title: Inactivation of the biological activities of the thermostable direct hemolysin of Vibrio parahaemolyticus by ganglioside Gt1.
abstract: Biological activities of the thermostable direct hemolysin produced by Vibrio parahaemolyticus, such as its hemolytic activity and lethal activity, were inhibited by neuraminidase-sensitive gangliosides, of which GT1 ganglioside was the most inhibitory. Neuraminidase-resistant gangliosides did not affect the activities of the hemolysin. Results showed that horse erythrocytes, which are resistant to the hemolysin, do not contain the neuraminidase-sensitive gangliosides GT1 and GD1a. Therefore, we propose that neuraminidase-sensitive gangliosides, and especially GT1 ganglioside, may be the receptor sites on the membranes for the thermostable direct hemolysin of V. parahaemolyticus.
mesh_terms: D001666:Binding Sites, Antibody; D002462:Cell Membrane / Q000032:analysis; D046508:Culture Techniques; D004912:Erythrocytes / Q000032:analysis / Q000276:immunology*; D005732:Gangliosides / Q000032:analysis / Q000494:pharmacology*; D006460:Hemolysin Proteins; D006461:Hemolysis / Q000187:drug effects; D006801:Humans; D009439:Neuraminidase / Q000494:pharmacology; D014734:Vibrio cholerae / Q000201:enzymology; D014736:Vibrio parahaemolyticus / Q000276:immunology*
chemical_list: D005732:Gangliosides; D006460:Hemolysin Proteins; D009439:Neuraminidase