Please use this identifier to cite or link to this item: https://hdl.handle.net/10316/109792
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dc.contributor.authorSilva, Daniela S.-
dc.contributor.authorPereira, Liliana M. G.-
dc.contributor.authorMoreira, Ana R.-
dc.contributor.authorFerreira-da-Silva, Frederico-
dc.contributor.authorBrito, Rui M.-
dc.contributor.authorFaria, Tiago Q.-
dc.contributor.authorZornetta, Irene-
dc.contributor.authorMontecucco, Cesare-
dc.contributor.authorOliveira, Pedro-
dc.contributor.authorAzevedo, Jorge E.-
dc.contributor.authorPereira, Pedro J. B.-
dc.contributor.authorMacedo-Ribeiro, Sandra-
dc.contributor.authordo Vale, Ana-
dc.contributor.authordos Santos, Nuno M. S.-
dc.date.accessioned2023-10-27T08:35:54Z-
dc.date.available2023-10-27T08:35:54Z-
dc.date.issued2013-02-
dc.identifier.issn1553-7374pt
dc.identifier.urihttps://hdl.handle.net/10316/109792-
dc.description.abstractAIP56 (apoptosis-inducing protein of 56 kDa) is a major virulence factor of Photobacterium damselae piscicida (Phdp), a Gram-negative pathogen that causes septicemic infections, which are among the most threatening diseases in mariculture. The toxin triggers apoptosis of host macrophages and neutrophils through a process that, in vivo, culminates with secondary necrosis of the apoptotic cells contributing to the necrotic lesions observed in the diseased animals. Here, we show that AIP56 is a NF-κB p65-cleaving zinc-metalloprotease whose catalytic activity is required for the apoptogenic effect. Most of the bacterial effectors known to target NF-κB are type III secreted effectors. In contrast, we demonstrate that AIP56 is an A-B toxin capable of acting at distance, without requiring contact of the bacteria with the target cell. We also show that the N-terminal domain cleaves NF-κB at the Cys(39)-Glu(40) peptide bond and that the C-terminal domain is involved in binding and internalization into the cytosol.pt
dc.language.isoengpt
dc.publisherPublic Library of Sciencept
dc.relationDaniela S. Silva and Liliana M. G. Pereira were funded by FCT fellowships SFRH/BD/35865/2007 and SFRH/BD/43501/2008, respectively. Ana do Vale was supported by Programa Cieˆncia – funded by POPH - QREN - Tipologia 4.2 - Promoc¸a˜o do Emprego Cientı´fico, co-funded by Fundo Social Europeu and National funding from MCTES. This work was supported by FCT projects PTDC/BIA-PRO/101111/2008, PTDC/CVT/099544/2008 PTDC/MAR/101143/2008 and PEst-C/SAU/ LA0002/2011 (EU-FEDER funding through COMPETE).pt
dc.rightsopenAccesspt
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt
dc.subject.meshAnimalspt
dc.subject.meshApoptosispt
dc.subject.meshApoptosis Regulatory Proteinspt
dc.subject.meshBacterial Toxinspt
dc.subject.meshBasspt
dc.subject.meshFish Diseasespt
dc.subject.meshHost-Pathogen Interactionspt
dc.subject.meshLeukocytespt
dc.subject.meshMetalloproteasespt
dc.subject.meshPhotobacteriumpt
dc.subject.meshRecombinant Proteinspt
dc.subject.meshTranscription Factor RelApt
dc.subject.meshVirulence Factorspt
dc.titleThe apoptogenic toxin AIP56 is a metalloprotease A-B toxin that cleaves NF-κb P65pt
dc.typearticle-
degois.publication.firstPagee1003128pt
degois.publication.issue2pt
degois.publication.titlePLoS Pathogenspt
dc.peerreviewedyespt
dc.identifier.doi10.1371/journal.ppat.1003128pt
degois.publication.volume9pt
dc.date.embargo2013-02-01*
uc.date.periodoEmbargo0pt
item.cerifentitytypePublications-
item.languageiso639-1en-
item.fulltextCom Texto completo-
item.grantfulltextopen-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypearticle-
crisitem.author.researchunitCQC - Coimbra Chemistry Centre-
crisitem.author.researchunitCNC - Center for Neuroscience and Cell Biology-
crisitem.author.parentresearchunitFaculty of Sciences and Technology-
crisitem.author.orcid0000-0001-9128-2557-
crisitem.author.orcid0000-0003-0564-8415-
Appears in Collections:FCTUC Química - Artigos em Revistas Internacionais
I&D CNC - Artigos em Revistas Internacionais
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