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Impact of temperature on the affinity of SARS-CoV-2 Spike glycoprotein for host ACE2
Journal article   Open access   Peer reviewed

Impact of temperature on the affinity of SARS-CoV-2 Spike glycoprotein for host ACE2

Jérémie Prévost, Jonathan Richard, Romain Gasser, Shilei Ding, Clément Fage, Sai Priya Anand, Damien Adam, Natasha Gupta Vergara, Alexandra Tauzin, Mehdi Benlarbi, …
The Journal of biological chemistry, v 297(4), 101151
Oct 2021
PMID: 34478710
url
https://doi.org/10.1016/j.jbc.2021.101151View
Published, Version of Record (VoR)CC BY V4.0 Open

Abstract

ACE2 coronavirus COVID-19 N501Y neutralization RBD SARS-CoV-2 Spike glycoproteins temperature variants of concern
The seasonal nature of outbreaks of respiratory viral infections with increased transmission during low temperatures has been well established. Accordingly, temperature has been suggested to play a role on the viability and transmissibility of SARS-CoV-2, the virus responsible for the COVID-19 pandemic. The receptor-binding domain (RBD) of the Spike glycoprotein is known to bind to its host receptor angiotensin-converting enzyme 2 (ACE2) to initiate viral fusion. Using biochemical, biophysical, and functional assays to dissect the effect of temperature on the receptor–Spike interaction, we observed a significant and stepwise increase in RBD-ACE2 affinity at low temperatures, resulting in slower dissociation kinetics. This translated into enhanced interaction of the full Spike glycoprotein with the ACE2 receptor and higher viral attachment at low temperatures. Interestingly, the RBD N501Y mutation, present in emerging variants of concern (VOCs) that are fueling the pandemic worldwide (including the B.1.1.7 (α) lineage), bypassed this requirement. This data suggests that the acquisition of N501Y reflects an adaptation to warmer climates, a hypothesis that remains to be tested.

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Collaboration types
Domestic collaboration
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Web of Science research areas
Biochemistry & Molecular Biology
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