Inactivation of the biological activities of the thermostable direct hemolysin of Vibrio parahaemolyticus by ganglioside Gt1.
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.
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*
D005732:Gangliosides; D006460:Hemolysin Proteins; D009439:Neuraminidase