Abstract
Toxoplasmosis is a major worldwide protozoan zoonosis. The surface antigen 1 (SAG1) of Toxoplasma gondii (T. gondii) has always been recognized as an ideal vaccine candidate antigen. However, the intact and soluble SAG1 protein is usually difficult to acquire in vitro, which is unfavorable for employing the recombinant protein as a vaccine candidate antigen. In the present study, we obtained the full-length SAG1 recombinant protein in soluble form by Escherichia coli Transetta (DE3) cells under optimized expression conditions. The immunogenicity and protective ability of this recombinant protein against T. gondii acute infection were evaluated in a mouse model. Monitoring changes in serum antibody levels and types, the presence of cytokines, and the rate of lymphocyte proliferation in vaccinated mice were used to assess humoral and cellular immune responses. Additional assessments were performed to determine the protective potency of the recombinant protein in combating T. gondii RH tachyzoites. It was found that the titers of both IgG2a and IgG2b were considerably greater in the immunized mice compared to the titers of IgG1 and IgG3. The levels of Th1-type cytokines (IFN-γ, IL-12p70, IL-2, and TNF-α) and Th2-type cytokines (IL-10) significantly increased when splenocytes from immunological group mice were treated with T. gondii lysate antigen. Compared to the control group, a recombinant protein substantially increased the longevity of infected mice, with an average death time prolonged by 14.50 ± 0.34 days (p < 0.0001). These findings suggest that the full-length and soluble SAG1 recombinant protein produced potent immune responses in mice and could be a preferred subunit vaccine candidate for T. gondii, offering a feasible option for vaccination against acute toxoplasmosis.