[Cloning and bioinformatics analysis of surface antigen-related sequence protein SRS67 and SRS20A genes in Toxoplasma gondii].

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OBJECTIVE: . METHODS: cDNA as a template. The amplification products were subjected to double restriction-enzyme digestion, and the target fragments were recovered and ligated into DH5α competent cells with T4 ligase. Positive single colonies were selected and cultured, and the pET-32a-SRS67 and pET-32a-SRS20A recombinant plasmids were extracted, transformed into competent cells for induction of recombinant protein expression. The expression of recombinant proteins was determined using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting. RESULTS: genes were approximately 633 bp and 987 bp in size. The SRS67 recombinant protein exhibited the highest expression in the precipitate following induction with 0.1 mmol/L IPTG for 16 h, and the SRS20A recombinant protein showed the highest expression following induction with 0.5 mmol/L IPTG for 16 h. SDS-PAGE and Western blotting confirmed successful expression of the recombinant proteins. CONCLUSIONS: The SRS67 and SRS20A proteins possess multiple cellular epitopes and exhibit favorable immunogenicity. The recombinant SRS67 and SRS20A proteins have been successfully expressed, which provides the theoretical evidence for deciphering protein functions and screening effective vaccine antigens against toxoplasmosis.

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