Abstract
The potential of genetically fusing recombinant proteins to the simian immunodeficiency virus (SIV) Tat protein has been investigated. The recombinant SIV Tat protein was initially expressed in very low amounts in E. coli, but optimization of the coding sequence for translation in the bacterial host significantly improved protein expression. Whilst fusion of SIV Tat to an experimental antigen (GST) facilitated the binding of the antigen to cell surfaces it did not appear to facilitate the transport of the protein into the cytosol. The immunogenicity of GST was significantly enhanced, in the absence of adjuvants, when fused to SIV Tat, with the induction of IgG1 and IgG2a antibodies indicative of a Th1 response being induced. However, no evidence was obtained that such an immunization scheme efficiently induced a CTL response.
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