Molecular interaction and inhibition of SARS-CoV-2 binding to the ACE2 receptor.
A549 Cells
Angiotensin-Converting Enzyme 2
Betacoronavirus
/ metabolism
Binding Sites
COVID-19
Coronavirus Infections
/ metabolism
Humans
Models, Molecular
Pandemics
Peptidyl-Dipeptidase A
/ chemistry
Pneumonia, Viral
/ metabolism
Protein Binding
Protein Interaction Domains and Motifs
Receptors, Virus
/ metabolism
SARS-CoV-2
Spike Glycoprotein, Coronavirus
/ chemistry
Virus Attachment
Virus Internalization
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
11 09 2020
11 09 2020
Historique:
received:
09
07
2020
accepted:
18
08
2020
entrez:
12
9
2020
pubmed:
13
9
2020
medline:
24
9
2020
Statut:
epublish
Résumé
Study of the interactions established between the viral glycoproteins and their host receptors is of critical importance for a better understanding of virus entry into cells. The novel coronavirus SARS-CoV-2 entry into host cells is mediated by its spike glycoprotein (S-glycoprotein), and the angiotensin-converting enzyme 2 (ACE2) has been identified as a cellular receptor. Here, we use atomic force microscopy to investigate the mechanisms by which the S-glycoprotein binds to the ACE2 receptor. We demonstrate, both on model surfaces and on living cells, that the receptor binding domain (RBD) serves as the binding interface within the S-glycoprotein with the ACE2 receptor and extract the kinetic and thermodynamic properties of this binding pocket. Altogether, these results provide a picture of the established interaction on living cells. Finally, we test several binding inhibitor peptides targeting the virus early attachment stages, offering new perspectives in the treatment of the SARS-CoV-2 infection.
Identifiants
pubmed: 32917884
doi: 10.1038/s41467-020-18319-6
pii: 10.1038/s41467-020-18319-6
pmc: PMC7486399
doi:
Substances chimiques
Receptors, Virus
0
Spike Glycoprotein, Coronavirus
0
spike protein, SARS-CoV-2
0
Peptidyl-Dipeptidase A
EC 3.4.15.1
ACE2 protein, human
EC 3.4.17.23
Angiotensin-Converting Enzyme 2
EC 3.4.17.23
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4541Commentaires et corrections
Type : ErratumIn
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