Evidence for concanavalin A binding sites on the surface coat of Trypanosoma congolense.
Glycoproteins of Trypanosoma congolense have been detected on SDS-polyacrylamide gels using the Concanavalin A peroxidase technique. Using [35S]diazoniobenzenesulphonate as a marker for cell surface proteins it was possible to distinguish between internal glycoproteins and the surface coat proteins. On SDS-polyacrylamide gels Con A reacted with the surface coat proteins. Results obtained from Con A-induced agglutination of living trypanosomes indicated that sugars of the surface coat proteins were accessible to Con A. This was reinforced by the cytochemical visualization of Con A binding to the trypanosome surface. The results suggested that the surface coat protein contained alpha-linked D-mannosyl, D-glucosyl, or N-acetyl-D-glucosaminoyl residues, which are exposed exteriorly on the surface coat.
D000818:Animals; D002462:Cell Membrane / Q000648:ultrastructure; D003208:Concanavalin A / Q000378:metabolism; D005260:Female; D006023:Glycoproteins / Q000032:analysis* / Q000378:metabolism; D008565:Membrane Proteins / Q000032:analysis* / Q000378:metabolism; D008766:Methylmannosides / Q000494:pharmacology; D051379:Mice; D011952:Receptors, Concanavalin A / Q000032:analysis* / Q000378:metabolism; D014345:Trypanosoma / Q000032:analysis* / Q000378:metabolism / Q000648:ultrastructure; D014353:Trypanosomiasis, African / Q000469:parasitology*
D006023:Glycoproteins; D008565:Membrane Proteins; D008766:Methylmannosides; D011952:Receptors, Concanavalin A; D003208:Concanavalin A