Mostrar el registro sencillo del ítem

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.f03t01
dc.identifier.issn1742-4658
dc.identifier.urihttps://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.typeartículo original
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


Ficheros en el ítem

Thumbnail

Este ítem aparece en la(s) siguiente(s) colección(ones)

Mostrar el registro sencillo del ítem