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Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein

Alexandra C. Walls, Young-Jun Park, M. Alexandra Tortorici, Abigail Wall, Andrew T. McGuire, David Veesler
doi: https://doi.org/10.1101/2020.02.19.956581
Alexandra C. Walls
1Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA
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Young-Jun Park
1Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA
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M. Alexandra Tortorici
1Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA
2Institute Pasteur & CNRS UMR 3569, Unité de Virologie Structurale, 75015, Paris, France
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Abigail Wall
3Vaccines and Infectious Diseases Division, Fred Hutchinson Cancer Research Center, Seattle, Washington 98195, USA
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Andrew T. McGuire
3Vaccines and Infectious Diseases Division, Fred Hutchinson Cancer Research Center, Seattle, Washington 98195, USA
4Department of Global Health, University of Washington, Seattle, Washington 98195, USA
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David Veesler
1Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA
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  • For correspondence: dveesler@uw.edu
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SUMMARY

The recent emergence of a novel coronavirus associated with an ongoing outbreak of pneumonia (Covid-2019) resulted in infections of more than 72,000 people and claimed over 1,800 lives. Coronavirus spike (S) glycoprotein trimers promote entry into cells and are the main target of the humoral immune response. We show here that SARS-CoV-2 S mediates entry in VeroE6 cells and in BHK cells transiently transfected with human ACE2, establishing ACE2 as a functional receptor for this novel coronavirus. We further demonstrate that the receptor-binding domains of SARS-CoV-2 S and SARS-CoV S bind with similar affinities to human ACE2, which correlates with the efficient spread of SARS-CoV-2 among humans. We found that the SARS-CoV-2 S glycoprotein harbors a furin cleavage site at the boundary between the S1/S2 subunits, which is processed during biogenesis and sets this virus apart from SARS-CoV and other SARS-related CoVs. We determined a cryo-electron microscopy structure of the SARS-CoV-2 S ectodomain trimer, demonstrating spontaneous opening of the receptor-binding domain, and providing a blueprint for the design of vaccines and inhibitors of viral entry. Finally, we demonstrate that SARS-CoV S murine polyclonal sera potently inhibited SARS-CoV-2 S-mediated entry into target cells, thereby indicating that cross-neutralizing antibodies targeting conserved S epitopes can be elicited upon vaccination.

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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-NC-ND 4.0 International license.
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Posted February 20, 2020.
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Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein
Alexandra C. Walls, Young-Jun Park, M. Alexandra Tortorici, Abigail Wall, Andrew T. McGuire, David Veesler
bioRxiv 2020.02.19.956581; doi: https://doi.org/10.1101/2020.02.19.956581
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Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein
Alexandra C. Walls, Young-Jun Park, M. Alexandra Tortorici, Abigail Wall, Andrew T. McGuire, David Veesler
bioRxiv 2020.02.19.956581; doi: https://doi.org/10.1101/2020.02.19.956581

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