The Cholesterol-Dependent Cytolysin Family of Gram-Positive Bacterial Toxins

2010/01/01 by Alejandro P. Heuck, Paul C. Moe, Benjamin B. Johnson · 1 citation
Biochemistry, Genetics and Molecular Biology · Medicine · #Antimicrobial Resistance in Staphylococcus #Bacterial Identification and Susceptibility Testing #Streptococcal Infections and Treatments

paper · doi:10.1007/978-90-481-8622-8_20

crossref issued 2010/01/01 · crossref published 2010/01/01 · crossref published-print 2010/01/01 · openalex publication_date 2010/01/01 · crossref published-online 2010/02/24 · crossref created 2010/03/05 · crossref deposited 2021/10/24 · openalex created_date 2025/10/10 · crossref indexed 2026/03/08 · openalex updated_date 2026/08/04

Citations

• Structure of a Cholesterol-Binding, Thiol-Activated Cytolysin and a Model of Its Membrane Form
• Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin
• Identification of a Membrane-Spanning Domain of the Thiol-Activated Pore-Forming Toxin Clostridium perfringens Perfringolysin O: An α-Helical to β-Sheet Transition Identified by Fluorescence Spectroscopy
• Characterization of a Streptococcal Cholesterol-Dependent Cytolysin with a Lewis y and b Specific Lectin Domain
• Differential interaction of the two cholesterol‐dependent, membrane‐damaging toxins, streptolysin O and Vibrio cholerae cytolysin, with enantiomeric cholesterol
• Monomer-Monomer Interactions Drive the Prepore to Pore Conversion of a β-Barrel-forming Cholesterol-dependent Cytolysin
• Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit β-strand alignment
• How Interaction of Perfringolysin O with Membranes Is Controlled by Sterol Structure, Lipid Structure, and Physiological Low pH
• Prepore to pore transition of a cholesterol-dependent cytolysin visualized by electron microscopy
• Conformational Changes That Effect Oligomerization and Initiate Pore Formation Are Triggered throughout Perfringolysin O upon Binding to Cholesterol
• Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions
• Structural Basis of Pore Formation by the Bacterial Toxin Pneumolysin
• The Mechanism of Membrane Insertion for a Cholesterol-Dependent Cytolysin
• Effect of lipidic factors on membrane cholesterol topology — mode of binding of θ-toxin to cholesterol in liposomes
• Differential function of Listeria monocytogenes listeriolysin O and phospholipases C in vacuolar dissolution following cell-to-cell spread
• Synergistic Effects of Alpha-Toxin and Perfringolysin O in Clostridium perfringens -Mediated Gas Gangrene
• Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins
• Vertical collapse of a cytolysin prepore moves its transmembrane β‐hairpins to the membrane
• Cholesterol Exposure at the Membrane Surface Is Necessary and Sufficient to Trigger Perfringolysin O Binding
• Cholesterol interactions with phospholipids in membranes

Cited by

• Cholesterol-dependent cytolysin [wikipedia]