Article
A mutant toxin of Vibrio parahaemolyticus thermostable direct hemolysin which has lost hemolytic activity but retains ability to bind to erythrocytes.
Infection and immunity - 1 Aug 1994
Tang G Q, Iida T, Yamamoto K, Honda T
Abstract excerpt
A mutant toxin, R7, of thermostable direct hemolysin (TDH) with a single amino acid substitution at glycine 62 was analyzed. The hemolytic activity of R7 decreased to less than 1/1,000 of that of wild-type TDH, and its mouse lethality was undetectable. This mutant toxin, however, showed a marked inhibitory effect on hemolysis by wild-type TDH. Enzyme immunoassay and flow cytometric analysis demonstrated that R7...
Topics
- Cell Membrane Permeability
- Erythrocytes
- Hemolysin Proteins
- Hemolysis
- Hot Temperature
- Humans
- Mutation
- Structure-Activity Relationship
- Vibrio parahaemolyticus