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Updated: Feb 1, 2026

Vibrio cholerae: Model Organism to Study Bacterial Pathogenesis - Interview
Published on: May 28, 2007
Piercing the lipid raft: the case of Vibrio cholerae cytolysin
1Département de Biochimie et Médecine Moléculaire, Université de Montréal, Montréal, Canada normand.cyr@umontreal.ca.
Insights
Cholesterol is essential for the pore-forming toxin Vibrio cholerae cytolysin (VCC) to bind membranes and create functional pores. Membrane lipid rafts also facilitate VCC binding and pore formation during V. cholerae infection.
Area of Science:
- Biochemistry
- Molecular Biology
- Microbiology
Background:
- The pore-forming toxin Vibrio cholerae cytolysin (VCC) is crucial for V. cholerae pathogenesis.
- Understanding VCC's interaction with host cell membranes is key to developing therapeutic strategies.
Purpose of the Study:
- To investigate the role of cholesterol in VCC membrane binding and pore formation.
- To explore the influence of membrane microstructures on VCC activity.
Main Methods:
- Biochemical assays to assess VCC binding to lipid bilayers.
- Analysis of VCC oligomerization and pore formation in the presence of cholesterol and lipid rafts.
Main Results:
- Cholesterol significantly facilitates VCC membrane binding and is essential for functional pore formation.
- VCC retains membrane-binding capability via lipid rafts in the absence of cholesterol, mediated by non-lipid components.
- Cholesterol and membrane microstructures play critical roles in VCC binding, assembly, and cytolysis.
Conclusions:
- Cholesterol is a key determinant for VCC pore formation.
- Membrane lipid rafts provide alternative binding sites for VCC, influencing its cytolytic activity.
- These findings offer new insights into VCC-host cell interactions during V. cholerae infections.
Abstract:
In a recent issue of Biochemical Journal, Kathuria et al. [Biochem. J. (2018) 475, 3039-3055] report that membrane binding of the pore-forming toxin Vibrio cholerae cytolysin (VCC) is facilitated by the presence of cholesterol, and the presence of this sterol within the lipid bilayer is key for the formation of a functional pore. Yet, in the presence of accessory non-lipid components, VCC retains its membrane-binding capability likely through membrane lipid raft structures. In light of their results, the authors provide new insights into the roles of cholesterol and of membrane microstructures in the binding, the oligomeric assembly and the cytolytic pore formation of VCC which all take place following infection by V. cholerae.
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