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dc.rights.licenseopenen_US
dc.contributor.authorFLAUGNATTI, Nicolas
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorRAPISARDA, Chiara
dc.contributor.authorREY, Martial
dc.contributor.authorBEAUVOIS, Solène
dc.contributor.authorNGUYEN, Viet Anh
dc.contributor.authorCANAAN, Stéphane
dc.contributor.authorDURAND, Eric
dc.contributor.authorCHAMOT‐ROOKE, Julia
dc.contributor.authorCASCALES, E.
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorFRONZES, Rémi
dc.contributor.authorJOURNET, Laure
dc.date.accessioned2023-06-02T10:31:25Z
dc.date.available2023-06-02T10:31:25Z
dc.date.issued2020-06-02
dc.identifier.issn0261-4189en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/182445
dc.description.abstractEnThe bacterial type VI secretion system (T6SS) is a macromolecular machine that injects effectors into prokaryotic and eukaryotic cells. The mode of action of the T6SS is similar to contractile phages: the contraction of a sheath structure pushes a tube topped by a spike into target cells. Effectors are loaded onto the spike or confined into the tube. In enteroaggregative Escherichia coli, the Tle1 phospholipase binds the C-terminal extension of the VgrG trimeric spike. Here, we purify the VgrG-Tle1 complex and show that a VgrG trimer binds three Tle1 monomers and inhibits their activity. Using covalent cross-linking coupled to high-resolution mass spectrometry, we provide information on the sites of contact and further identify the requirement for a Tle1 N-terminal secretion sequence in complex formation. Finally, we report the 2.6-Å-resolution cryo-electron microscopy tri-dimensional structure of the (VgrG) 3-(Tle1) 3 complex revealing how the effector binds its cargo, and how VgrG inhibits Tle1 phospholipase activity. The inhibition of Tle1 phospholipase activity once bound to VgrG suggests that Tle1 dissociation from VgrG is required upon delivery.
dc.description.sponsorshipContribution des Effecteurs du Système de Sécrétion de Type VI à la pathogénicité des Escherichia coli adhérents-invasifsen_US
dc.description.sponsorshipGuerre bactérienne: Architecture et Fonction du Système de Sécrétion de Type VI - ANR-14-CE14-0006en_US
dc.description.sponsorshipBloc-outil et Imagerie de Précision pour le Binage Intra-rang Précoce - ANR-17-ROSE-0001en_US
dc.description.sponsorshipCibler le métabolisme des fibroblastes adventitiels activés pour traiter l'hypertension pulmonaire - ANR-20-CE14-0006en_US
dc.language.isoENen_US
dc.subject.entype VI secretion system
dc.subject.enStructural Biology
dc.subject.enVirology & Host Pathogen Interaction
dc.subject.entype VI secretion system Subject Categories Microbiology
dc.subject.enprotein secretion
dc.subject.encryo-electron microscopy
dc.subject.enbacterial toxin
dc.subject.enbacterial competition
dc.title.enStructural basis for loading and inhibition of a bacterial T6 SS phospholipase effector by the VgrG spike
dc.typeArticle de revueen_US
dc.identifier.doi10.15252/embj.2019104129en_US
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaireen_US
dc.subject.halSciences du Vivant [q-bio]en_US
dc.description.sponsorshipEuropeInfrastructure for NMR, EM and X-ray crystallography for translational researchen_US
bordeaux.journalEMBO Journalen_US
bordeaux.pagee104129en_US
bordeaux.volume39en_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.issue11en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcehal
hal.identifierhal-02915537
hal.version1
hal.exportfalse
workflow.import.sourcehal
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=EMBO%20Journal&rft.date=2020-06-02&rft.volume=39&rft.issue=11&rft.spage=e104129&rft.epage=e104129&rft.eissn=0261-4189&rft.issn=0261-4189&rft.au=FLAUGNATTI,%20Nicolas&RAPISARDA,%20Chiara&REY,%20Martial&BEAUVOIS,%20Sol%C3%A8ne&NGUYEN,%20Viet%20Anh&rft.genre=article


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