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Structural basis of receptor recognition by SARS-CoV-2.
- Source :
-
Nature [Nature] 2020 May; Vol. 581 (7807), pp. 221-224. Date of Electronic Publication: 2020 Mar 30. - Publication Year :
- 2020
-
Abstract
- A novel severe acute respiratory syndrome (SARS)-like coronavirus (SARS-CoV-2) recently emerged and is rapidly spreading in humans, causing COVID-19 <superscript>1,2</superscript> . A key to tackling this pandemic is to understand the receptor recognition mechanism of the virus, which regulates its infectivity, pathogenesis and host range. SARS-CoV-2 and SARS-CoV recognize the same receptor-angiotensin-converting enzyme 2 (ACE2)-in humans <superscript>3,4</superscript> . Here we determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 (engineered to facilitate crystallization) in complex with ACE2. In comparison with the SARS-CoV RBD, an ACE2-binding ridge in SARS-CoV-2 RBD has a more compact conformation; moreover, several residue changes in the SARS-CoV-2 RBD stabilize two virus-binding hotspots at the RBD-ACE2 interface. These structural features of SARS-CoV-2 RBD increase its ACE2-binding affinity. Additionally, we show that RaTG13, a bat coronavirus that is closely related to SARS-CoV-2, also uses human ACE2 as its receptor. The differences among SARS-CoV-2, SARS-CoV and RaTG13 in ACE2 recognition shed light on the potential animal-to-human transmission of SARS-CoV-2. This study provides guidance for intervention strategies that target receptor recognition by SARS-CoV-2.
- Subjects :
- Angiotensin-Converting Enzyme 2
Animals
Betacoronavirus drug effects
Betacoronavirus metabolism
Binding Sites
COVID-19
China epidemiology
Chiroptera virology
Coronavirus chemistry
Coronavirus isolation & purification
Coronavirus Infections drug therapy
Coronavirus Infections epidemiology
Coronavirus Infections transmission
Coronavirus Infections virology
Crystallization
Crystallography, X-Ray
Disease Reservoirs virology
Eutheria virology
Humans
Models, Molecular
Pandemics
Pneumonia, Viral drug therapy
Pneumonia, Viral epidemiology
Pneumonia, Viral transmission
Pneumonia, Viral virology
Protein Binding
Protein Domains
Protein Stability
Severe acute respiratory syndrome-related coronavirus chemistry
SARS-CoV-2
Spike Glycoprotein, Coronavirus genetics
Zoonoses epidemiology
Zoonoses transmission
Betacoronavirus chemistry
Peptidyl-Dipeptidase A chemistry
Peptidyl-Dipeptidase A metabolism
Receptors, Virus chemistry
Receptors, Virus metabolism
Spike Glycoprotein, Coronavirus chemistry
Spike Glycoprotein, Coronavirus metabolism
Zoonoses virology
Subjects
Details
- Language :
- English
- ISSN :
- 1476-4687
- Volume :
- 581
- Issue :
- 7807
- Database :
- MEDLINE
- Journal :
- Nature
- Publication Type :
- Academic Journal
- Accession number :
- 32225175
- Full Text :
- https://doi.org/10.1038/s41586-020-2179-y