Involvement of a surface concanavalin A-binding glycoprotein in the adhesion of Trichomonas vaginalis to substrates.

Treatment of Trichomonas vaginalis with EDTA removes their ability to adhere to glass surfaces and changes their affinity to Concanavalin A (ConA) by a different distribution of their surface structures. Filtrates of the EDTA-treated Trichomonas passed through affinity chromatography columns (ConA bound to Sepharose 4B) separate into 2 fractions, one fraction was bound to the ConA-Sepharose beads, the other was not. The Con A - bound fraction appears to be a glycoprotein which restores in a specific way the ability of the EDTA-treated protozoa to adhere to glass.