Journal
FEBS LETTERS
Volume 553, Issue 3, Pages 229-231Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(03)01023-8
Keywords
streptolysin O; cholesterol-binding cytolysins; Vibrio cholerae cytolysin; protein-cholesterol interaction; enantiomeric cholesterol
Funding
- NIGMS NIH HHS [GM 47969] Funding Source: Medline
- PHS HHS [55935] Funding Source: Medline
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Membrane cholesterol is essential to the activity of at least two structurally unrelated families of bacterial pore-forming toxins, represented by streptolysin 0 (SLO) and Vibrio cholerae cytolysin (VCC), respectively. Here, we report that SLO and VCC differ sharply in their interaction with liposome membranes containing enantiomeric cholesterol (ent-cholesterol). VCC had very low activity with ent-cholesterol, which is in line with a stereospecific mode of interaction of this toxin with cholesterol. In contrast, SLO was only slightly less active with ent-cholesterol than with cholesterol, suggesting a rather limited degree of structural specificity in the toxin-cholesterol interaction. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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