Similarities between the primary structures of two distinct major surface proteins of Toxoplasma gondii

Abstract

Toxoplasma gondii possesses a 43-kDa surface protein (SAG3) that is expressed by all invasive stages. We have cloned and sequenced cDNAs encoding SAG3, with the longest one encoding a primary product of 385 amino acid residues. The deduced amino acid sequence contains a putative NH2-terminal signal sequence, as well as a glycosylphosphatidylinositol anchor attachment site. It is characterized by 12 cysteine residues whose distribution suggests a tandem duplication of a single ancestral motif containing 6 cysteine residues. Although no DNA sequence analogies were found, comparative amino acid sequence analysis detected a resemblance to SAG1, which is the major surface antigen specifically expressed by the proliferative tachyzoite stage. Despite a low degree of identity between the two amino acid sequences (24%), the conservative distribution of the cysteine and tryptophan residues, as well as of repeated motifs, together with oligopeptide identities suggest similar folding and possibly similar function for both proteins.