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http://conacyt.repositorioinstitucional.mx/jspui/handle/1000/8464| Virion morphology and on-virus spike protein structures of diverse SARS-CoV-2 variants | |
| Zunlong Ke Thomas Peacock Jonathan Brown Carol Sheppard Tristan Croll Abhay Kotecha Daniel Goldhill Wendy Barclay John Briggs | |
| Acceso Abierto | |
| Atribución-NoComercial-SinDerivadas | |
| https://doi.org/10.1101/2023.12.21.572824 | |
| https://www.biorxiv.org/content/10.1101/2023.12.21.572824v1 | |
| The evolution of SARS-CoV-2 variants with increased fitness has been accompanied by structural changes in the spike (S) proteins that are the major target for the adaptive immune response. Single-particle cryo-EM analysis of soluble S from SARS-CoV-2 variants has revealed this structural adaptation at high-resolution. The analysis of S trimers in situ on intact virions has the potential to provide more functionally relevant insights into S structure and virion morphology. Here, we characterized B.1, Alpha, Beta, Gamma, Delta, Kappa, and Mu variants by cryo-electron microscopy and tomography, assessing S cleavage, virion morphology, S incorporation, “in-situ” high-resolution S structures and the range of S conformational states. We found no evidence for adaptive changes in virion morphology, but describe multiple different positions in the S protein where amino acid changes alter local protein structure. Considered together, our data is consistent with a model where amino acid changes at multiple positions from the top to the base of the spike cause structural changes that can modulate the conformational dynamics of S. | |
| bioRxiv | |
| 22-12-2023 | |
| Preimpreso | |
| Inglés | |
| Público en general | |
| VIRUS RESPIRATORIOS | |
| Aparece en las colecciones: | Materiales de Consulta y Comunicados Técnicos |
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| Virion morphology and on-virus spike protein structures of diverse SARS-CoV-2 variants.pdf | 4.23 MB | Adobe PDF | Visualizar/Abrir |