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dc.rights.licenseopenen_US
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorCARLON-ANDRES, Irene
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorLAGADEC, Floriane
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorPIED, Noemie
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorRAYNE, Fabienne
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorLAFON, Marie-Edith
dc.contributor.authorKEHLENBACH, Ralph H
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorWODRICH, Harald
dc.date.accessioned2023-11-13T12:06:09Z
dc.date.available2023-11-13T12:06:09Z
dc.date.issued2020-05-04
dc.identifier.issn1098-5514en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/184729
dc.description.abstractEnNuclear import of viral genomes is an important step during the life cycle of adenoviruses (AdV), requiring soluble cellular factors as well as proteins of the nuclear pore complex (NPC). We addressed the role of the cytoplasmic nucleoporin Nup358 during adenoviral genome delivery by performing depletion/reconstitution experiments and time-resolved quantification of adenoviral genome import. Nup358-depleted cells displayed reduced efficiencies of nuclear import of adenoviral genomes, and the nuclear import receptor transportin 1 became rate limiting under these conditions. Furthermore, we identified a minimal N-terminal region of Nup358 that was sufficient to compensate for the import defect. Our data support a model where Nup358 functions as an assembly platform that promotes the formation of transport complexes, allowing AdV to exploit a physiological protein import pathway for accelerated transport of its DNA. Nuclear import of viral genomes is an essential step to initiate productive infection for several nuclear replicating DNA viruses. On the other hand, DNA is not a physiological nuclear import substrate; consequently, viruses have to exploit existing physiological transport routes. Here, we show that adenoviruses use the nucleoporin Nup358 to increase the efficiency of adenoviral genome import. In its absence, genome import efficiency is reduced and the transport receptor transportin 1 becomes rate limiting. We show that the N-terminal half of Nup358 is sufficient to drive genome import and identify a transportin 1 binding region. In our model, adenovirus genome import exploits an existing protein import pathway and Nup358 serves as an assembly platform for transport complexes.
dc.language.isoENen_US
dc.subject.enActive Transport
dc.subject.enCell Nucleus
dc.subject.enAdenoviridae
dc.subject.enGenome
dc.subject.enViral
dc.subject.enHEK293 Cells
dc.subject.enHeLa Cells
dc.subject.enHumans
dc.subject.enMolecular Chaperones
dc.subject.enNuclear Pore
dc.subject.enNuclear Pore Complex Proteins
dc.subject.enProtein Transport
dc.subject.enReceptors
dc.subject.enCytoplasmic and Nuclear
dc.subject.enbeta Karyopherins
dc.title.enNup358 and Transportin 1 Cooperate in Adenoviral Genome Import.
dc.title.alternativeJ Virolen_US
dc.typeArticle de revueen_US
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologieen_US
dc.identifier.pubmed32161167en_US
bordeaux.journalJournal of Virologyen_US
bordeaux.volume94en_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.issue10en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcepubmed
hal.identifierhal-04282169
hal.version1
hal.date.transferred2023-11-13T12:06:12Z
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exporttrue
workflow.import.sourcepubmed
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Journal%20of%20Virology&rft.date=2020-05-04&rft.volume=94&rft.issue=10&rft.eissn=1098-5514&rft.issn=1098-5514&rft.au=CARLON-ANDRES,%20Irene&LAGADEC,%20Floriane&PIED,%20Noemie&RAYNE,%20Fabienne&LAFON,%20Marie-Edith&rft.genre=article


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