Delineation and comparison of ganglioside-binding epitopes for the toxins of Vibrio cholerae, Escherichia coli, and Clostridium tetani: evidence for overlapping epitopes.
Binding studies of various glycolipids, mainly belonging to the ganglio series, to the toxins isolated from Vibrio cholerae, Escherichia coli, and Clostridium tetani have been performed, using the microtiter well assay. By using the found binding preferences in conjunction with minimum-energy conformations obtained from molecular modeling of the various ligands, binding epitopes on the natural receptor glycolipids for the toxins have been defined. The binding preferences for the cholera toxin and the heat-labile E. coli toxin are very similar, with the ganglioside GM1 being the most efficient ligand. The tetanus toxin binds strongly to gangliosides of the G1b series, with GT1b as the most efficient ligand. It is found that the binding epitope on GM1 for the cholera and heat-labile toxins to a large extent overlaps with the epitope on GQ1b for the tetanus toxin.
Angström
J
J
Department of Medical Biochemistry, Göteborg University, Sweden.
Teneberg
S
S
Karlsson
K A
KA
D001427:Bacterial Toxins / Q000737:chemistry* / Q000276:immunology; D001665:Binding Sites; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002772:Cholera Toxin / Q000737:chemistry* / Q000276:immunology; D003017:Clostridium tetani; D004768:Enterotoxins / Q000737:chemistry* / Q000276:immunology; D000939:Epitopes; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D005732:Gangliosides; D006017:Glycolipids; D006028:Glycosphingolipids; D008958:Models, Molecular; D008969:Molecular Sequence Data; D013744:Tetanus Toxin / Q000737:chemistry* / Q000276:immunology; D013816:Thermodynamics; D014734:Vibrio cholerae
D001427:Bacterial Toxins; D004768:Enterotoxins; D000939:Epitopes; D029968:Escherichia coli Proteins; D005732:Gangliosides; D006017:Glycolipids; D006028:Glycosphingolipids; D013744:Tetanus Toxin; D002772:Cholera Toxin; C027538:heat-labile enterotoxin, E coli