antibody response to an antigen (using for example, but not limited to, the method as described in Section 6, infra) and the delayed-type hypersensitivity (DTH) response (also described in Section 6 infra), measured by an increase in footpad swelling after inoculation in the footpad of the test animal, as compared to the measurements in animals administered the antigen in a composition not containing chemokine. For example, as test animals BALB/c mice may be used. The test group each receives an inoculation with fixed amount of antigen and varying amount of one or more chemokines. The control group receives an inoculation of comparable amount of antigen alone. Serum samples may be drawn from the mice after the final inoculation (for example every one or two weeks after inoculation), and serum is analyzed for antibodies against the antigen using known methods in the art, e.g., using an ELISA. DTH responses to the antigen may be measured after the final inoculation (e.g. within 1 -7 days). An increase in the serum titer of antibodies recognizing the antigen and/or an increase in footpad swelling in the animals receiving the antigen-compositions containing the chemokine(s) as compared to the serum titer of antibodies against the antigen and/or the footpad swelling in the animals receiving the antigen composition not containing the chemokine(s), indicates that the chemokine(s) enhance the immune response to antigen. An increase in the serum titer of antibodies recognizing the antigen and/or an increase in footpad swelling in the animals receiving the antigen- compositions containing the chemokines as compared to the serum titer of antibodies against the antigen and/or the footpad swelling in the animals receiving the antigen composition not containing chemokine(s), indicates that the chemokine(s) enhances the immune response to antigen. An increase in the serum titer of antibodies recognizing the antigen and/or an increase in footpad swelling in the animals receiving the antigen-compositions containing MDC as compared to the serum titer of antibodies against the antigen and/or the footpad swelling in the animals receiving the antigen composition not containing MDC, indicates that the MDC enhances the immune response to antigen. An increase in the serum titer of antibodies recognizing the antigen and/or an increase in footpad swelling in the animals receiving the antigen- compositions containing MDC as compared to the serum titer of antibodies against the antigen and/or the footpad swelling in the animals receiving the antigen composition not containing MDC, indicates that the MDC enhances the immune response to antigen. 6. EXAMPLE: IMMUNIZATION WITH MDC-CONTAINING COMPOSITION The following experiment illustrates the evaluation of whether MDC will act as an adjuvant for a protein antigen and enhance the efficacy of a vaccine. However, it will be appreciated that the description applies equally to other chemokines and combinations of chemokines. 6.1. MATERIALS AND METHODS 6.1.1. ANIMALS AND REAGENTS BALB/c mice are purchased from Harlan-Sprague-Dawley (Indianapolis, IN). Human MDC (hMDC) was obtained from CD8 + T cell clones immortalized in vitro prepared as previously described (Markham et al., 1983 Int. ]. Cancer 3_ :413; Markham et al. 1984, Int. j. Cancer 33_: 13). One such immortalized CD8 + T cell clone, F3b Clone 19, was adapted to growth in serum-free medium by the following procedure and used for further studies. F3b Clone 19 cells were grown in complete medium containing rlL-2 (16 ng/ml) at 37?C in a CO2 incubator. After expanding the culture to 200 ml, the cells were pelleted and resuspended in RPMI medium containing HB101 (Irvine Scientific) supplemented with 16 ng/ml of rlL-2, 1 % glutamine and 1 % penicillin/streptomycin. The cells were grown to full confluence and the medium harvested by centrifugation at 670 x g for 10 minutes. Human MDC (hMDC) was purified from F3b Clone 19 as described in Pal et al., 1997, Science 278:695-698. Briefly, the cell free culture supernatant from F3b Clone 19 was clarified by high speed centrifugation and fractionated by heparin affinity chromatography, taking advantage of the heparin binding characteristics of chemokines (Witt and Lander, 1994, Current Biology 4:394; Proost et al., 1996, Method: A Companion to Methods in Enzymology 10:82). Culture supernatant (1200 ml) from F3b Clone 19, grown to high cell density in serum-free medium supplemented with rlL-2 was clarified by high speed centrifugation (100,000 x g for 60 minutes at 4?C) and applied to a 5 ml HiTrap heparin affinity FPLC column (Pharmacia) equilibrated in 10 mM Tris-HCl, pH 7.6 containing 0.1 M NaCl (column buffer). The column was then washed extensively with column buffer and the bound proteins eluted from the column with 10 mM Tris-HCl, pH 7.6 containing 2.0 M NaCl at a flow rate of 0.5 to 1 ml/minute. Virtually all of the HIV suppressive activity effective against primary NSI and SI isolates and HIV-1 IHB was recovered in the column eluate (data not shown). The heparin affinity column eluate was brought to pH 2.0 by addition of trifluoracetic acid (TFA) and subjected to reversed phase HPLC on a PEEK C-18 column (Waters Instruments) equilibrated in H2O containing 0.1 % TFA. Proteins bound to the column were eluted with a 5 minute linear gradient of aqueous acetonitrile (0 to 35 %) containing 0.1 % TFA. After 10 minutes at 35% acetonitrile, the column was further developed with a 60 minute linear gradient of 35-70%> aqueous acetonitrile in TFA. The flow rate was maintained at 0.5 to 1 ml/minute. The fractions obtained were then tested for suppressor activity in the acute infectivity assay using HIV-I 111B. Active fractions were pooled, diluted twofold in H2O with 0.1 % TFA and reapplied to the column. The column was then developed with a 30 minute linear aqueous acetonitrile gradient (0-60%) containing 0.1 %> TFA at a flow rate of 0.5 to 1 ml/minute. The fractions obtained were assayed as above. Active fractions were pooled, diluted with H2O/O. I % TFA and fractionated under the same conditions to obtain a single protein peak. The fraction corresponding to the peak and flanking fractions were tested in the infectivity assay to verify that suppressor activity was cofractionated with the protein. Suppressive activity against H IV-1 IMB in the absence of cytotoxic effects consistently copurified with a single protein peak that appeared as a homogeneous 8 kDa band when analyzed by SDS-polyacrylamide gel electrophoresis. This protein was not reactive in ELISAs for RANTES, MIP-1 α or MlP-l β (R&D Systems). Recombinant gp120 protein derived from HIV-1 1MB isolate is purchased from Intracel (Foster City, CA). 6.1.2 IMMUNIZATION OF MICE The hMDC and the gp120 is resuspended in a total volume of 50 μl of phosphate-buffered saline (PBS). Mice are divided into 5 groups with 3-4 mice in each group. Groups 1 -4 are inoculated with 10 μg gp120 and 0.3 μg, 0.1 μg, 0.03 μg, and 0.01 μg of hMDC, respectively. As a control, group 5 is inoculated with 10 μg of gp120 in the absence of hMDC. For primary inoculation, each group of mice is inoculated with 10 μl of the hMDC and gp120 solution via footpad. Two to three weeks after the primary inoculation, each mouse is given the same does of hMDC/gp120 that is used in primary inoculation. 6.1.3 ELISA ASSAY Serum samples are collected one week after the second inoculation via tail vein bleed. gp120 serum responses are measured using standard gp120 antibody ELISA assays. 6.1.4 DTH ASSAY The delayed-type hypersensitivity (DTH) response is measured from 1 -7 days after the second inoculation. A caliper is to be used to measure footpad swelling. 6.2. RESULTS Mice inoculated with hMDC/gp120 are expected to have greater serum antibody and DTH responses than mice inoculated with gp120 alone. The improved responses will be reflected in either increased titers of serum antibody responses or increased footpad swelling. A dose response effect is expected - increasing the dose of hMDC used is expected to cause a corresponding improvement in the serum and DHT gp120-specific responses. 7. EXAMPLE: OTHER CHEMOKINES AND COMBINATIONS OF CHEMOKINES The foregoing experiments can be repeated using other chemokines and combinations of chemokines. For example, the experiments are preferably repeated using one or more chemokines selected from the group consisting of: Macrophage- derived chemokine, Monocyte chemotactic protein 1 , Monocyte chemotactic protein 2, Monocyte chemotactic protein 3, Monocyte chemotactic protein 4, activated macrophage specific chemokine 1 , Macrophage inflammatory protein 1 alpha, Macrophage inflammatory protein 1 beta, Macrophage inflammatory protein 1 gamma, Macrophage inflammatory protein 1 delta, Macrophage inflammatory protein 2 alpha, Macrophage inflammatory protein 3 alpha, Macrophage inflammatory protein 3 beta, Regulated upon activation, normal T cell expressed and secreted (and its variants), I- 309, EBI 1 -ligand chemokine, Pulmonary and activation regulated chemokine, Liver and activation-regulated chemokine, Thymus and activation regulated chemokine, Eotaxin (and variants), Human CC chemokine 1 , Human CC chemokine 2, Human CC chemokine 3, IL-10-inducible chemokine, liver-expressed chemokine., 6Ckine, Exodus 1 , Exodus 2, Exodus 3, thymus-expressed chemokine, Secondary Lymphoid tissue chemokine, Lymphocyte and Monocyte chemoattractant; Monotactin, Activation- induced, chemokine-related molecule, Myeloid progenitor inhibitory factor-1 , Myeloid progenitor inhibitory factor-2, Stromal cell-derived factor 1 alpha, Stromal cell-derived factor 1 beta, B-cell-attracting chemokine 1 , HuMIG, H1 74, Interferon-stimulated T- cell alpha chemoattractant, lnterleukin-8, IP-10, platelet factor 4, growth-regulated gene-alpha, growth-regulated gene-beta, growth-regulated gene-gamma, Neutrophil- activating protein 2, ENA-78, granulocyte chemotactic protein 2, LYMPHOTACTIN, and Fractalkine/neurotactin. The present invention is not to be limited in scope by the specific embodiments described herein. Indeed, various modifications of the invention in addition to those described herein will become apparent to those skilled in the art from the foregoing description. Such modifications are intended to fall within the scope of the appended claims. Various references are cited herein, the disclosures of which are incorporated by reference in their entireties.

Claims: THE CLAIMS: 1 . A method to enhance the efficacy of a vaccine in a subject comprising administering to the subject an immunogenic amount of one or more purified antigens against which an immune response is desired in the subject and an amount of one or more chemokines, or purified fragments or derivatives thereof, effective to enhance the efficacy of said vaccine. 2. The method of claim 1 , wherein the one or more chemokines are selected from a chemokine class selected from the group consisting of: CC, CXC, C-C and CX3C. 3. The method of claim 1 , wherein the one or more chemokines are selected from the group consisting of: Macrophage-derived chemokine, Monocyte chemotactic protein 1 , Monocyte chemotactic protein 2, Monocyte chemotactic protein 3, Monocyte chemotactic protein 4, activated macrophage specific chemokine 1 , Macrophage inflammatory protein 1 alpha, Macrophage inflammatory protein 1 beta, Macrophage inflammatory protein 1 gamma, Macrophage inflammatory protein 1 delta, Macrophage inflammatory protein 2 alpha, Macrophage inflammatory protein 3 alpha, Macrophage inflammatory protein 3 beta, Regulated upon activation, normal T cell expressed and secreted (and its variants), I-309, EBI1 -ligand chemokine, Pulmonary and activation regulated chemokine, Liver and activation-regulated chemokine, Thymus and activation regulated chemokine, Eotaxin (and variants), Human CC chemokine 1 , Human CC chemokine 2, Human CC chemokine 3, IL-10- inducible chemokine, liver-expressed chemokine, 6Ckine, Exodus 1 , Exodus 2, Exodus 3, thymus-expressed chemokine, Secondary Lymphoid tissue chemokine, Lymphocyte and Monocyte chemoattractant; Monotactin, Activation-induced, chemokine-related molecule, Myeloid progenitor inhibitory factor-1 , Myeloid progenitor inhibitory factor-2, Stromal cell-derived factor 1 alpha, Stromal cell-derived factor 1 beta, B-cell-attracting chemokine 1 , HuMIG, H 1 74, Interferon-stimulated T-cell alpha chemoattractant, lnterleukin-8, IP-10, platelet factor 4, growth-regulated gene-alpha, growth- regulated gene-beta, growth-regulated gene-gamma, Neutrophil-activating protein 2, ENA-78, granulocyte chemotactic protein 2, LYMPHOTACTIN, and Fractal kine/neurotactin. 4. The method of claim 1 , wherein the one or more chemokines are selected from the group consisting of: MDC, SDF-1 , BLC, and MCP-1 . 5. The method of claim 1 wherein the fragment(s) or derivative(s) are truncation isoforms. 6. The method of claim 1 , wherein the one or more chemokines include MDC comprising the amino acid sequence of SEQ ID NO: 2. 7. The method of claim 1 , wherein the one or more chemokine fragment includes an MDC fragmentselected from the group consisting of amino acid numbers 2- 69, 3-69, 5-69, 7-69 and 9-69 of SEQ ID NO: 2. 8. The method of claim 1 , wherein the one or more chemokine fragment includes an MDC fragment selected from the group consisting of amino acid numbers 2- 69, 3-69, 5-69, 7-69 and 9-69 of SEQ ID NO: 2., which derivative has activity to enhance the efficacy of the vaccine. 9. The method of claim 1 , wherein the one or more chemokine derivatives has one or more insertions or substitutions with one or more non-classical amino acids relative to a corresponding wildtype chemokine, which derivative has activity to enhance the efficacy of the vaccine. 10. The method of claim 1 , including a chemokine derivative having one or more conservative substitutions in sequence relative a wildtype MDC, which derivative has activity to enhance the efficacy of the vaccine. 1 1 . The method of claim 1 , wherein the one or more chemokines include a human chemokine. 12. The method of claim 1 , wherein the purified chemokine(s) or purified fragment(s) or derivative(s) thereof is/are administered concurrently with the purified antigen(s). 1 3. The method of claim 1 wherein the purified chemokine(s) or purified fragment(s) or derivative(s) thereof, are administered within a time period before or after administration of the purified antigen, which time period permits the purified MDC or purified fragment or derivative thereof MDC to enhance the efficacy of the vaccine. 14. The method of claim 1 , wherein the antigen is an HIV antigen. 1 5. The method of claim 14, wherein the HIV antigen is HIV-associated gp120 protein. 16. The method of claim 1 , wherein the subject is a human. 1 7. The method of claim 1 , wherein the subject is infected or at risk of being infected with HIV virus. 18. The method of claim 1 , wherein the vaccine elicits a humoral response against the antigen in the subject. 19. The method of claim 1 , wherein the vaccine elicits a cell-mediated response against the antigen in the subject. 20. The method of claim 1 , wherein the vaccine elicits both a humoral and a cell- mediated response against the antigen in the subject. 21 . The method of claim 1 , wherein the vaccine further comprises pharmaceutically acceptable excipient, auxiliary substance, adjuvant, wetting or emulsifying agent, or pH buffering agent. 22. A method to enhance the efficacy of a vaccine in a subject comprising administering to the subject a first amount of a first set of one or more purified nucleotide sequences encoding one or more antigens against which an immune response is desired in the subject and a second second set of one or more purified nucleic acids, each comprising a nucleotide sequence encoding one or more chemokines, or fragments or derivatives thereof, wherein the antigen(s) and the chemokine(s) are expressed in a coordinated manner upon introduction into a suitable cell, said first amount is immunogenic and said second amount is effective in enhancing the efficacy of the vaccine. 23. The method of claim 22, wherein the one or more chemokines are selected from a chemokine class selected from the group consisting of: CC, CXC, C-C and CX3C. 24. The method of claim 22, wherein the one or more chemokines are selected from the group consisting of: Macrophage-derived chemokine, Monocyte chemotactic protein 1 , Monocyte chemotactic protein 2, Monocyte chemotactic protein 3, Monocyte chemotactic protein 4, activated macrophage specific chemokine 1 , Macrophage inflammatory protein 1 alpha, Macrophage inflammatory protein 1 beta, Macrophage inflammatory protein 1 gamma, Macrophage inflammatory protein 1 delta, Macrophage inflammatory protein 2 alpha, Macrophage inflammatory protein 3 alpha, Macrophage inflammatory protein 3 beta, Regulated upon activation, normal T cell expressed and secreted (and its variants), I-309, EBI1-ligand chemokine, Pulmonary and activation regulated chemokine, Liver and activation-regulated chemokine, Thymus and activation regulated chemokine, Eotaxin (and variants), Human CC chemokine 1 , Human CC chemokine 2, Human CC chemokine 3, IL-10- inducible chemokine, liver-expressed chemokine, 6Ckine, Exodus 1 , Exodus 2, Exodus 3, thymus-expressed chemokine, Secondary Lymphoid tissue chemokine, Lymphocyte and Monocyte chemoattractant; Monotactin, Activation-induced, chemokine-related molecule, Myeloid progenitor inhibitory factor-1 , Myeloid progenitor inhibitory factor-2, Stromal cell-derived factor 1 alpha, Stromal cell-derived factor 1 beta, B-cell-attracting chemokine 1 , HuMIG, H1 74, Interferon-stimulated T-cell alpha chemoattractant, lnterleukin-8, IP-10, platelet factor 4, growth-regulated gene-alpha, growth- regulated gene-beta, growth-regulated gene-gamma, Neutrophil-activating protein 2, ENA-78, granulocyte chemotactic protein 2, LYMPHOTACTIN, and Fractalkine/neurotactin. 25. The method of claim 22, wherein the one or more chemokines are selected from the group consisting of: MDC, SDF-1 , BLC, and MCP-1 . 26. The method of claim 22 wherein the fragment(s) or derivative(s) are truncation isoforms. 27. The method of claim 22, wherein the nucleotide sequence encoding one or more chemokines comprises the nucleotide sequence of SEQ ID NO:1. 28. The method of claim 22, wherein one or more of the chemokine derivative(s) have deletional, insertional or substitutional mutations and combination thereof, which derivative has activity to enhance the efficacy of the vaccine. 29. The method of claim 22, wherein the vaccine elicits a humoral response against the antigen in the subject. 30. The method of claim 22, wherein the vaccine elicits a cell-mediated response against the antigen in the subject. 31 . The method of claim 22, wherein the vaccine elicits both a humoral and a cell- mediated response against the antigen in the subject. 32. The method of claim 22, wherein the vaccine further comprises pharmaceutically acceptable excipient, auxiliary substance, adjuvant, wetting or emulsifying agent, or pH buffering agent. 33. A composition comprising: an immunogenic amount of one or more purified antigens and an amount of one or more purified chemokines, or purified fragments or derivatives thereof, effective to enhance the immune response to said antigen(s); and a pharmaceutically acceptable carrier. 34. The composition of claim 33, wherein the one or more chemokines are selected from the group consisting of: MDC, SDF-1 , BLC, and MCP-1 . 35. The composition of claim 33, wherein the one or more chemokines are selected from a chemokine class selected from the group consisting of: CC, CXC, C-C and CX3C. 36. The composition of claim 33, wherein the one or more chemokines are selected from the group consisting of: Macrophage-derived chemokine, Monocyte chemotactic protein 1 , Monocyte chemotactic protein 2, Monocyte chemotactic protein 3, Monocyte chemotactic protein 4, activated macrophage specific chemokine 1 , Macrophage inflammatory protein 1 alpha, Macrophage inflammatory protein 1 beta, Macrophage inflammatory protein 1 gamma, Macrophage inflammatory protein 1 delta, Macrophage inflammatory protein 2 alpha, Macrophage inflammatory protein 3 alpha, Macrophage inflammatory protein 3 beta, Regulated upon activation, normal T cell expressed and secreted (and its variants), I-309, EBI 1 -ligand chemokine, Pulmonary and activation regulated chemokine, Liver and activation-regulated chemokine, Thymus and activation regulated chemokine, Eotaxin (and variants), Human CC chemokine 1 , Human CC chemokine 2, Human CC chemokine 3, IL-10- inducible chemokine, liver-expressed chemokine, 6Ckine, Exodus 1 , Exodus 2, Exodus 3, thym us-expressed chemokine, Secondary Lymphoid tissue chemokine, Lymphocyte and Monocyte chemoattractant; Monotactin, Activation-induced, chemokine-related molecule, Myeloid progenitor inhibitory factor-1 , Myeloid progenitor inhibitory factor-2, Stromal cell-derived factor 1 alpha, Stromal cell-derived factor 1 beta, B-cell-attracting chemokine 1 , HuMIG, H1 74, Interferon-stimulated T-cell alpha chemoattractant, lnterleukin-8, IP-10, platelet factor 4, growth-regulated gene-alpha, growth- regulated gene-beta, growth-regulated gene-gamma, Neutrophil-activating protein 2, ENA-78, granulocyte chemotactic protein 2, LYMPHOTACTIN, and Fractalkine/neurotactin. 37. The composition of claim 33, wherein the fragment(s) or derivative(s) are truncation isoforms. 38. The composition of claim 33, wherein the one or more chemokine fragment includes an MDC fragmentselected from the group consisting of amino acid numbers 2-69, 3-69, 5-69, 7-69 and 9-69 of SEQ ID NO: 2. 39. The composition of claim 33, wherein the one or more chemokine fragment includes an MDC fragmentselected from the group consisting of amino acid numbers 2-69, 3-69, 5-69, 7-69 and 9-69 of SEQ ID NO: 2, which derivative has activity to enhance the efficacy of the vaccine. 40. The composition of claim 33, wherein the one or more chemokine derivatives has one or more insertions of or substitutions with one or more non-classical amino acids relative to a corresponding wildtype chemokine, which derivative has activity to enhance the efficacy of the vaccine. 41 . The composition of claim 33, wherein the one or more chemokine derivatives has one or more conservative substitutions in sequence relative a corresponding wildtype chemokine, which derivative has activity to enhance the efficacy of the vaccine. 42. The composition of claim 33, wherein the chemokine is a human chemokine. 43. The composition of claim 33, wherein the antigen is an HIV antigen. 44. The composition of claim 43, wherein the antigen is HIV associated gp120 protein. 45. A composition comprising an amount of a first set of purified nucleic acids comprising one or more nucleotide sequences encoding one or more antigens and a second set of purified nucleic acids comprising one or more nucleotide sequences encoding one or more chemokines, or fragments or derivatives thereof, wherein the antigen(s) and the chemokine(s), or fragment(s) or derivative(s) thereof, are expressed from said first set of nucleic acid(s) and second set of nucleic acid(s) in a coordinated manner such that upon introduction into a suitable cell, the amount of said first set of nucleic acid(s) is sufficient to express an immunogenic amount of the antigen and the amount of the said second set of nucleic acid(s) is effective in enhancing the efficacy of the vaccine; and a pharmaceutically acceptable carrier. 46. The composition of claim 45, wherein the chemokine is MDC and the nucleic acid encoding the MDC comprises the nucleotide sequence of SEQ ID NO: 1 . 47. The composition of claim 45, wherein the chemokine derivative(s) have deletional, insertional or substitutional mutations and/or combinations thereof, and the derivative(s) have activity to enhance the efficacy of the vaccine. 48. The composition of claim 45, further comprising pharmaceutically acceptable excipient, auxiliary substance, adjuvant, wetting or emulsifying agent, or pH buffering agent. 49. A composition comprising a first set of purified nucleotide sequences encoding one or more antigens and a second set of purified nucleotide sequences encoding one or more chemokines, or fragments or derivatives thereof, wherein the antigen(s) and the chemokine(s) are expressed in a coordinated manner such that upon introduction into a suitable cell, the sets produce an amount of said antigen(s) that is immunogenic and an amount of chemokine(s), or fragment(s) or derivative(s) thereof, that is effective in enhancing the efficacy of the vaccine relative to a corresponding vaccine composition without such chemokine(s), fragment(s) or derivative(s) thereof. 50. The composition of claim 49, wherein the one or more chemokines are selected from the group consisting of: Macrophage-derived chemokine, Monocyte chemotactic protein 1 , Monocyte chemotactic protein 2, Monocyte chemotactic protein 3, Monocyte chemotactic protein 4, activated macrophage specific chemokine 1 , Macrophage inflammatory protein 1 alpha, Macrophage inflammatory protein 1 beta, Macrophage inflammatory protein 1 gamma, Macrophage inflammatory protein 1 delta, Macrophage inflammatory protein 2 alpha, Macrophage inflammatory protein 3 alpha, Macrophage inflammatory protein 3 beta, Regulated upon activation, normal T cell expressed and secreted (and its variants), I-309, EBI1 -ligand chemokine, Pulmonary and activation regulated chemokine, Liver and activation-regulated chemokine, Thymus and activation regulated chemokine, Eotaxin (and variants), Human CC chemokine 1 , Human CC chemokine 2, Human CC chemokine 3, IL-10- inducible chemokine, liver-expressed chemokine, 6Ckine, Exodus 1 , Exodus 2, Exodus 3, thym us-expressed chemokine, Secondary Lymphoid tissue chemokine, Lymphocyte and Monocyte chemoattractant; Monotactin, Activation-induced, chemokine-related molecule, Myeloid progenitor inhibitory factor-1 , Myeloid progenitor inhibitory factor-2, Stromal cell-derived factor 1 alpha, Stromal cell-derived factor 1 beta, B-cell-attracting chemokine 1 , HuMIG, H1 74, Interferon-stimulated T-cell alpha chemoattractant, lnterleukin-8, IP-10, platelet factor 4, growth-regulated gene-alpha, growth- regulated gene-beta, growth-regulated gene-gamma, Neutrophil-activating protein 2, ENA-78, granulocyte chemotactic protein 2, LYMPHOTACTIN, and Fractalkine/neurotactin. 51. The method of claim 49, wherein the one or more chemokines are selected from a chemokine class selected from the group consisting of: CC, CXC, C-C and CX3C. 52. The method of claim 49, wherein the one or more chemokines are selected from the group consisting of: MDC, SDF-1 , BLC, and MCP-1 . 53. The composition of claim 49, wherein the fragment(s) or derivative(s) are truncation isoforms. 54. The composition of claim 49, wherein the nucleic acid is administered directly to the subject. 55. The composition of claim 49, wherein the nucleic acid is introduced into a suitable host cell and said suitable host cell is introduced into the subject.

Inventors: DEVICO ANTHONY L, GALLO ROBERT C, GARZINO-DEMO ALFREDO
Applicants: DEVICO ANTHONY L, GALLO ROBERT C, GARZINO DEMO ALFREDO, UNIV MARYLAND BIOTECH INST
Application year: 1998
Main classification: C07K14
IPC codes: A61K39, A61K48, C12N15