ArticleJournal of molecular biology2013
Vibrio cholerae cytolysin recognizes the heptasaccharide core of complex N-glycans with nanomolar affinity.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Enigmatic roles ofJournal of bacteriology · 2025Review
- Pore Formation by Pore Forming Proteins in Lipid Membranes: Structural Insights Through Cryo-EM.The Journal of membrane biology · 2025Review
- Overview of Bacterial Protein Toxins from Pathogenic Bacteria: Mode of Action and Insights into Evolution.Toxins · 2024Review
- Structural basis for calcium-stimulating pore formation of Vibrio α-hemolysin.Nature communications · 2023Article
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Review
- Glycan Array Technology.Advances in biochemical engineering/biotechnology · 2021Article
- Spatiotemporal Regulation ofToxins · 2020Review
- Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis.Nature communications · 2020Article
- Vibiro vulnificus hemolysin associates with gangliosides.BMC microbiology · 2020Article
- The 1.9 Å crystal structure of the extracellular matrix protein Bap1 fromThe Journal of biological chemistry · 2019Article
- Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB.Nature communications · 2018Article
- Structural basis of mammalian glycan targeting by Vibrio cholerae cytolysin and biofilm proteins.PLoS pathogens · 2018Article
- Haemolytic actinoporins interact with carbohydrates using their lipid-binding module.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Article
- NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold.Scientific reports · 2017Article
- Article
- Article
- Pore-forming toxins: ancient, but never really out of fashion.Nature reviews. Microbiology · 2016Review
- The Relationship between Glycan Binding and Direct Membrane Interactions in Vibrio cholerae Cytolysin, a Channel-forming Toxin.The Journal of biological chemistry · 2015Article
- Glycan specificity of the Vibrio vulnificus hemolysin lectin outlines evolutionary history of membrane targeting by a toxin family.Journal of molecular biology · 2014Article
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3 authors.
Funding
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 better understand this specificity, we used a combination of structural and functional approaches to characterize the carbohydrate-binding activity of the VCC toxin. We first probed the monosaccharide-binding activity of VCC and demonstrated that the toxin exhibits millimolar affinity for aldohexoses. To understand this specificity, we solved the crystal structure of the VCC β-prism domain bound to methyl-α-mannose. Next, we utilized a mammalian glycan screen to determine that the β-prism domain preferentially binds complex N-glycans with a heptasaccharide GlcNAc(4)Man(3) core (NGA2). Fluorescence anisotropy and surface plasmon resonance indicated an approximately 100-nM affinity of the β-prism domain for the heptasaccharide core. Our results suggest that carbohydrate-binding domains on the VCC toxin facilitate high-affinity targeting of mammalian cell membranes, which may contribute to the ability of VCC to lyse cells at picomolar concentrations.
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