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Identification of residues critical for toxicity in Clostridium perfringens phospholipase C, the key toxin in gas gangrene
dc.creator | Alape Girón, Alberto | |
dc.creator | Flores Díaz, Marietta | |
dc.creator | Guillouard, Isabelle | |
dc.creator | Naylor, Claire E. | |
dc.creator | Titball, Richard | |
dc.creator | Rucavado Romero, Alexandra | |
dc.creator | Lomonte, Bruno | |
dc.creator | Basak, Ajit K. | |
dc.creator | Gutiérrez, José María | |
dc.creator | Cole, Steward T. | |
dc.creator | Thelestam, Mónica | |
dc.date.accessioned | 2017-01-30T14:38:26Z | |
dc.date.available | 2017-01-30T14:38:26Z | |
dc.date.issued | 2000-08 | |
dc.identifier.citation | http://onlinelibrary.wiley.com/doi/10.1046/j.1432-1327.2000.01588.x/abstract;jsessionid=C9CB49492B0F301FFEFD4283817CDE46.f03t01 | |
dc.identifier.issn | 1742-4658 | |
dc.identifier.uri | https://hdl.handle.net/10669/29468 | |
dc.description.abstract | Clostridium perfringens phospholipase C (PLC), also called α-toxin, is the major virulence factor in the pathogenesis of gas gangrene. The toxic activities of genetically engineered α-toxin variants harboring single amino-acid substitutions in three loops of its C-terminal domain were studied. The substitutions were made in aspartic acid residues which bind calcium, and tyrosine residues of the putative membrane-interacting region. The variants D269N and D336N had less than 20% of the hemolytic activity and displayed a cytotoxic potency 103-fold lower than that of the wild-type toxin. The variants in which Tyr275, Tyr307, and Tyr331 were substituted by Asn, Phe, or Leu had 11–73% of the hemolytic activity and exhibited a cytotoxic potency 102- to 105-fold lower than that of the wild-type toxin. The results demonstrated that the sphingomyelinase activity and the C-terminal domain are required for myotoxicity in vivo and that the variants D269N, D336N, Y275N, Y307F, and Y331L had less than 12% of the myotoxic activity displayed by the wild-type toxin. This work therefore identifies residues critical for the toxic activities of C. perfringens PLC and provides new insights toward understanding the mechanism of action of this toxin at a molecular level. | es_ES |
dc.description.sponsorship | Universidad de Costa Rica/[741-98-287]/UCR/Costa Rica | es_ES |
dc.description.sponsorship | Swedish Cancer Society/[3826-B96-01XAB]//Suecia | es_ES |
dc.description.sponsorship | Consejo Nacional de Investigaciones Científicas y Tecnológicas de Costa Rica//CONICIT/Costa Rica | es_ES |
dc.description.sponsorship | Swedish Medical Research Council/[16X-05969]//Suecia | es_ES |
dc.description.sponsorship | Karolinska Institutet Research Funds///Suecia | es_ES |
dc.language.iso | en_US | es_ES |
dc.source | European Journal of Biochemistry; Volumen 267, Número 16. 2000 | es_ES |
dc.subject | Bacterial Toxins | es_ES |
dc.subject | Muscular Diseases | es_ES |
dc.subject | Molecular Models | es_ES |
dc.subject | Skeletal Muscle | es_ES |
dc.subject | Cell Survival | es_ES |
dc.title | Identification of residues critical for toxicity in Clostridium perfringens phospholipase C, the key toxin in gas gangrene | es_ES |
dc.type | artículo original | |
dc.identifier.doi | 10.1046/j.1432-1327.2000.01588.x | |
dc.description.procedence | UCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP) | es_ES |
dc.identifier.codproyecto | 741-98-287 | |
dc.identifier.pmid | 10931204 |
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Microbiología [1170]