Recombinant fusion protein of Treponema pallidum (Tp) was expressed, purified and analyzed for its antigenicity and immunogenicity, which provided a new candidate antigen for diagnostic reagent and vaccine of syphilis. Method:Recombinant Tp fusion gene Tp0453-TpF1-Tp0965 was synthesized and recombinant protein was expressed in Escherichia coli. Recombinant fusion protein was purified by Nickel-affinity chromatography column and identified by Western blot. Human serum samples were used for Enzyme linked immunosorbent assay (ELISA) to determine the antigencity of recombinant fusion protein. New Zealand rabbit was immunized with recombinant fusion protein, and the serum antibodies from immunized rabbit were tested by ELISA to evaluate the immunogenicity of recombinant fusion protein. Recombinant fusion protein Tp0453-TpF1-Tp0965 with a molecular weight of 50 kD was expressed successfully in E. coli. Recombinant fusion protein was recognized by syphilis antibody positive serum, but not negative serum. Recombinant fusion protein was used as antigen to analyze the serum antibody of syphilis patient group and non syphilis patient group, and statistically significant difference for syphilis antibody was observed between two groups. The rabbit immunized with recombinant fusion protein produced persistently syphilis antibody with a high titer. Recombinant fusion protein Tp0453-TpF1-Tp0965 had good antigenicity and immunogenicity, and could be used as a good syphilis diagnostic reagent and an ideal syphilis vaccine candidate.
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维普
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