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dc.rights.licenseopenen_US
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorKHARE, Shashank
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorVILLALBA, Miryam
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorCANUL-TEC, Juan
hal.structure.identifierUniversité de Bâle = University of Basel = Basel Universität [Unibas]
dc.contributor.authorCAJIAO, Arantza
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorKUMAR, Anand
hal.structure.identifierVirologie Structurale - Structural Virology
dc.contributor.authorBACKOVIC, Marija
hal.structure.identifierVirologie Structurale - Structural Virology
dc.contributor.authorREY, Felix
hal.structure.identifierVrije Universiteit Brussel [Bruxelles] [VUB]
hal.structure.identifierVIB-VUB Center for Structural Biology [Bruxelles]
dc.contributor.authorPARDON, Els
hal.structure.identifierVrije Universiteit Brussel [Bruxelles] [VUB]
hal.structure.identifierVIB-VUB Center for Structural Biology [Bruxelles]
dc.contributor.authorSTEYAERT, Jan
hal.structure.identifierUniversité de Bâle = University of Basel = Basel Universität [Unibas]
hal.structure.identifierUniversity of Georgia [USA]
dc.contributor.authorPEREZ, Camilo
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorREYES, Nicolas
dc.date.accessioned2025-02-18T08:04:48Z
dc.date.available2025-02-18T08:04:48Z
dc.date.issued2024-09
dc.identifier.issn1545-9993en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/204994
dc.description.abstractEnHuman syncytin-1 and suppressyn are cellular proteins of retroviral origin involved in cell-cell fusion events to establish the maternal-fetal interface in the placenta. In cell culture, they restrict infections from members of the largest interference group of vertebrate retroviruses, and are regarded as host immunity factors expressed during development. At the core of the syncytin-1 and suppressyn functions are poorly understood mechanisms to recognize a common cellular receptor, the membrane transporter ASCT2. Here, we present cryo-electron microscopy structures of human ASCT2 in complexes with the receptor-binding domains of syncytin-1 and suppressyn. Despite their evolutionary divergence, the two placental proteins occupy similar positions in ASCT2, and are stabilized by the formation of a hybrid β-sheet or 'clamp' with the receptor. Structural predictions of the receptor-binding domains of extant retroviruses indicate overlapping binding interfaces and clamping sites with ASCT2, revealing a competition mechanism between the placental proteins and the retroviruses. Our work uncovers a common ASCT2 recognition mechanism by a large group of endogenous and disease-causing retroviruses, and provides high-resolution views on how placental human proteins exert morphological and immunological functions.
dc.description.sponsorshipIntegrative Biology of Emerging Infectious Diseases - ANR-10-LABX-0062en_US
dc.language.isoENen_US
dc.subject.enElectron microscopy
dc.subject.enMembrane proteins
dc.subject.enStructural biology
dc.subject.enViral membrane fusion
dc.title.enReceptor-recognition and antiviral mechanisms of retrovirus-derived human proteins
dc.typeArticle de revueen_US
dc.identifier.doi10.1038/s41594-024-01295-6en_US
dc.subject.halSciences du Vivant [q-bio]en_US
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologieen_US
dc.identifier.pubmed38671230en_US
dc.description.sponsorshipEuropeTransport and Receptor Mechanisms of Human Solute Carriersen_US
bordeaux.journalNature Structural and Molecular Biologyen_US
bordeaux.page1368 - 1376en_US
bordeaux.volume31en_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.issue9en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcehal
hal.identifierpasteur-04947831
hal.version1
hal.popularnonen_US
hal.audienceInternationaleen_US
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=Nature%20Structural%20and%20Molecular%20Biology&rft.date=2024-09&rft.volume=31&rft.issue=9&rft.spage=1368%20-%201376&rft.epage=1368%20-%201376&rft.eissn=1545-9993&rft.issn=1545-9993&rft.au=KHARE,%20Shashank&VILLALBA,%20Miryam&CANUL-TEC,%20Juan&CAJIAO,%20Arantza&KUMAR,%20Anand&rft.genre=article


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