Binding of cholesterol by sulfhydryl-activated cytolysins

Author:

Johnson M K,Geoffroy C,Alouf J E

Abstract

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.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

Reference21 articles.

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3. Interaction between membranes and cytolytic bacterial toxins;Bernheimer A. W.;Biochim. Biophys. Acta,1974

4. Bernheimer A. W. 1976. Sulfhydryl activated toxins p. 85-97. In A. W. Bernheimer (ed.) Mechanisms of bacterial toxinology. John Wiley & Sons Inc. New York.

5. Inactivation of pneumococcal hemolysin by certain sterols;Cohen B.;Proc. Soc. Exp. Biol. Med.,1937

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