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.
D002448:Cell Adhesion / Q000187:drug effects; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D003208:Concanavalin A / Q000276:immunology / Q000378:metabolism*; D003513:Cycloheximide / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D005455:Fluorescent Antibody Technique; D006023:Glycoproteins; D011955:Receptors, Drug / Q000187:drug effects; D014246:Trichomonas vaginalis / Q000187:drug effects / Q000378:metabolism*
D006023:Glycoproteins; D011955:Receptors, Drug; D003208:Concanavalin A; D003513:Cycloheximide; D004492:Edetic Acid