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

Tytuł:: Impact of temperature on the affinity of SARS-CoV-2 Spike glycoprotein for host ACE2.
Autorzy:: Prévost J; Centre de Recherche du CHUM, axe Immunopathologie, Montreal, Quebec, Canada; Département de Microbiologie, Infectiologie et Immunologie, Université de Montréal, Montreal, Quebec, Canada.
Richard J; Centre de Recherche du CHUM, axe Immunopathologie, Montreal, Quebec, Canada; Département de Microbiologie, Infectiologie et Immunologie, Université de Montréal, Montreal, Quebec, Canada.
Gasser R; Centre de Recherche du CHUM, axe Immunopathologie, Montreal, Quebec, Canada; Département de Microbiologie, Infectiologie et Immunologie, Université de Montréal, Montreal, Quebec, Canada.
Ding S; Centre de Recherche du CHUM, axe Immunopathologie, Montreal, Quebec, Canada.
Fage C; Centre de Recherche du CHU de Québec, Université Laval, Quebec City, Quebec, Canada.
Anand SP; Centre de Recherche du CHUM, axe Immunopathologie, Montreal, Quebec, Canada; Department of Microbiology and Immunology, McGill University, Montreal, Quebec, Canada.
Adam D; Centre de Recherche du CHUM, axe Immunopathologie, Montreal, Quebec, Canada; Département de Médicine, Université de Montréal, Montréal, Quebec, Canada.
Gupta Vergara N; Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania, USA.
Tauzin A; Centre de Recherche du CHUM, axe Immunopathologie, Montreal, Quebec, Canada; Département de Microbiologie, Infectiologie et Immunologie, Université de Montréal, Montreal, Quebec, Canada.
Benlarbi M; Centre de Recherche du CHUM, axe Immunopathologie, Montreal, Quebec, Canada.
Gong SY; Centre de Recherche du CHUM, axe Immunopathologie, Montreal, Quebec, Canada; Department of Microbiology and Immunology, McGill University, Montreal, Quebec, Canada.
Goyette G; Centre de Recherche du CHUM, axe Immunopathologie, Montreal, Quebec, Canada.
Privé A; Centre de Recherche du CHUM, axe Immunopathologie, Montreal, Quebec, Canada.
Moreira S; Laboratoire de Santé Publique du Québec, Institut Nationale de Santé Publique du Québec, Sainte-Anne-de-Bellevue, Quebec, Canada.
Charest H; Laboratoire de Santé Publique du Québec, Institut Nationale de Santé Publique du Québec, Sainte-Anne-de-Bellevue, Quebec, Canada.
Roger M; Centre de Recherche du CHUM, axe Immunopathologie, Montreal, Quebec, Canada; Département de Microbiologie, Infectiologie et Immunologie, Université de Montréal, Montreal, Quebec, Canada; Laboratoire de Santé Publique du Québec, Institut Nationale de Santé Publique du Québec, Sainte-Anne-de-Bellevue, Quebec, Canada.
Mothes W; Department of Microbial Pathogenesis, Yale University School of Medicine, New Haven, Connecticut, USA.
Pazgier M; Infectious Disease Division, Department of Medicine, Uniformed Services University of the Health Sciences, Bethesda, Maryland, USA.
Brochiero E; Centre de Recherche du CHUM, axe Immunopathologie, Montreal, Quebec, Canada; Département de Médicine, Université de Montréal, Montréal, Quebec, Canada.
Boivin G; Centre de Recherche du CHU de Québec, Université Laval, Quebec City, Quebec, Canada.
Abrams CF; Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania, USA.
Schön A; Department of Biology, The Johns Hopkins University, Baltimore, Maryland, USA.
Finzi A; Centre de Recherche du CHUM, axe Immunopathologie, Montreal, Quebec, Canada; Département de Microbiologie, Infectiologie et Immunologie, Université de Montréal, Montreal, Quebec, Canada; Department of Microbiology and Immunology, McGill University, Montreal, Quebec, Canada. Electronic address: .
Źródło:: The Journal of biological chemistry [J Biol Chem] 2021 Oct; Vol. 297 (4), pp. 101151. Date of Electronic Publication: 2021 Aug 31.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
Język:: English
Imprint Name(s):: Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
MeSH Terms:: Angiotensin-Converting Enzyme 2/*metabolism
SARS-CoV-2/*metabolism
Spike Glycoprotein, Coronavirus/*metabolism
Angiotensin-Converting Enzyme 2/chemistry ; COVID-19/pathology ; COVID-19/virology ; Calorimetry ; Humans ; Interferometry ; Polymorphism, Single Nucleotide ; Protein Binding ; Protein Structure, Quaternary ; SARS-CoV-2/isolation & purification ; Spike Glycoprotein, Coronavirus/chemistry ; Temperature ; Thermodynamics
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Contributed Indexing:: Keywords: ACE2; COVID-19; N501Y; RBD; SARS-CoV-2; Spike glycoproteins; coronavirus; neutralization; temperature; variants of concern
Substance Nomenclature:: 0 (Spike Glycoprotein, Coronavirus)
0 (spike protein, SARS-CoV-2)
EC 3.4.17.23 (Angiotensin-Converting Enzyme 2)
Entry Date(s):: Date Created: 20210903 Date Completed: 20211110 Latest Revision: 20231107
Update Code:: 20240105
PubMed Central ID:: PMC8406544
DOI:: 10.1016/j.jbc.2021.101151
PMID:: 34478710
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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.
Competing Interests: Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.
(Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.)

Update of: bioRxiv. 2021 Jul 09;:. (PMID: 34268505)

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