OmniVira

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

Jian Shang1 Gang Ye1 Ke Shi2 Yushun Wan1 Chuming Luo1 Hideki Aihara2 Qibin Geng1 Ashley Auerbach1 Fang Li3
Affiliations 3 institutions
  1. Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, MN, USA.
  2. Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN, USA.
  3. Department of Veterinary and Biomedical Sciences, University of Minnesota, Saint Paul, MN, USA. [email protected].
PMID32225175 DOI10.1038/s41586-020-2179-y Year2020 Journal Nature Languageeng Publication statusActive
Active Last checked 2026-10-06 03:30:27 Source: NCBI PubMed

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 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.

Supporting text Virus Host Location
Angiotensin-Converting Enzyme 2 178 Animals 1981 Betacoronavirus 79 Binding Sites 90 China 234 Chiroptera 376 Coronavirus 93 Coronavirus Infections 172 COVID-19 427 Crystallization 5 Crystallography, X-Ray 32 Disease Reservoirs 149 Eutheria 9 Humans 1455 Models, Molecular 99 Pandemics 109 Peptidyl-Dipeptidase A 58 Pneumonia, Viral 42 Protein Binding 194 Protein Domains 45 Protein Stability 12 Receptors, Virus 208 SARS-CoV-2 456 Severe acute respiratory syndrome-related coronavirus 79

Evidence records

2 total
Functional Mechanism
2 records · 1 evidence types
Evidence type Receptor Usage
2 records
OVE3700 Receptor Usage
Key finding

SARS-CoV-2 and SARS-CoV both use human ACE2 as their cellular receptor.

Virus
Severe acute respiratory syndrome coronavirus 2 Severe Acute Respiratory Syndrome Coronavirus
Host
human Homo sapiens Experimental system
Location
Not specified
Supporting text

SARS-CoV-2 and SARS-CoV recognize the same receptor-angiotensin-converting enzyme 2 (ACE2)-in humans.

Method
crystal structure analysis | receptor-binding domain complex determination
Receptors
ACE2 | angiotensin-converting enzyme 2