Open AccessStudies on the Mechanism of Action of Oxygen-labile Haemolysins
Author(s) -
Mark Johnson,
Kathryn S. Aultman
Publication year - 1977
Publication title -
journal of general microbiology/journal of general microbiology
Language(s) - English
Resource type - Journals
eISSN - 2059-9323
pISSN - 0022-1287
DOI - 10.1099/00221287-101-2-237
Subject(s) - pneumolysin , streptolysin , lytic cycle , lysis , hemolysin , lysin , cytolysis , haemolysis , mechanism of action , chemistry , biochemistry , hemolysis , microbiology and biotechnology , biology , in vitro , cytotoxicity , escherichia coli , immunology , virulence , bacterial protein , bacteriophage , virus , gene
The sensitivities of the binding step and the lytic step of haemolysis by pneumolysin to the action of various inhibitors and to variations in the assay conditions were studied. Binding was inhibited by HgCl2 and N-ethylmaleimide. Lysis by previously fixed lysin was insensitive to HgCl2 and only slightly sensitive to N-ethylmaleimide. Binding of pneumolysin was independent of ionic strength. Binding of pneumolysin and streptolysin O decreased above pH 8-0 and 8-4 respectively. These results suggest that binding requires a non-ionized unsubstituted sulphydryl group. Incubation of erythrocytes with NaF caused inhibition of pneumolysin, indicating that some metabolic function of the cell may be involved in lysis. The action of streptolysin O was not affected by NaF.