Impact of temperature on the affinity of SARS-CoV-2 Spike for ACE2
Jeremie Prevost; Jonathan Richard; Romain Gasser; Shilei Ding; Clement Fage; Sai Priya Anand; Damien Adam; Natasha Gupta Vergara; Alexandra Tauzin; Mehdi Benlarbi; Shang Yu Gong; Guillaume Goyette; Anik Prive; Sandrine Moreira; Hugues Charest; Michel Roger; Walther Mothes; Marzena Pazgier; Emanuelle Brochiero; Guy Boivin; Cameron F Abrams; Arne Schon; Andres Finzi.
Preprint
en Inglés
| PREPRINT-BIORXIV | ID: ppbiorxiv-451812
The seasonal nature in the outbreaks of respiratory viral infections with increased transmission during low temperatures has been well established. The current COVID-19 pandemic makes no exception, and temperature has been suggested to play a role on the viability and transmissibility of SARS-CoV-2. The receptor binding domain (RBD) of the Spike glycoprotein binds to the angiotensin-converting enzyme 2 (ACE2) to initiate viral fusion. Studying 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 to 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, bypassed this requirement. This data suggests that the acquisition of N501Y reflects an adaptation to warmer climates, a hypothesis that remains to be tested.
Texto completo
Documentos relacionados