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Toxicon. 2001 Nov;39(11):1681-9.

The family of thiol-activated, cholesterol-binding cytolysins.

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Department of Medical Biochemistry and Genetics, Texas A&M University, 440 Reynolds Medical Building, College Station, TX 77843-1114, USA.


Several species of both pathogenic and non-pathogenic grampositive bacteria within the genera Streptococcus, Clostridium and Bacillus secrete cytolytic proteins that belong to a single, highly homologous family. The most widely known members of this family are streptolysin O, listeriolysin, perfringolysin, and pneumolysin. These toxins specifically require membrane cholesterol but, apparently, do not depend on any other specific cell surface receptor, so that they are able to lyse the cytoplasmic membranes of virtually any animal cell. Upon binding as monomers, they oligomerize to form large pores with up to 30 nm internal diameter. These are the largest pores known, permitting permeation not only of ions and small metabolites but also of macromolecules. The latter property renders these toxins useful tools in cell biology. While several of these cytolysins have been shown to be determinants of bacterial pathogenicity, their biological roles may vary, as do the lifestyles of the bacteria secreting them. A unique function is surely fulfilled by listeriolysin O, which helps the intracellular pathogen Listeria monocytogenes escape from phagolysosomes and then spread to adjacent host cells.

[Indexed for MEDLINE]

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