Cited by 544SARS-CoV-2 and COVID-19 ResearchAnimal Virus Infections StudiesEnzyme Structure and Function

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SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects

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Wrobel, Antoni G., Benton, Donald J., Xu, Pengqi, Roustan, Chloë, Martin, Stephen R., Rosenthal, Peter B., Skehel, John J., Gamblin, Steven J.·2020·Nature Structural & Molecular Biology

DOI 10.1038/s41594-020-0468-7PMC PMC7610980

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Abstract

SARS-CoV-2 is thought to have emerged from bats, possibly via a secondary host. Here, we investigate the relationship of spike (S) glycoprotein from SARS-CoV-2 with the S protein of a closely related bat virus, RaTG13. We determined cryo-EM structures for RaTG13 S and for both furin-cleaved and uncleaved SARS-CoV-2 S; we compared these with recently reported structures for uncleaved SARS-CoV-2 S. We also biochemically characterized their relative stabilities and affinities for the SARS-CoV-2 receptor ACE2. Although the overall structures of human and bat virus S proteins are similar, there are key differences in their properties, including a more stable precleavage form of human S and about 1,000-fold tighter binding of SARS-CoV-2 to human receptor. These observations suggest that cleavage at the furin-cleavage site decreases the overall stability of SARS-CoV-2 S and facilitates the adoption of the open conformation that is required for S to bind to the ACE2 receptor.

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Authors: Wrobel, A. G., Benton, D. J., Xu, P., Roustan, C., Martin, S. R., Rosenthal, P. B., Skehel, J. J., & Gamblin, S. J.
Affiliations: The Francis Crick Institute (GB)
Sun Yat-sen University (CN)
Corresponding author: Wrobel, Antoni G.
Benton, Donald J.
ORCID: Wrobel, Antoni G.
Benton, Donald J.
Roustan, Chloë
Martin, Stephen R.
Rosenthal, Peter B.
Skehel, John J.
Gamblin, Steven J.
Venue: Nature Structural & Molecular Biology
Publisher: Springer Science and Business Media LLC
Published: 2020-07-09
Volume: 27
Issue: 8
Pages: 763-767
ISSN: 1545-9985 (ISSN-L)
1545-9993
DOI: 10.1038/s41594-020-0468-7
PMC: PMC7610980
OpenAlex: W3040801746
Cited by: 544
References: 37
Citations by year: 2026: 20 · 2025: 30 · 2024: 53 · 2023: 82 · 2022: 129 · 2021: 180 · 2020: 48
FWCI: 14.43
Type: journal article
Language: en
Update notices: correction (2020-08-26)
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Nature Structural & Molecular Biology (publishedVersion)
Research Square (acceptedVersion, cc-by)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: Cancer Research UK (FC001078, FC001143)
Wellcome Trust (FC001078, FC001143)
RCUK | Medical Research Council (FC001078, FC001143)
Sun Yat-sen University
100 Top Talents Program of Sun Yat-sen University & the Sanming Project of Medicine in Shenzhen
Topics: Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: SARS-CoV-2, RaTG13, spike protein, furin cleavage, ACE2 binding, protein stability, bat coronaviruses, viral evolution, SARS-CoV-2 origin, receptor binding affinity
MeSH terms: Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Betacoronavirus, Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, Animals, Binding Sites, Chiroptera, Humans, Peptidyl-Dipeptidase A, Models, Molecular, Pneumonia, Viral, Protein Binding, Receptors, Virus, Recombinant Proteins, Gene Expression, Coronavirus Infections, Evolution, Molecular, Protein Isoforms, Cryoelectron Microscopy, Structural Homology, Protein, Furin, Protein Interaction Domains and Motifs, Host-Pathogen Interactions, Protein Stability, HEK293 Cells, Pandemics, Proteolysis, Spike Glycoprotein, Coronavirus

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SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects

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