Structural basis of receptor recognition by SARS-CoV-2

A novel severe acute respiratory syndrome (SARS)-like coronavirus (SARS-CoV-2) recently emerged and is rapidly spreading in humans, causing COVID-19 . A key to tackling this pandemic is to understand the receptor recognition mechanism of the virus, which regulates its infectivity, pathogenesis and h...

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Bibliographic Details
Published in:Nature (London) 2020-05, Vol.581 (7807), p.221-224
Main Authors: Shang, Jian, Ye, Gang, Shi, Ke, Wan, Yushun, Luo, Chuming, Aihara, Hideki, Geng, Qibin, Auerbach, Ashley, Li, Fang
Format: Article
Language:English
Subjects:
ACE2
Analysis
Angiotensin
Angiotensin converting enzyme
Angiotensin-Converting Enzyme 2
Animals
Betacoronavirus - chemistry
Betacoronavirus - drug effects
Betacoronavirus - metabolism
Binding
Binding Sites
China - epidemiology
Chiroptera - virology
Coronaviridae
Coronavirus - chemistry
Coronavirus - isolation & purification
Coronavirus Infections - drug therapy
Coronavirus Infections - epidemiology
Coronavirus Infections - transmission
Coronavirus Infections - virology
Coronaviruses
COVID-19
Crystal structure
Crystallization
Crystallography, X-Ray
Crystals
Disease hot spots
Disease Reservoirs - virology
Disease transmission
Eutheria - virology
Host range
Humans
Hydrogen bonds
Infectivity
Membrane proteins
Models, Molecular
Pandemics
Pathogenesis
Peptidyl-dipeptidase A
Peptidyl-Dipeptidase A - chemistry
Peptidyl-Dipeptidase A - metabolism
Pneumonia, Viral - drug therapy
Pneumonia, Viral - epidemiology
Pneumonia, Viral - transmission
Pneumonia, Viral - virology
Protein Binding
Protein Domains
Protein Stability
Proteins
Radioligand assay
Receptors
Receptors, Virus - chemistry
Receptors, Virus - metabolism
SARS-CoV-2
Severe acute respiratory syndrome
Severe acute respiratory syndrome coronavirus 2
Severe acute respiratory syndrome-related coronavirus - chemistry
Spike Glycoprotein, Coronavirus - chemistry
Spike Glycoprotein, Coronavirus - genetics
Spike Glycoprotein, Coronavirus - metabolism
Spike protein
Structure
Target recognition
Viral diseases
Viruses
Zoonoses - epidemiology
Zoonoses - transmission
Zoonoses - virology
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Summary:A novel severe acute respiratory syndrome (SARS)-like coronavirus (SARS-CoV-2) recently emerged and is rapidly spreading in humans, causing COVID-19 . 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 . 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.
ISSN:0028-0836
1476-4687
DOI:10.1038/s41586-020-2179-y