Please use this identifier to cite or link to this item: https://covid-19.conacyt.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
Appears in Collections:Artículos científicos

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