TOXOPLASMA-GONDII - UPTAKE OF FETUIN AND IDENTIFICATION OF A 15-KDA FETUIN-BINDING PROTEIN

Lectin-binding studies demonstrated the presence of a 68-kDa glycoprotein in tachyzoites of Toxoplasma gondii harvested from P388D1 macrophage cell cultures but not in tachyzoites maintained in peritoneal cavities of NMRI mice. This protein was identified as the embryonic protein fetuin that regularly is contained in fetal calf serum, a component of cell-culture media. Uptake of fetuin by T. gondii was demonstrated by intracellular localization of this protein. As shown by latex agglutination and immunofluorescence, no specific binding of fetuin to the parasite's surface was detected. Using affinity chromatography on fetuin-agarose, it was demonstrated that fetuin bound specifically to a 15-kDa antigen of tachyzoites. As revealed by inhibition studies with sialic acid and the lectin Sambucus nigra agglutinin, the 15-kDa protein probably recognized glycan structures of fetuin.