6533b851fe1ef96bd12aa27f
RESEARCH PRODUCT
Differential interaction of the two cholesterol-dependent, membrane-damaging toxins, streptolysin O and Vibrio cholerae cytolysin, with enantiomeric cholesterol.
Michael PalmerEmily J. WestoverAlexander ZitzerDouglas F. Coveysubject
Cell Membrane Permeabilitygenetic structuresBiophysicsBiologymedicine.disease_causeBiochemistrySubstrate Specificity03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsStructural Biologyotorhinolaryngologic diseasesGeneticsmedicineStreptolysin OMolecular BiologyVibrio cholerae030304 developmental biology0303 health sciencesLiposomeVibrio cholerae cytolysinCholesterolToxinCytotoxinsEnantiomeric cholesterol030302 biochemistry & molecular biologyMembranes ArtificialStereoisomerismCell BiologyFluoresceinseye diseasesRecombinant ProteinsCholesterol-binding cytolysinsMembraneCholesterolchemistryBiochemistryVibrio choleraeLiposomesStreptolysinsProtein–cholesterol interactionlipids (amino acids peptides and proteins)Streptolysinsense organsCytolysinEnantiomerProtein Bindingdescription
AbstractMembrane 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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2003-10-24 | FEBS letters |