Micellar gangliosides mediate the lipid insertion of cholera toxin protomer A.
The topology of the interaction of cholera toxin with ganglioside and detergent micelles was studied with the technique of hydrophobic photolabelling. Cholera toxin alpha and gamma polypeptide chains appear to penetrate into the hydrophobic core of ganglioside micelles. Micelles of SDS cause the labelling also of the beta polypeptide chains, while Triton X-100 micelles have little ability to mediate the labelling of the toxin. The specific reduction of the alpha-gamma disulfide bond allows the penetration of the alpha polypeptide chain into Triton X-100 micelles, but does not affect the interaction of cholera toxin with either ganglioside or SDS micelles. Thus, ganglioside micelles appear to cause a conformational change of the native toxin, such as to induce the penetration of the alpha chain into the micelle hydrophobic core.
D002772:Cholera Toxin; D003102:Colloids; D003902:Detergents; D004220:Disulfides; D005732:Gangliosides; D007700:Kinetics; D008823:Micelles; D010084:Oxidation-Reduction; D011485:Protein Binding; D013696:Temperature
D003102:Colloids; D003902:Detergents; D004220:Disulfides; D005732:Gangliosides; D008823:Micelles; D002772:Cholera Toxin