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Cryo-EM Structure of the 2019-nCoV Spike in the Prefusion Conformation

Daniel Wrapp, Nianshuang Wang, Kizzmekia S. Corbett, Jory A. Goldsmith, Ching-Lin Hsieh, Olubukola Abiona, Barney S. Graham, View ORCID ProfileJason S. McLellan
doi: https://doi.org/10.1101/2020.02.11.944462
Daniel Wrapp
1Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA
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Nianshuang Wang
1Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA
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Kizzmekia S. Corbett
2Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
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Jory A. Goldsmith
1Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA
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Ching-Lin Hsieh
1Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA
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Olubukola Abiona
2Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
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Barney S. Graham
2Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
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Jason S. McLellan
1Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA
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  • ORCID record for Jason S. McLellan
  • For correspondence: jmclellan@austin.utexas.edu
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Abstract

The outbreak of a novel betacoronavirus (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 urgently needed vaccines, therapeutic antibodies, and diagnostics. To facilitate medical countermeasure (MCM) development we determined a 3.5 Å-resolution cryo-EM 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 show biophysical and structural evidence that the 2019-nCoV S binds ACE2 with higher affinity than SARS-CoV S. Additionally we tested several published SARS-CoV RBD-specific monoclonal antibodies and found that they do not have appreciable binding to nCoV-2019 S, suggesting antibody cross-reactivity may be limited between the two virus RBDs. The atomic-resolution structure of 2019-nCoV S should enable rapid development and evaluation of MCMs to address the ongoing public health crisis.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted February 15, 2020.
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Cryo-EM Structure of the 2019-nCoV Spike in the Prefusion Conformation
Daniel Wrapp, Nianshuang Wang, Kizzmekia S. Corbett, Jory A. Goldsmith, Ching-Lin Hsieh, Olubukola Abiona, Barney S. Graham, Jason S. McLellan
bioRxiv 2020.02.11.944462; doi: https://doi.org/10.1101/2020.02.11.944462
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Cryo-EM Structure of the 2019-nCoV Spike in the Prefusion Conformation
Daniel Wrapp, Nianshuang Wang, Kizzmekia S. Corbett, Jory A. Goldsmith, Ching-Lin Hsieh, Olubukola Abiona, Barney S. Graham, Jason S. McLellan
bioRxiv 2020.02.11.944462; doi: https://doi.org/10.1101/2020.02.11.944462

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