Structural basis of receptor recognition by SARS-CoV-2
Date
2020Author
Shang, Jian
Ye, Gang
Shi, Ke
Wan, Yushun
Luo, Chuming
Aihara, Hideki
Geng, Qibin
Auerbach, Ashley
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Abstract
A novel severe acute respiratory syndrome (SARS)-like coronavirus (SARS-CoV-2)
recently emerged and is rapidly spreading in humans, causing COVID-191,2
. 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
humans3,4
. 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
afnity. Additionally, we show that RaTG13, a bat coronavirus that is closely related to
SARS-CoV-2, also uses human ACE2 as its receptor. The diferences 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.
Palabras clave
Structural basis; SARS-CoV-2; COVID-19Link to resource
https://doi.org/10.1038/s41586-020-2179-yCollections
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