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....

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Bibliographic Details
Published in:Parasitology 1980-02, Vol.80 (1), p.113-122
Main Authors: Rautenberg, P., Reinwald, E., Risse, H-J.
Format: Article
Language:English
Subjects:
Animals
Cell Membrane - ultrastructure
Concanavalin A - metabolism
Female
Glycoproteins - analysis
Glycoproteins - metabolism
Membrane Proteins - analysis
Membrane Proteins - metabolism
Methylmannosides - pharmacology
Mice
Receptors, Concanavalin A - analysis
Receptors, Concanavalin A - metabolism
Trypanosoma - analysis
Trypanosoma - metabolism
Trypanosoma - ultrastructure
Trypanosomiasis, African - parasitology
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Summary: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 α-linked d-mannosyl, d-glucosyl, or N-acetyl-d-glucosaminoyl residues, which are exposed exteriorly on the surface coat.
ISSN:0031-1820
1469-8161
DOI:10.1017/S0031182000000561