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The amphipathic helix of adenovirus capsid protein VI contributes to penton release and postentry sorting.

dc.rights.licenseopenen_US
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorMARTINEZ, Ruben
dc.contributor.authorSCHELLENBERGER, Pascale
dc.contributor.authorVASISHTAN, Daven
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorAKNIN, Cindy
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorAUSTIN, Sisley
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorDACHEUX, Denis
IDREF: 230332838
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorRAYNE, Fabienne
dc.contributor.authorSIEBERT, Alistair
hal.structure.identifierMax Von Pettenkofer Institute [MVP]
dc.contributor.authorRUZSICS, Zsolt
dc.contributor.authorGRUENEWALD, Kay
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorWODRICH, Harald
dc.date.accessioned2023-11-13T13:20:45Z
dc.date.available2023-11-13T13:20:45Z
dc.date.issued2015-02-01
dc.identifier.issn1098-5514en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/184734
dc.description.abstractEnNuclear delivery of the adenoviral genome requires that the capsid cross the limiting membrane of the endocytic compartment and traverse the cytosol to reach the nucleus. This endosomal escape is initiated upon internalization and involves a highly coordinated process of partial disassembly of the entering capsid to release the membrane lytic internal capsid protein VI. Using wild-type and protein VI-mutated human adenovirus serotype 5 (HAdV-C5), we show that capsid stability and membrane rupture are major determinants of entry-related sorting of incoming adenovirus virions. Furthermore, by using electron cryomicroscopy, as well as penton- and protein VI-specific antibodies, we show that the amphipathic helix of protein VI contributes to capsid stability by preventing premature disassembly and deployment of pentons and protein VI. Thus, the helix has a dual function in maintaining the metastable state of the capsid by preventing premature disassembly and mediating efficient membrane lysis to evade lysosomal targeting. Based on these findings and structural data from cryo-electron microscopy, we suggest a refined disassembly mechanism upon entry. In this study, we show the intricate connection of adenovirus particle stability and the entry-dependent release of the membrane-lytic capsid protein VI required for endosomal escape. We show that the amphipathic helix of the adenovirus internal protein VI is required to stabilize pentons in the particle while coinciding with penton release upon entry and that release of protein VI mediates membrane lysis, thereby preventing lysosomal sorting. We suggest that this dual functionality of protein VI ensures an optimal disassembly process by balancing the metastable state of the mature adenovirus particle.
dc.language.isoENen_US
dc.subject.enAdenoviruses
dc.subject.enHuman
dc.subject.enCapsid Proteins
dc.subject.enCell Line
dc.subject.enCryoelectron Microscopy
dc.subject.enHumans
dc.subject.enVirus Internalization
dc.subject.enVirus Uncoating
dc.title.enThe amphipathic helix of adenovirus capsid protein VI contributes to penton release and postentry sorting.
dc.title.alternativeJ Virolen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1128/JVI.02257-14en_US
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologieen_US
dc.identifier.pubmed25473051en_US
bordeaux.journalJournal of Virologyen_US
bordeaux.page2121-35en_US
bordeaux.volume89en_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.issue4en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcepubmed
hal.identifierhal-04282377
hal.version1
hal.date.transferred2023-11-13T13:20:48Z
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=2015-02-01&rft.volume=89&rft.issue=4&rft.spage=2121-35&rft.epage=2121-35&rft.eissn=1098-5514&rft.issn=1098-5514&rft.au=MARTINEZ,%20Ruben&SCHELLENBERGER,%20Pascale&VASISHTAN,%20Daven&AKNIN,%20Cindy&AUSTIN,%20Sisley&rft.genre=article


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