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http://conacyt.repositorioinstitucional.mx/jspui/handle/1000/8083| Sialoglycan binding triggers spike opening in a human coronavirus | |
| Matti Pronker Robert Creutznacher Ieva Drulyte Ruben Hulswit Zeshi Li Frank van Kuppeveld Joost Snijder Yifei Lang Berend-Jan Bosch Geert-Jan Boons Martin Frank Raoul J. de Groot Daniel Hurdiss | |
| Acceso Abierto | |
| Atribución-NoComercial-SinDerivadas | |
| https://doi.org/10.1101/2023.04.20.536837 | |
| https://www.biorxiv.org/content/10.1101/2023.04.20.536837v1 | |
| Abstract Coronavirus (CoV) spikes mediate receptor binding and membrane fusion, making them prime targets for neutralising antibodies. In the cases of SARS-CoV, SARS-CoV-2, and MERS-CoV, spikes transition freely between open and closed conformations to balance host cell attachment and immune evasion. The open conformation exposes domain S1B, allowing it to bind to proteinaceous cell surface receptors. It also facilitates protein refolding during spike-mediated membrane fusion. However, with a single exception, the pre-fusion spikes of all other CoVs studied so far have been observed exclusively in the closed state. This raises the possibility of regulation, where spikes more commonly transition to open states in response to specific cues, rather than spontaneously. In our study, using cryo-EM and molecular dynamics simulations, we show that the spike protein of the common cold human coronavirus HKU1 undergoes local and long-range conformational changes upon binding a sialoglycan-based primary receptor to domain S1A. This binding triggers the transition of S1B domains to the open state via allosteric inter-domain cross-talk. Our findings paint a more elaborate picture of CoV attachment, with possibilities of dual receptor usage and priming of entry as a means of immune escape. | |
| bioRxiv | |
| 20-04-2023 | |
| Preimpreso | |
| Inglés | |
| Público en general | |
| VIRUS RESPIRATORIOS | |
| Aparece en las colecciones: | Materiales de Consulta y Comunicados Técnicos |
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