Cited by 8,897SARS-CoV-2 and COVID-19 ResearchAdvanced Electron Microscopy Techniques and ApplicationsAnimal Virus Infections Studies

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Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation

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Wrapp, Daniel, Wang, Nianshuang, Corbett, Kizzmekia S., Goldsmith, Jory A., Hsieh, Ching-Lin, Abiona, Olubukola, Graham, Barney S., McLellan, Jason S.·2020·Science

DOI 10.1126/science.abb2507PMC PMC7164637

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Abstract

The outbreak of a novel coronavirus (2019-nCoV) represents a pandemic threat that has been declared a public health emergency of international concern. The CoV spike (S) glycoprotein is a key target for vaccines, therapeutic antibodies, and diagnostics. To facilitate medical countermeasure development, we determined a 3.5-angstrom-resolution cryo–electron microscopy structure of the 2019-nCoV S trimer in the prefusion conformation. The predominant state of the trimer has one of the three receptor-binding domains (RBDs) rotated up in a receptor-accessible conformation. We also provide biophysical and structural evidence that the 2019-nCoV S protein binds angiotensin-converting enzyme 2 (ACE2) with higher affinity than does severe acute respiratory syndrome (SARS)-CoV S. Additionally, we tested several published SARS-CoV RBD-specific monoclonal antibodies and found that they do not have appreciable binding to 2019-nCoV S, suggesting that antibody cross-reactivity may be limited between the two RBDs. The structure of 2019-nCoV S should enable the rapid development and evaluation of medical countermeasures to address the ongoing public health crisis.

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“Several prefusion conformations have been resolved for the S protein, where the three RBDs display distinct orientations: up or down (Walls et al., 2020; Wrapp et al., 2020).”
BackgroundInfluential
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Authors: Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S.
Affiliations: The University of Texas at Austin (US)
National Institutes of Health (US)
Corresponding author: McLellan, Jason S.
ORCID: Wrapp, Daniel
Wang, Nianshuang
Corbett, Kizzmekia S.
Goldsmith, Jory A.
Hsieh, Ching-Lin
Abiona, Olubukola
Graham, Barney S.
McLellan, Jason S.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2020-03-13
Volume: 367
Issue: 6483
Pages: 1260-1263
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.abb2507
PMC: PMC7164637
OpenAlex: W3007643904
Cited by: 8,897
References: 42
Citations by year: 2026: 220 · 2025: 378 · 2024: 570 · 2023: 894 · 2022: 1482 · 2021: 2591 · 2020: 2749
FWCI: 252.13
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
Locations: Science (publishedVersion, cc-by)
bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
PubMed Central (submittedVersion, cc-by)
Funders: National Institute of Allergy and Infectious Diseases (R01-AI127521)
Topics: Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
Keywords: SARS-CoV-2, receptor binding domain, ACE2 binding affinity, antibody cross-reactivity
MeSH terms: Protein Domains, Betacoronavirus, Receptors, Coronavirus, Angiotensin-Converting Enzyme 2, SARS-CoV-2, Antibodies, Monoclonal, Antibodies, Viral, Cross Reactions, Image Processing, Computer-Assisted, Peptidyl-Dipeptidase A, Models, Molecular, Protein Binding, Protein Conformation, Receptors, Virus, Cryoelectron Microscopy, Severe acute respiratory syndrome-related coronavirus, Protein Multimerization, Spike Glycoprotein, Coronavirus

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Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation

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