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The major surface immunodominant antigen (P30) of Toxoplasma gondii was purified by two methods (i) SDS-PAGE and (ii) immunoaffinity chromatography. The secondary elements within this protein were assessed by circular dichroism and spectra obtained were compared to those proposed by Manavalan & Johnson (1983). The results allowed us to determine an all beta protein status for this antigen. This experimental result was in agreement with the predicted secondary structures deduced from the P30 primary sequence. Modifications in conformation according to pH and temperature were recorded without any change in immunoactivity. The epitope, which was always recognized by a monoclonal antibody against P30, could be a linear epitope.
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