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Helicobacter pullorum cytolethal distending toxin targets vinculin and cortactin and triggers formation of lamellipodia in intestinal epithelial cells

dc.contributor.authorVaron, C.
dc.contributor.authorMocan, I.
dc.contributor.authorMihi, B.
dc.contributor.authorPéré-Védrenne, C.
dc.contributor.authorAboubacar, A.
dc.contributor.authorMoraté, C.
dc.contributor.authorOleastro, M.
dc.contributor.authorDoignon, F.
dc.contributor.authorLaharie, D.
dc.contributor.authorMégraud, F.
dc.contributor.authorMénard, A.
dc.date.accessioned2015-02-19T13:53:17Z
dc.date.available2015-02-19T13:53:17Z
dc.date.issued2014-02-15
dc.description.abstractHelicobacter pullorum, a bacterium initially isolated from poultry, has been associated with human digestive disorders. However, the factor responsible for its cytopathogenic effects on epithelial cells has not been formally identified. The cytopathogenic alterations induced by several human and avian H. pullorum strains were investigated on human intestinal epithelial cell lines. Moreover, the effects of the cytolethal distending toxin (CDT) were evaluated first by using a wild-type strain and its corresponding cdtB isogenic mutant and second by delivering the active CdtB subunit of the CDT directly into the cells. All of the H. pullorum strains induced cellular distending phenotype, actin cytoskeleton remodeling, and G2/M cell cycle arrest. These effects were dependent on the CDT, as they were (1) not observed in response to a cdtB isogenic mutant strain and (2) present in cells expressing CdtB. CdtB also induced an atypical delocalization of vinculin from focal adhesions to the perinuclear region, formation of cortical actin-rich large lamellipodia with an upregulation of cortactin, and decreased cellular adherence. In conclusion, the CDT of H. pullorum is responsible for major cytopathogenic effects in vitro, confirming its role as a main virulence factor of this emerging human pathogen.por
dc.description.sponsorshipThis work was supported by the Institut national de la santé et de la recherche médicale, the University Bordeaux Segalen, the Conseil Régional d’Aquitaine (grants 20030304002FA and 20040305003 FA), the Société Nationale Française de Gastroentérologie, the European Union (FEDER no. 2003227)por
dc.identifier.citationJ Infect Dis. 2014 Feb 15;209(4):588-99. doi: 10.1093/infdis/jit539por
dc.identifier.doi10.1093/infdis/jit539
dc.identifier.issn0022-1899
dc.identifier.urihttp://hdl.handle.net/10400.18/2922
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherOxford University Press/Infectious Diseases Society of America
dc.relationEC/FP7/2003227por
dc.relation.publisherversionhttp://jid.oxfordjournals.org/content/209/4/588.longpor
dc.subjectHelicobacter pullorumpor
dc.subjectActinpor
dc.subjectAdherencepor
dc.subjectCortactinpor
dc.subjectCytolethal Distending Toxinpor
dc.subjectEpithelial Cellspor
dc.subjectIsogenic Mutantpor
dc.subjectLamellipodiapor
dc.subjectLentiviruspor
dc.subjectVinculinpor
dc.subjectInfecções Gastrointestinaispor
dc.titleHelicobacter pullorum cytolethal distending toxin targets vinculin and cortactin and triggers formation of lamellipodia in intestinal epithelial cellspor
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage599por
oaire.citation.startPage588por
oaire.citation.titleJournal of Infectious Diseasespor
oaire.citation.volume209por
rcaap.rightsopenAccesspor
rcaap.typearticlepor

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