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Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
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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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- M. Hoffmann H. Kleine-Weber N. Krüger M. Müller C. Drosten S. Pöhlmann The novel coronavirus 2019 (2019-nCoV) uses the SARS-coronavirus receptor ACE2 and the cellular protease TMPRSS2 for entry into target cells. bioRxiv 929042 [Preprint]. 31 January 2020. https://doi.org/10.1101/2020.01.31.929042. · DOI
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Metadata
- 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
- Venue
- Science
- Published
- 2020-03-13
- Volume
- 367
- Issue
- 6483
- Pages
- 1260-1263
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- 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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