Theβ-prism lectin domain of vibrio cholerae hemolysin promotes self-assembly of the β-pore-forming toxin by a carbohydrate-independent mechanism

Abstract

Background: Vibrio cholerae hemolysin is a pore-forming toxin with a β-prism lectin domain. Results: Although amphipathicity-driven interactions with lipids dominate membrane targeting, relocation of the lectin domain during toxin assembly generates entropy to push oligomerization and thereby promote pore formation. Conclusion: The lectin domain promotes toxin assembly by a carbohydrate-independent mechanism. Significance: A novel role for the lectin domain in protein oligomerization is revealed. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc..