Studies of the ligand binding to cholera toxin, II. The hydrophilic moiety of sialoglycolipids.
The binding between cholera toxin or its B-protein subunit and various ganglioside-related oligosaccharides was studied by equilibrium displacement dialysis. At low concentrations of ligand, the  binding of monosialo-gangliotetraitol exceeded that of the parent ganglioside II3NeuAcGgOse4-Cer, the possible cell surface receptor for the toxin. The terminal galactose residue and an intact carboxyl group of the sialic acid moiety of monosialo-gangliotetraose were found to be necessary for strong binding to the toxin.
D055598:Chemical Phenomena; D002621:Chemistry; D004768:Enterotoxins / Q000378:metabolism*; D005732:Gangliosides / Q000378:metabolism*; D008024:Ligands; D011485:Protein Binding; D014734:Vibrio cholerae
D004768:Enterotoxins; D005732:Gangliosides; D008024:Ligands