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

Alexander Zitzer; Emily J. Westover; Douglas F. Covey; Michael Palmer

doi:10.1016/S0014-5793(03)01023-8

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

Alexander Zitzer
, Emily J. Westover
, Douglas F. Covey
, Michael Palmer

Research output: Contribution to journal › Article › peer-review

42 Scopus citations

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.

Original language	English
Pages (from-to)	229-231
Number of pages	3
Journal	FEBS Letters
Volume	553
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(03)01023-8
State	Published - Oct 23 2003

Keywords

Cholesterol-binding cytolysins
Enantiomeric cholesterol
Protein-cholesterol interaction
Streptolysin O
Vibrio cholerae cytolysin

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10.1016/S0014-5793(03)01023-8

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

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.",

keywords = "Cholesterol-binding cytolysins, Enantiomeric cholesterol, Protein-cholesterol interaction, Streptolysin O, Vibrio cholerae cytolysin",

author = "Alexander Zitzer and Westover, \{Emily J.\} and Covey, \{Douglas F.\} and Michael Palmer",

note = "Funding Information: We thank Robert Bittman and Evan Mintzer for useful discussions. This work was supported by NSERC grant No. 250265-2003 GSC-032 (to M.P.), NIH GM47969 (to D.F.C.), the Lucille P. Markey Predoctoral Fellowship and Cardiovascular Research Training Grant NIH 55935 (to E.J.W.).",

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doi = "10.1016/S0014-5793(03)01023-8",

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T1 - Differential interaction of the two cholesterol-dependent, membrane-damaging toxins, streptolysin O and Vibrio cholerae cytolysin, with enantiomeric cholesterol

AU - Zitzer, Alexander

AU - Westover, Emily J.

AU - Covey, Douglas F.

AU - Palmer, Michael

N1 - Funding Information: We thank Robert Bittman and Evan Mintzer for useful discussions. This work was supported by NSERC grant No. 250265-2003 GSC-032 (to M.P.), NIH GM47969 (to D.F.C.), the Lucille P. Markey Predoctoral Fellowship and Cardiovascular Research Training Grant NIH 55935 (to E.J.W.).

PY - 2003/10/23

Y1 - 2003/10/23

N2 - 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.

AB - 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.

KW - Cholesterol-binding cytolysins

KW - Enantiomeric cholesterol

KW - Protein-cholesterol interaction

KW - Streptolysin O

KW - Vibrio cholerae cytolysin

UR - https://www.scopus.com/pages/publications/0142231450

U2 - 10.1016/S0014-5793(03)01023-8

DO - 10.1016/S0014-5793(03)01023-8

M3 - Article

C2 - 14572629

AN - SCOPUS:0142231450

SN - 0014-5793

VL - 553

SP - 229

EP - 231

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

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

Abstract

Keywords

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