Major surface protein of Toxoplasma gondii (p30) contains an immunodominant region with repetitive epitopes.

Four monoclonal antibodies (mAb) against surface antigens of tachyzoites of Toxoplasma gondii were produced. Immunoprecipitation of extracts of 125I-labeled tachyzoites identified the same polypeptide with apparent molecular weight of 30 000 (p30). A competition binding assay indicated that a single region of p30 was recognized by all 4 of the mAb. Furthermore, we found that single mAb inhibited 25-50% of the specific binding of antibodies of patients with toxoplasmosis to the antigenic extract of tachyzoites. It appears, therefore, that p30 is the most immunogenic constituent of tachyzoites, and that a single region of this molecule contains most of the immunogenic activity. Finally, a two-site/one-antibody immunoradiometric assay with the same mAb indicated that the p30 molecule is multivalent with respect to the expression of a single epitope.