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Selective autophagy impedes KSHV entry after recruiting the membrane damage sensor galectin-8 to virus-containing endosomes.

dc.rights.licenseopenen_US
dc.contributor.authorSCHMIDT, Katarina Wendy
dc.contributor.authorMONTESPAN, Charlotte
dc.contributor.authorTHOMPSON, Danielle
dc.contributor.authorLUCAS, Miriam S
dc.contributor.authorLIGEON, Laure-Anne
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorWODRICH, Harald
dc.contributor.authorHAHN, Alexander S
dc.contributor.authorGREBER, Urs F
dc.contributor.authorMÜNZ, Christian
dc.date.accessioned2024-12-04T09:35:21Z
dc.date.available2024-12-04T09:35:21Z
dc.date.issued2024-11-26
dc.identifier.issn2211-1247en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/203684
dc.description.abstractEnKaposi sarcoma-associated herpesvirus (KSHV) is an oncogenic γ-herpesvirus. Autophagy during KSHV entry has remained unexplored. We show that LC3 lipidation as a hallmark of autophagy is induced shortly after KSHV entry. LC3 co-localizes with KSHV in amphisomes during entry and loss of LC3 lipidation increases infection. Accordingly, NDP52, a receptor of selective autophagy, was recruited to endocytosed viral particles, and its reduction increased KSHV infection. Additionally, virus particles co-localized with the endolysosome damage sensor galectin-8 upon KSHV entry and depletion of galectin-8 promoted KSHV infection. Compared with herpes simplex virus, listeriolysin, adenovirus, and influenza virus, and in contrast to what was previously thought about enveloped viruses, KSHV binding to EphA2 by its envelope protein gH causes endolysosomal membrane damage, akin to non-enveloped viruses and bacteria. Taken together, our study identifies an important anti-viral role for galectin-8, NDP52, and the autophagy machinery at virus-damaged endosomes, restricting KSHV entry by selective autophagy.
dc.language.isoENen_US
dc.title.enSelective autophagy impedes KSHV entry after recruiting the membrane damage sensor galectin-8 to virus-containing endosomes.
dc.title.alternativeCell Repen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1016/j.celrep.2024.115019en_US
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologieen_US
dc.identifier.pubmed39602307en_US
bordeaux.journalCell Reportsen_US
bordeaux.page115019en_US
bordeaux.volume43en_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.issue12en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcepubmed
hal.identifierhal-04818206
hal.version1
hal.date.transferred2024-12-04T09:35:23Z
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=Cell%20Reports&rft.date=2024-11-26&rft.volume=43&rft.issue=12&rft.spage=115019&rft.epage=115019&rft.eissn=2211-1247&rft.issn=2211-1247&rft.au=SCHMIDT,%20Katarina%20Wendy&MONTESPAN,%20Charlotte&THOMPSON,%20Danielle&LUCAS,%20Miriam%20S&LIGEON,%20Laure-Anne&rft.genre=article


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