Unmasking of actual and potential receptor sites for cholera toxin in intestinal mucosal homogenates.
Endongenous and exogenous sialidases appear to unmask sialidase-stable and sialidase-labile gangliosides in intestinal mucosal homogenates by attacking glycoproteins. Exogenous (but not endogenous) sialidase then converts sialidase-labile gangliosides into the cholera toxin-binding, sialidase-stable ganglioside GM1 (galactosyl-N-acetylgalactosaminyl [sialosyl] lactosyl ceramide). Since Vibrio cholerae produces sialidase, these observations may be relevant to the course of cholera.
D000818:Animals; D002417:Cattle; D002772:Cholera Toxin / Q000494:pharmacology*; D005732:Gangliosides / Q000378:metabolism / Q000494:pharmacology; D006023:Glycoproteins; D007413:Intestinal Mucosa / Q000032:analysis / Q000187:drug effects*; D009439:Neuraminidase / Q000494:pharmacology*; D011817:Rabbits; D011955:Receptors, Drug / Q000032:analysis / Q000187:drug effects*; D014734:Vibrio cholerae / Q000201:enzymology
D005732:Gangliosides; D006023:Glycoproteins; D011955:Receptors, Drug; D002772:Cholera Toxin; D009439:Neuraminidase