Binding of cholesterol by sulfhydryl-activated cytolysins.

AUTOR(ES)

Johnson, M K

RESUMO

The binding of cholesterol by pneumolysin, alveolysin, and streptolysin O has been demonstrated. The properties of the cytolysin-cholesterol interaction parallel those of cytolysin-erythrocyte interaction in that the reaction is rapid, temperature independent, decreased at elevated pH, and shows the same specificity with respect to other related sterols. However, oxidized or p-hydroxymercuribenzoate-treated thoxin showed no decrease in cholesterol-binding activity, whereas the ability of cytolysin to bind to erythrocytes was modified by such treatment.

Documentos Relacionados

• Purification, characterization, and toxicity of the sulfhydryl-activated hemolysin listeriolysin O from Listeria monocytogenes.
• Antigenic relationships among thiol-activated cytolysins.
• Molecular cloning, characterization, and complete nucleotide sequence of the gene for pneumolysin, the sulfhydryl-activated toxin of Streptococcus pneumoniae.
• Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins
• LYSIS OF ESCHERICHIA COLI BY SULFHYDRYL-BINDING REAGENTS