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Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
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Abstract
A new and highly pathogenic coronavirus (severe acute respiratory syndrome coronavirus-2, SARS-CoV-2) caused an outbreak in Wuhan city, Hubei province, China, starting from December 2019 that quickly spread nationwide and to other countries around the world 1-3. Here, to better understand the initial step of infection at an atomic level, we determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 bound to the cell receptor ACE2. The overall ACE2-binding mode of the SARS-CoV-2 RBD is nearly identical to that of the SARS-CoV RBD, which also uses ACE2 as the cell receptor 4. Structural analysis identified residues in the SARS-CoV-2 RBD that are essential for ACE2 binding, the majority of which either are highly conserved or share similar side chain properties with those in the SARS-CoV RBD. Such similarity in structure and sequence strongly indicate convergent evolution between the SARS-CoV-2 and SARS-CoV RBDs for improved binding to ACE2, although SARS-CoV-2 does not cluster within SARS and SARS-related coronaviruses 1-3,5. The epitopes of two SARS-CoV antibodies that target the RBD are also analysed for binding to the SARS-CoV-2 RBD, providing insights into the future identification of cross-reactive antibodies.
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“This amino acid sequence extends from residue Thr333 to residue Gly526 [28].”
From Effects of Mangiferin on LPS-Induced Inflammation and SARS-CoV-2 Viral Adsorption in Human Lung Cells (2022) · cites this paper as [28]
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“Importantly, ACE2 (angiotensin-converting enzyme 2) had been identified as the receptor for SARS-CoV 4,5 and SARS-CoV-2.”
From COVID-19, Myocarditis and Pericarditis (2023) · cites this paper as [7]
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“When binding to hACE2, spike amino acid F486 interacts with hACE2 residues L79, M82 and Y83, which collectively comprise a hotspot for ACE2 differences between mammalian species13.”
From Emergence of SARS-CoV-2 Omicron lineages BA.4 and BA.5 in South Africa (2022) · cites this paper as [13]
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Transmission of SARS-CoV-2 from humans to animals and potential host adaptationPreprint
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Metadata
- Authors
- Lan, J., Ge, J., Yu, J., Shan, S., Zhou, H., Fan, S., Zhang, Q., Shi, X., Wang, Q., Zhang, L., & Wang, X.
- Affiliations
- Tsinghua University (CN)
- Chinese Academy of Sciences (CN)
- Corresponding author
- Zhang, Qi
- Zhang, Linqi
- Wang, Xinquan
- ORCID
- Venue
- Nature
- Published
- 2020-03-30
- Volume
- 581
- Issue
- 7807
- Pages
- 215-220
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W3014067025
- Cited by
- 5,983
- References
- 38
- Citations by year
- 2026: 207 · 2025: 404 · 2024: 573 · 2023: 797 · 2022: 1237 · 2021: 1678 · 2020: 1076
- FWCI
- 152.41
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Nature (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Salt Science Research Foundation
- Tencent
- Tsinghua University (20201080053)
- Beijing Municipal Science and Technology Commission (171100000517-001 and -003)
- Beijing Advanced Innovation Center for Structural Biology, Tsinghua University
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Keywords
- SARS-CoV-2, spike protein, receptor binding domain, ACE2, crystal structure, SARS-CoV, convergent evolution, antibody epitopes, cross-reactive antibodies, viral entry, binding site residues
- MeSH terms
- Protein Domains, Betacoronavirus, Angiotensin-Converting Enzyme 2, SARS-CoV-2, Amino Acid Sequence, Epitopes, Binding Sites, Humans, Hydrogen Bonding, Peptidyl-Dipeptidase A, Models, Molecular, Protein Binding, Receptors, Virus, Salts, Water, Sequence Alignment, Conserved Sequence, Crystallography, X-Ray, Evolution, Molecular, Severe acute respiratory syndrome-related coronavirus, Antibodies, Neutralizing, Spike Glycoprotein, Coronavirus
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