Studies of the ligand binding to cholera toxin, I. The lipophilic moiety of sialoglycolipids.
The fixation of cholera toxin by ganglioside GGtet1 is dependent on the nature of the carbohydrate as well as the lipid moiety of the glycolipid. The role of the lipid in binding to the toxin investigated with synthetic ganglioside analogues (gangliosidoides). The interaction between glycolipid and toxin was followed by precipitate formation, by inhibition of toxicity and in polyacrylamide gel electrophoresis. For specific precipitation, an aliphatic hydrocarbon chain at least 14 C-atoms in length is required. Some of the gangliosidoides form high molecular weight complexes with cholera toxin at lower molar ratios of ligand to protein than the natural compound. None of the synthetic gangliosidoides equalled natural ganglioside in its ability to inhibit the effects of the toxin in vivo, but some did show considerable inhibitory activity ih monosialo-gangliotetraose or corresponding sialo-glycolipids prevents the easy degradation of the B-protein of cholera toxin into protein subunits by sodium dodecylsulfate.
D001427:Bacterial Toxins; D004591:Electrophoresis, Polyacrylamide Gel; D004768:Enterotoxins; D005732:Gangliosides; D006017:Glycolipids; D008024:Ligands; D012794:Sialic Acids / Q000032:analysis; D014734:Vibrio cholerae
D001427:Bacterial Toxins; D004768:Enterotoxins; D005732:Gangliosides; D006017:Glycolipids; D008024:Ligands; D012794:Sialic Acids