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

• Published in: FEBS letters Vol. 553; no. 3; pp. 229 - 231
• Main Authors: Zitzer, Alexander, Westover, Emily J, Covey, Douglas F, Palmer, Michael
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 23.10.2003
• Subjects: Bacterial Proteins; Cell Membrane Permeability; Cholesterol - chemistry; Cholesterol - metabolism; Cholesterol-binding cytolysins; Cytotoxins - metabolism; Enantiomeric cholesterol; Fluoresceins - metabolism; Liposomes - chemistry; Liposomes - metabolism; Membranes, Artificial; Protein Binding; Protein–cholesterol interaction; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Stereoisomerism; Streptolysin O; Streptolysins - genetics; Streptolysins - metabolism; Substrate Specificity; Vibrio cholerae - chemistry; Vibrio cholerae cytolysin; Vibrio cholerae cytolysin; Enantiomeric cholesterol; Streptolysin O; Protein–cholesterol interaction; Cholesterol-binding cytolysins
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(03)01023-8

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.