Vibrio cholerae cytolysin recognizes the heptasaccharide core of complex N-glycans with nanomolar affinity.

ABSTRACT: Pathogens selectively target host cells using adhesion molecules and secreted virulence factors that may utilize protein, lipid, or carbohydrate ligands on the cell surface. The human intestinal pathogen Vibrio cholerae secretes a pore-forming toxin, V.cholerae cytolysin (VCC), which contains two domains that are structurally similar to known carbohydrate-binding proteins. These tandem domains are attached to the carboxy-terminus of the cytolytic domain and contain a β-trefoil fold and a β-prism fold. VCC has been shown to bind glycosylated proteins, and removal of the β-prism domain leads to a large decrease in lytic activity against rabbit erythrocytes. Despite these clues, the identity of the glycan receptors of VCC and the role of glycan binding in toxin activity remain unknown. To bet

SUBMITTER: Levan S 

PROVIDER: S-EPMC3578121 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature