ArticleStructure (London, England : 1993)2012
Structure of the lectin regulatory domain of the cholesterol-dependent cytolysin lectinolysin reveals the basis for its lewis antigen specificity.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Microbial Lectin-Targeting Mucus: A Glycobioinformatic Approach.Methods in molecular biology (Clifton, N.J.) · 2025Article
- F-type lectins: Structural and functional aspects, and potential biomedical applications.BBA advances · 2025Article
- In Vitro and In Silico Studies of the Antimicrobial Activity of Prenylated Phenylpropanoids of Green Propolis and Their Derivatives against Oral Bacteria.Antibiotics (Basel, Switzerland) · 2024Article
- Identifying the molecular basis of Laminin N-terminal domain CaBiophysical journal · 2024Article
- Story of Pore-Forming Proteins from Deadly Disease-Causing Agents to Modern Applications with Evolutionary Significance.Molecular biotechnology · 2024Review
- Glycan Stability and Flexibility: Thermodynamic and Kinetic Characterization of Nonconventional Hydrogen Bonding in Lewis Antigens.Journal of the American Chemical Society · 2023Article
- Cholesterol-dependent cytolysins: The outstanding questions.IUBMB life · 2022Review
- Structure of the Streptococcus pyogenes NADJournal of bacteriology · 2022Article
- Proteome-wide prediction of bacterial carbohydrate-binding proteins as a tool for understanding commensal and pathogen colonisation of the vaginal microbiome.NPJ biofilms and microbiomes · 2021Article
- Review
- Interaction of Macrophages and Cholesterol-Dependent Cytolysins: The Impact on Immune Response and Cellular Survival.Toxins · 2020Review
- All major cholesterol-dependent cytolysins use glycans as cellular receptors.Science advances · 2020Article
- Human Serum Albumin Binds Streptolysin O (SLO) Toxin Produced by Group AFrontiers in immunology · 2020Article
- Membrane Binding, Cellular Cholesterol Content and Resealing Capacity Contribute to Epithelial Cell Damage Induced by Suilysin ofPathogens (Basel, Switzerland) · 2019Article
- Article
- An F-type lectin domain directs the activity of Streptosporangium roseum alpha-l-fucosidase.Glycobiology · 2018Article
- Cholesterol-dependent cytolysins: from water-soluble state to membrane pore.Biophysical reviews · 2018Review
- Haemolytic actinoporins interact with carbohydrates using their lipid-binding module.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Article
- F-Type Lectins: A Highly Diversified Family of Fucose-Binding Proteins with a Unique Sequence Motif and Structural Fold, Involved in Self/Non-Self-Recognition.Frontiers in immunology · 2017Review
- Pore-forming toxins: ancient, but never really out of fashion.Nature reviews. Microbiology · 2016Review
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8 authors.
Funding
Abstract
The cholesterol-dependent cytolysins (CDCs) punch holes in target cell membranes through a highly regulated process. Streptococcus mitis lectinolysin (LLY) exhibits another layer of regulation with a lectin domain that enhances the pore-forming activity of the toxin. We have determined the crystal structures of the lectin domain by itself and in complex with various glycans that reveal the molecular basis for the Lewis antigen specificity of LLY. A small-angle X-ray scattering study of intact LLY reveals the molecule is flat and elongated with the lectin domain oriented so that the Lewis antigen-binding site is exposed. We suggest that the lectin domain enhances the pore-forming activity of LLY by concentrating toxin molecules at fucose-rich sites on membranes, thus promoting the formation of prepore oligomers on the surface of susceptible cells.
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