Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein.
Identifieur interne : 000659 ( PubMed/Corpus ); précédent : 000658; suivant : 000660Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein.
Auteurs : Alexandra C. Walls ; Young-Jun Park ; M Alejandra Tortorici ; Abigail Wall ; Andrew T. Mcguire ; David VeeslerSource :
- Cell [ 1097-4172 ] ; 2020.
Abstract
The emergence of SARS-CoV-2 has resulted in >90,000 infections and >3,000 deaths. Coronavirus spike (S) glycoproteins promote entry into cells and are the main target of antibodies. We show that SARS-CoV-2 S uses ACE2 to enter cells and that the receptor-binding domains of SARS-CoV-2 S and SARS-CoV S bind with similar affinities to human ACE2, correlating 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 SARS-related CoVs. We determined cryo-EM structures of the SARS-CoV-2 S ectodomain trimer, providing a blueprint for the design of vaccines and inhibitors of viral entry. Finally, we demonstrate that SARS-CoV S murine polyclonal antibodies potently inhibited SARS-CoV-2 S mediated entry into cells, indicating that cross-neutralizing antibodies targeting conserved S epitopes can be elicited upon vaccination.
DOI: 10.1016/j.cell.2020.02.058
PubMed: 32155444
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<author><name sortKey="Walls, Alexandra C" sort="Walls, Alexandra C" uniqKey="Walls A" first="Alexandra C" last="Walls">Alexandra C. Walls</name>
<affiliation><nlm:affiliation>Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.</nlm:affiliation>
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<author><name sortKey="Park, Young Jun" sort="Park, Young Jun" uniqKey="Park Y" first="Young-Jun" last="Park">Young-Jun Park</name>
<affiliation><nlm:affiliation>Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.</nlm:affiliation>
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<author><name sortKey="Tortorici, M Alejandra" sort="Tortorici, M Alejandra" uniqKey="Tortorici M" first="M Alejandra" last="Tortorici">M Alejandra Tortorici</name>
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<author><name sortKey="Wall, Abigail" sort="Wall, Abigail" uniqKey="Wall A" first="Abigail" last="Wall">Abigail Wall</name>
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<author><name sortKey="Mcguire, Andrew T" sort="Mcguire, Andrew T" uniqKey="Mcguire A" first="Andrew T" last="Mcguire">Andrew T. Mcguire</name>
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<author><name sortKey="Veesler, David" sort="Veesler, David" uniqKey="Veesler D" first="David" last="Veesler">David Veesler</name>
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<series><title level="j">Cell</title>
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<front><div type="abstract" xml:lang="en">The emergence of SARS-CoV-2 has resulted in >90,000 infections and >3,000 deaths. Coronavirus spike (S) glycoproteins promote entry into cells and are the main target of antibodies. We show that SARS-CoV-2 S uses ACE2 to enter cells and that the receptor-binding domains of SARS-CoV-2 S and SARS-CoV S bind with similar affinities to human ACE2, correlating 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 S<sub>1</sub>
/S<sub>2</sub>
subunits, which is processed during biogenesis and sets this virus apart from SARS-CoV and SARS-related CoVs. We determined cryo-EM structures of the SARS-CoV-2 S ectodomain trimer, providing a blueprint for the design of vaccines and inhibitors of viral entry. Finally, we demonstrate that SARS-CoV S murine polyclonal antibodies potently inhibited SARS-CoV-2 S mediated entry into cells, indicating that cross-neutralizing antibodies targeting conserved S epitopes can be elicited upon vaccination.</div>
</front>
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<DateRevised><Year>2020</Year>
<Month>04</Month>
<Day>20</Day>
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<Issue>2</Issue>
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<Title>Cell</Title>
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<ArticleTitle>Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein.</ArticleTitle>
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<Abstract><AbstractText>The emergence of SARS-CoV-2 has resulted in >90,000 infections and >3,000 deaths. Coronavirus spike (S) glycoproteins promote entry into cells and are the main target of antibodies. We show that SARS-CoV-2 S uses ACE2 to enter cells and that the receptor-binding domains of SARS-CoV-2 S and SARS-CoV S bind with similar affinities to human ACE2, correlating 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 S<sub>1</sub>
/S<sub>2</sub>
subunits, which is processed during biogenesis and sets this virus apart from SARS-CoV and SARS-related CoVs. We determined cryo-EM structures of the SARS-CoV-2 S ectodomain trimer, providing a blueprint for the design of vaccines and inhibitors of viral entry. Finally, we demonstrate that SARS-CoV S murine polyclonal antibodies potently inhibited SARS-CoV-2 S mediated entry into cells, indicating that cross-neutralizing antibodies targeting conserved S epitopes can be elicited upon vaccination.</AbstractText>
<CopyrightInformation>Copyright © 2020 Elsevier Inc. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Walls</LastName>
<ForeName>Alexandra C</ForeName>
<Initials>AC</Initials>
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<Author ValidYN="Y"><LastName>Park</LastName>
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<Author ValidYN="Y"><LastName>Wall</LastName>
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<ForeName>Andrew T</ForeName>
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<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">SARS-CoV</Keyword>
<Keyword MajorTopicYN="N">SARS-CoV-2</Keyword>
<Keyword MajorTopicYN="N">antibodies</Keyword>
<Keyword MajorTopicYN="N">coronavirus</Keyword>
<Keyword MajorTopicYN="N">cryo-EM</Keyword>
<Keyword MajorTopicYN="N">neutralizing antibodies</Keyword>
<Keyword MajorTopicYN="N">spike glycoprotein</Keyword>
<Keyword MajorTopicYN="N">viral receptor</Keyword>
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<CoiStatement>Declaration of Interests The authors declare no competing financial interests.</CoiStatement>
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