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http://conacyt.repositorioinstitucional.mx/jspui/handle/1000/7296| A single de novo substitution in SARS-CoV-2 spike informs enhanced adherence to human ACE2. | |
| Elena Erausquin JACINTO LOPEZ SAGASETA | |
| Acceso Abierto | |
| Atribución-NoComercial | |
| https://doi.org/10.1101/2021.07.16.452441 | |
| https://www.biorxiv.org/content/10.1101/2021.07.16.452441v1 | |
| SARS-CoV-2 initiates colonization of host cells by binding to cell membrane ACE2 receptor. This binding is mediated by the viral spike receptor binding domain (RBD). The COVID-19 pandemic has brought devastating consequences at a clinical, social and economical levels. Therefore, anticipation of potential novel SARS-causing species or SARS-CoV-2 variants with enhanced binding to ACE2 is key in the prevention of future threats to come. We have characterized a de novo single substitution, Q498Y, in SARS-CoV-2 RBD that confers stronger adherence to ACE2. While the SARS-CoV-2 beta variant, which includes three simultaneous amino acid replacements, induces a 4-fold stronger affinity, a single Q498Y substitution results in 2.5-fold tighter binding, compared to the Wuhan-Hu-1 SARS-CoV-2 2019 strain. Additionally, we crystallized RBDQ498Y complexed with ACE2 and provide here the structural basis for this enhanced affinity. These studies inform a rationale for prevention of potential SARS-causing viruses to come. | |
| biorxiv | |
| 16-07-2021 | |
| Preimpreso | |
| www.biorxiv.org | |
| Inglés | |
| Epidemia COVID-19 | |
| Público en general | |
| VIRUS RESPIRATORIOS | |
| Versión publicada | |
| publishedVersion - Versión publicada | |
| Aparece en las colecciones: | Artículos científicos |
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| A single novo substitution in SARS COV2 spike informs.pdf | 7.03 MB | Adobe PDF | Visualizar/Abrir |