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Vaccination of BALB/c mice withLeishmania major promastigote culture filtrate proteins plusCorynebacterium parvum confers resistance to infection withL. major . To define immunogenic components of this protein mixture, we used sera from vaccinated mice to screen anL. major amastigote cDNA expression library. One of the immunoreactive clones thus obtained encoded a novel protein ofL. major with a molecular mass of 22.1 kDa. The predicted amino acid sequence of this clone exhibited significant homology to eukaryotic thiol-specific-antioxidant (TSA) proteins. Therefore, we have designated this proteinL. major TSA protein. Southern blot hybridization analyses indicate that there are multiple copies of the TSA gene in all species ofLeishmania analyzed. Northern blot analyses demonstrated that the TSA gene is constitutively expressed inL. major promastigotes and amastigotes. Recombinant TSA protein containing an amino-terminal six-histidine tag was expressed inEscherichia coli with the pET17b system and was purified to homogeneity by affinity chromatography. Immunization of BALB/c mice with recombinant TSA protein resulted in the development of strong cellular immune responses and conferred protective immune responses against infection withL. major when the protein was combined with interleukin 12. In addition, recombinant TSA protein elicited in vitro proliferative responses from peripheral blood mononuclear cells of human leishmaniasis patients and significant TSA protein-specific antibody titers were detected in sera of both cutaneous-leishmaniasis and visceral-leishmaniasis patients. Together, these data suggest that the TSA protein may be useful as a component of a subunit vaccine against leishmaniasis.

Human and Murine Immune Responses to a NovelLeishmania majorRecombinant Protein Encoded by Members of a Multicopy Gene Family