Differential interaction of the two cholesterol-dependent, membrane-damaging toxins, streptolysin O and Vibrio cholerae cytolysin, with enantiomeric cholesterol.
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.
Department of Hematology and Oncology, Johannes Gutenberg University, D-55101 Mainz, Germany.
Alexander
A
Zitzer
Emily J
EJ
Westover
Douglas F
DF
Covey
Michael
M
Palmer
D001426:Bacterial Proteins; D002463:Cell Membrane Permeability; D002784:Cholesterol / Q000737:chemistry* / Q000378:metabolism*; D003603:Cytotoxins / Q000378:metabolism*; D005452:Fluoresceins / Q000378:metabolism; D008081:Liposomes / Q000737:chemistry / Q000378:metabolism; D008567:Membranes, Artificial; D011485:Protein Binding; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D013237:Stereoisomerism; D013301:Streptolysins / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity; D014734:Vibrio cholerae / Q000737:chemistry*
D001426:Bacterial Proteins; D003603:Cytotoxins; D005452:Fluoresceins; D008081:Liposomes; D008567:Membranes, Artificial; D011994:Recombinant Proteins; D013301:Streptolysins; C025964:streptolysin O; D002784:Cholesterol; C007740:fluorexon