Interaction of human ACE2 to membrane-bound SARS-CoV-1 and SARS-CoV-2 S glycoproteins

Sai Priya Anand, Yaozong Chen, Jérémie Prévost, Romain Gasser, Guillaume Beaudoin-Bussières, Cameron F. Abrams, Marzena Pazgier, Andrés Finzi*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


Severe acute respiratory syndrome virus 2 (SARS-CoV-2) is responsible for the current global coronavirus disease 2019 (COVID-19) pandemic, infecting millions of people and causing hundreds of thousands of deaths. The viral entry of SARS-CoV-2 depends on an interaction between the receptor-binding domain of its trimeric spike glycoprotein and the human angiotensin-converting enzyme 2 (ACE2) receptor. A better understanding of the spike/ACE2 interaction is still required to design anti-SARS-CoV-2 therapeutics. Here, we investigated the degree of cooperativity of ACE2 within both the SARS-CoV-2 and the closely related SARS-CoV-1 membrane-bound S glycoproteins. We show that there exist differential inter-protomer conformational transitions between both spike trimers. Interestingly, the SARS-CoV-2 spike exhibits a positive cooperativity for monomeric soluble ACE2 binding when compared to the SARS-CoV-1 spike, which might have more structural restraints. Our findings can be of importance in the development of therapeutics that block the spike/ACE2 interaction.

Original languageEnglish
Article number1104
Issue number10
StatePublished - Oct 2020
Externally publishedYes


  • ACE2-Fc
  • COVID-19
  • CR3022 antibody
  • Coronavirus
  • Human ACE2 receptor
  • Neutralization
  • SARS-CoV-1
  • SARS-CoV-2
  • Spike glycoproteins


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