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Impact of temperature on the affinity of SARS-CoV-2 Spike glycoprotein for host ACE2. 2021
Jérémie Prévost, and
Jonathan Richard, and
Romain Gasser, and
Shilei Ding, and
Clément Fage, and
Sai Priya Anand, and
Damien Adam, and
Natasha Gupta Vergara, and
Alexandra Tauzin, and
Mehdi Benlarbi, and
Shang Yu Gong, and
Guillaume Goyette, and
Anik Privé, and
Sandrine Moreira, and
Hugues Charest, and
Michel Roger, and
Walther Mothes, and
Marzena Pazgier, and
Emmanuelle Brochiero, and
Guy Boivin, and
Cameron F Abrams, and
Arne Schön, and
Andrés Finzi
Centre de Recherche du CHUM, axe Immunopathologie, Montreal, Quebec, Canada; Département de Microbiologie, Infectiologie et Immunologie, Université de Montréal, Montreal, Quebec, Canada.
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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