Differential interaction of the two cholesterol‐dependent, membrane‐damaging toxins, streptolysin O and Vibrio cholerae cytolysin, with enantiomeric cholesterol

2003/09/24 by Alexander Zitzer, Emily J. Westover, Douglas F. Covey +1 · 3 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Medicine · #Bacteria #Bacterial protein #Biochemistry #Biology #Chemistry #Cholera toxin #Cholesterol #Cytolysin #Lipid Membrane Structure and Behavior #Liposome #Membrane #Microbiology #Streptococcal Infections and Treatments #Streptolysin #Toxin #Vibrio bacteria research studies #Vibrio cholerae

paper · pdf · doi:10.1016/s0014-5793(03)01023-8

openalex publication_date 2003/09/24 · openalex created_date 2016/06/24 · openalex updated_date 2026/08/06

Abstract

Membrane cholesterol is essential to the activity of at least two structurally unrelated families of bacterial pore-forming toxins, represented by streptolysin O (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.

Citations

• Vesicles of variable sizes produced by a rapid extrusion procedure
• Structure of a Cholesterol-Binding, Thiol-Activated Cytolysin and a Model of Its Membrane Form
• Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin

Cited by

• Cholesterol Exposure at the Membrane Surface Is Necessary and Sufficient to Trigger Perfringolysin O Binding
• The Cholesterol-Dependent Cytolysin Family of Gram-Positive Bacterial Toxins
• Cholesterol-dependent cytolysin [wikipedia]