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.