Receptor-recognition and antiviral mechanisms of retrovirus-derived human proteins
dc.rights.license | open | en_US |
hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
dc.contributor.author | KHARE, Shashank | |
hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
dc.contributor.author | VILLALBA, Miryam | |
hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
dc.contributor.author | CANUL-TEC, Juan | |
hal.structure.identifier | Université de Bâle = University of Basel = Basel Universität [Unibas] | |
dc.contributor.author | CAJIAO, Arantza | |
hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
dc.contributor.author | KUMAR, Anand | |
hal.structure.identifier | Virologie Structurale - Structural Virology | |
dc.contributor.author | BACKOVIC, Marija | |
hal.structure.identifier | Virologie Structurale - Structural Virology | |
dc.contributor.author | REY, Felix | |
hal.structure.identifier | Vrije Universiteit Brussel [Bruxelles] [VUB] | |
hal.structure.identifier | VIB-VUB Center for Structural Biology [Bruxelles] | |
dc.contributor.author | PARDON, Els | |
hal.structure.identifier | Vrije Universiteit Brussel [Bruxelles] [VUB] | |
hal.structure.identifier | VIB-VUB Center for Structural Biology [Bruxelles] | |
dc.contributor.author | STEYAERT, Jan | |
hal.structure.identifier | Université de Bâle = University of Basel = Basel Universität [Unibas] | |
hal.structure.identifier | University of Georgia [USA] | |
dc.contributor.author | PEREZ, Camilo | |
hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
dc.contributor.author | REYES, Nicolas | |
dc.date.accessioned | 2025-02-18T08:04:48Z | |
dc.date.available | 2025-02-18T08:04:48Z | |
dc.date.issued | 2024-09 | |
dc.identifier.issn | 1545-9993 | en_US |
dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/204994 | |
dc.description.abstractEn | Human 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.sponsorship | Integrative Biology of Emerging Infectious Diseases - ANR-10-LABX-0062 | en_US |
dc.language.iso | EN | en_US |
dc.subject.en | Electron microscopy | |
dc.subject.en | Membrane proteins | |
dc.subject.en | Structural biology | |
dc.subject.en | Viral membrane fusion | |
dc.title.en | Receptor-recognition and antiviral mechanisms of retrovirus-derived human proteins | |
dc.type | Article de revue | en_US |
dc.identifier.doi | 10.1038/s41594-024-01295-6 | en_US |
dc.subject.hal | Sciences du Vivant [q-bio] | en_US |
dc.subject.hal | Sciences du Vivant [q-bio]/Microbiologie et Parasitologie | en_US |
dc.identifier.pubmed | 38671230 | en_US |
dc.description.sponsorshipEurope | Transport and Receptor Mechanisms of Human Solute Carriers | en_US |
bordeaux.journal | Nature Structural and Molecular Biology | en_US |
bordeaux.page | 1368 - 1376 | en_US |
bordeaux.volume | 31 | en_US |
bordeaux.hal.laboratories | MFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234 | en_US |
bordeaux.issue | 9 | en_US |
bordeaux.institution | CNRS | en_US |
bordeaux.peerReviewed | oui | en_US |
bordeaux.inpress | non | en_US |
bordeaux.import.source | hal | |
hal.identifier | pasteur-04947831 | |
hal.version | 1 | |
hal.popular | non | en_US |
hal.audience | Internationale | en_US |
hal.export | false | |
workflow.import.source | hal | |
dc.rights.cc | Pas de Licence CC | en_US |
bordeaux.COinS | ctx_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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