ArticleBiochemistry2008
Characterization of a streptococcal cholesterol-dependent cytolysin with a lewis y and b specific lectin domain.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 65 citations in OpenAlex.
- Insights into the Protein-Lipid Interaction of Perivitellin-2, an Unusual Snail Pore-Forming Toxin.Toxins · 2025Article
- F-type lectins: Structural and functional aspects, and potential biomedical applications.BBA advances · 2025Article
- Cholesterol-dependent cytolysins: The outstanding questions.IUBMB life · 2022Review
- Structure of the Streptococcus pyogenes NADJournal of bacteriology · 2022Article
- Dual functions of discoidinolysin, a cholesterol-dependent cytolysin with N-terminal discoidin domain produced fromJournal of oral microbiology · 2022Article
- 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
- Immunotherapy targeting the Streptococcus pyogenes M protein or streptolysin O to treat or prevent influenza A superinfection.PloS one · 2020Article
- The Structural Basis for a Transition State That Regulates Pore Formation in a Bacterial Toxin.mBio · 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
- The Distribution of Lectins across the Phylum Nematoda: A Genome-Wide Search.International journal of molecular 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
- Insights into the Evolutionary Relationships of LytA Autolysin and Ply Pneumolysin-Like Genes in Streptococcus pneumoniae and Related Streptococci.Genome biology and evolution · 2015Article
- Dual modes of membrane binding direct pore formation by Streptolysin O.Molecular microbiology · 2015Article
- Blood Groups in Infection and Host Susceptibility.Clinical microbiology reviews · 2015Review
- The cytolytic activity of vaginolysin strictly depends on cholesterol and is potentiated by human CD59.Toxins · 2015Article
- A novel cholesterol-insensitive mode of membrane binding promotes cytolysin-mediated translocation by Streptolysin O.Molecular microbiology · 2014Article
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
The cholesterol-dependent cytolysins (CDCs) are a large family of pore-forming toxins that often exhibit distinct structural changes that modify their pore-forming activity. A soluble platelet aggregation factor from Streptococcus mitis (Sm-hPAF) was characterized and shown to be a functional CDC with an amino-terminal fucose-binding lectin domain. Sm-hPAF, or lectinolysin (LLY) as renamed herein, is most closely related to CDCs from Streptococcus intermedius (ILY) and Streptococcus pneumoniae (pneumolysin or PLY). The LLY gene was identified in strains of S. mitis, S. pneumoniae, and Streptococcus pseudopneumoniae. LLY induces pore-dependent changes in the light scattering properties of the platelets that mimic those induced by platelet aggregation but does not induce platelet aggregation. LLY monomers form the typical large homooligomeric membrane pore complex observed for the CDCs. The pore-forming activity of LLY on platelets is modulated by the amino-terminal lectin domain, a structure that is not present in other CDCs. Glycan microarray analysis showed the lectin domain is specific for difucosylated glycans within Lewis b (Le (b)) and Lewis y (Le (y)) antigens. The glycan-binding site is occluded in the soluble monomer of LLY but is apparently exposed after cell binding, since it significantly increases LLY pore-forming activity in a glycan-dependent manner. Hence, LLY represents a new class of CDC whose pore-forming mechanism is modulated by a glycan-binding domain.
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