Clostridium perfringens Enterotoxin: The Toxin Forms Highly Cation-Selective Channels in Lipid Bilayers
| Autor: | Michel R. Popoff, Roland Benz |
|---|---|
| Přispěvatelé: | Department of Life Sciences and Chemistry [Bremen], Jacobs University [Bremen], Toxines bactériennes - Bacterial Toxins, Institut Pasteur [Paris] (IP), The authors would like to thank Eva Waltenberger and Serge Pauillac for expert technical assistance., Institut Pasteur [Paris] |
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
pore-forming toxins Health Toxicology and Mutagenesis viruses [SDV]Life Sciences [q-bio] 030106 microbiology lcsh:Medicine MESH: Vero Cells Enterotoxin [SDV.BC]Life Sciences [q-bio]/Cellular Biology [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC] Toxicology medicine.disease_cause Article 03 medical and health sciences chemistry.chemical_compound MESH: Propidium/metabolism MESH: Chlorocebus aethiops clostridium perfringens enterotoxin (CPE) [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB] medicine MESH: Animals Propidium iodide Lipid bilayer Ion transporter MESH: Clostridium perfringens Pore-forming toxin cation-selectivity MTT-test lcsh:R MESH: Enterotoxins/toxicity propidium iodide uptake Clostridium perfringens biochemical phenomena metabolism and nutrition [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology MESH: Ion Channels/metabolism MESH: Lipid Bilayers/metabolism lipid bilayer membrane 030104 developmental biology Membrane channel formation [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology chemistry Biophysics Cation transport |
| Zdroj: | Toxins Toxins, 2018, 10 (9), pp.341. ⟨10.3390/toxins10090341⟩ Toxins, Vol 10, Iss 9, p 341 (2018) Toxins, MDPI, 2018, 10 (9), pp.341. ⟨10.3390/toxins10090341⟩ Volume 10 Issue 9 |
| ISSN: | 2072-6651 |
| Popis: | International audience; One of the numerous toxins produced by Clostridium perfringens is Clostridium perfringens enterotoxin (CPE), a polypeptide with a molecular mass of 35.5 kDa exhibiting three different domains. Domain one is responsible for receptor binding, domain two is involved in hexamer formation and domain three has to do with channel formation in membranes. CPE is the major virulence factor of this bacterium and acts on the claudin-receptor containing tight junctions between epithelial cells resulting in various gastrointestinal diseases. The activity of CPE on Vero cells was demonstrated by the entry of propidium iodide (PI) in the cells. The entry of propidium iodide caused by CPE was well correlated with the loss of cell viability monitored by the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) test. CPE formed ion-permeable channels in artificial lipid bilayer membranes with a single-channel conductance of 620 pS in 1 M KCl. The single-channel conductance was not a linear function of the bulk aqueous salt concentration indicating that point-negative charges at the CPE channel controlled ion transport. This resulted in the high cation selectivity of the CPE channels, which suggested that anions are presumably not permeable through the CPE channels. The possible role of cation transport by CPE channels in disease caused by C. perfringens is discussed. |
| Databáze: | OpenAIRE |
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