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Structural basis of receptor recognition by SARS-CoV-2.

Authors :
Shang J
Ye G
Shi K
Wan Y
Luo C
Aihara H
Geng Q
Auerbach A
Li F
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.

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