Abstract

To explore the biological function of rhoptry protein 38 (ROP38) of Toxoplasma gondii, and to identify the reactogenicity of the recombinant protein (rROP38). The ROP38 was amplified by RT-PCR from T. gondii RH strain, and was cloned into prokaryotic expression vector pET-28a (+). The recombinant plasmid was transformed into E. coli BL21 (DE3) competent cells. Then the rROP38 was analyzed by SDS-PAGE and identified by Western blot. SDS-PAGE showed that rROP38 was efficient expression with a molecular weight of about 43 kD. Western blot showed that rROP38 reacted with antibody of His tag or human positive antibody, which indicated that ROP38 had good reactogenicity and could be a serological diagnostic antigen. The study successfully obtains the rROP38 of T. gondii with good reactogenicity.

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