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Interaction of Human ACE2 to Membrane-Bound SARS-CoV-1 and SARS-CoV-2 S Glycoproteins

1
Centre de Recherche du CHUM, Montréal, QC H2X 0A9, Canada
2
Department of Microbiology and Immunology, McGill University, Montréal, QC H3A 2B4, Canada
3
Infectious Disease Division, Department of Medicine, Uniformed Services University of the Health Sciences, Bethesda, MD 20814–4712, USA
4
Departement de Microbiologie, Infectiologie et Immunologie, Université de Montréal, Montréal, QC H2X 0A9, Canada
5
Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19104, USA
*
Author to whom correspondence should be addressed.
Viruses 2020, 12(10), 1104; https://doi.org/10.3390/v12101104
Received: 3 September 2020 / Revised: 21 September 2020 / Accepted: 24 September 2020 / Published: 29 September 2020
(This article belongs to the Section Antivirals & Vaccines)
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. View Full-Text
Keywords: Coronavirus; SARS-CoV-1; SARS-CoV-2; spike glycoproteins; human ACE2 receptor; ACE2-Fc; CR3022 antibody; neutralization; COVID-19 Coronavirus; SARS-CoV-1; SARS-CoV-2; spike glycoproteins; human ACE2 receptor; ACE2-Fc; CR3022 antibody; neutralization; COVID-19
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Anand, S.P.; Chen, Y.; Prévost, J.; Gasser, R.; Beaudoin-Bussières, G.; Abrams, C.F.; Pazgier, M.; Finzi, A. Interaction of Human ACE2 to Membrane-Bound SARS-CoV-1 and SARS-CoV-2 S Glycoproteins. Viruses 2020, 12, 1104.

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