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

Jérémie Prévost, Jonathan Richard, Romain asser, Shilei Ding, Clément Fage, Sai Priya Anand, Damien Adam, Natasha Gupta Vergara, Alexandra auzin, Mehdi Benlarbi, Shang Yu Gong, Guillaume oyette, Anik Privé, Sandrine Moreira, Hugues Charest, Michel Roger, Walther Mothes, Marzena Pazgier, Emmanuelle Brochiero, Guy BoivinCameron F. Abrams, Arne Schön, Andrés Finzi*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

Abstract

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 angiotensinconverting 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.

Original languageEnglish
Article number101151
JournalJournal of Biological Chemistry
Volume297
Issue number4
DOIs
StatePublished - 1 Oct 2021
Externally publishedYes

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