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dc.creatorAlape Girón, Alberto
dc.creatorFlores Díaz, Marietta
dc.creatorGuillouard, Isabelle
dc.creatorNaylor, Claire E.
dc.creatorTitball, Richard
dc.creatorRucavado Romero, Alexandra
dc.creatorLomonte, Bruno
dc.creatorBasak, Ajit K.
dc.creatorGutiérrez, José María
dc.creatorCole, Steward T.
dc.creatorThelestam, Mónica
dc.date.accessioned2017-01-30T14:38:26Z
dc.date.available2017-01-30T14:38:26Z
dc.date.issued2000-08
dc.identifier.citationhttp://onlinelibrary.wiley.com/doi/10.1046/j.1432-1327.2000.01588.x/abstract;jsessionid=C9CB49492B0F301FFEFD4283817CDE46.f03t01es_ES
dc.identifier.issn1742-4658
dc.identifier.urihttp://hdl.handle.net/10669/29468
dc.description.abstractClostridium 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.sponsorshipUniversidad de Costa Rica/[741-98-287]/UCR/Costa Ricaes_ES
dc.description.sponsorshipSwedish Cancer Society/[3826-B96-01XAB]//Sueciaes_ES
dc.description.sponsorshipConsejo Nacional de Investigaciones Científicas y Tecnológicas de Costa Rica//CONICIT/Costa Ricaes_ES
dc.description.sponsorshipSwedish Medical Research Council/[16X-05969]//Sueciaes_ES
dc.description.sponsorshipKarolinska Institutet Research Funds///Sueciaes_ES
dc.language.isoen_USes_ES
dc.sourceEuropean Journal of Biochemistry; Volumen 267, Número 16. 2000es_ES
dc.subjectBacterial Toxinses_ES
dc.subjectMuscular Diseaseses_ES
dc.subjectMolecular Modelses_ES
dc.subjectSkeletal Musclees_ES
dc.subjectCell Survivales_ES
dc.titleIdentification of residues critical for toxicity in Clostridium perfringens phospholipase C, the key toxin in gas gangrenees_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1046/j.1432-1327.2000.01588.x
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.codproyecto741-98-287
dc.identifier.pmid10931204


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