Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein
Identifieur interne : 000061 ( Pmc/Checkpoint ); précédent : 000060; suivant : 000062Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein
Auteurs : Alexandra C. Walls [États-Unis] ; Young-Jun Park [États-Unis] ; M. Alejandra Tortorici [États-Unis, France] ; Abigail Wall [États-Unis] ; Andrew T. Mcguire [États-Unis] ; David Veesler [États-Unis]Source :
- Cell [ 0092-8674 ] ; 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.
Url:
DOI: 10.1016/j.cell.2020.02.058
PubMed: 32155444
PubMed Central: 7102599
Affiliations:
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<front><div type="abstract" xml:lang="en"><title>Summary</title>
<p>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.</p>
</div>
</front>
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<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Cell</journal-id>
<journal-id journal-id-type="iso-abbrev">Cell</journal-id>
<journal-title-group><journal-title>Cell</journal-title>
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<issn pub-type="ppub">0092-8674</issn>
<issn pub-type="epub">1097-4172</issn>
<publisher><publisher-name>Elsevier Inc.</publisher-name>
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<article-meta><article-id pub-id-type="pmid">32155444</article-id>
<article-id pub-id-type="pmc">7102599</article-id>
<article-id pub-id-type="publisher-id">S0092-8674(20)30262-2</article-id>
<article-id pub-id-type="doi">10.1016/j.cell.2020.02.058</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
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<title-group><article-title>Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein</article-title>
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<contrib-group><contrib contrib-type="author" id="au1"><name><surname>Walls</surname>
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<xref rid="aff1" ref-type="aff">1</xref>
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</contrib>
<contrib contrib-type="author" id="au4"><name><surname>Wall</surname>
<given-names>Abigail</given-names>
</name>
<xref rid="aff3" ref-type="aff">3</xref>
</contrib>
<contrib contrib-type="author" id="au5"><name><surname>McGuire</surname>
<given-names>Andrew T.</given-names>
</name>
<xref rid="aff3" ref-type="aff">3</xref>
<xref rid="aff4" ref-type="aff">4</xref>
</contrib>
<contrib contrib-type="author" id="au6"><name><surname>Veesler</surname>
<given-names>David</given-names>
</name>
<email>dveesler@uw.edu</email>
<xref rid="aff1" ref-type="aff">1</xref>
<xref rid="fn2" ref-type="fn">6</xref>
<xref rid="cor1" ref-type="corresp">∗</xref>
</contrib>
</contrib-group>
<aff id="aff1"><label>1</label>
Department of Biochemistry, University of Washington, Seattle, WA 98195, USA</aff>
<aff id="aff2"><label>2</label>
Institute Pasteur & CNRS UMR 3569, Unité de Virologie Structurale, Paris 75015, France</aff>
<aff id="aff3"><label>3</label>
Vaccines and Infectious Diseases Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98195, USA</aff>
<aff id="aff4"><label>4</label>
Department of Global Health, University of Washington, Seattle, WA 98195, USA</aff>
<author-notes><corresp id="cor1"><label>∗</label>
Corresponding author <email>dveesler@uw.edu</email>
</corresp>
<fn id="fn1"><label>5</label>
<p id="ntpara0010">These authors contributed equally</p>
</fn>
<fn id="fn2"><label>6</label>
<p id="ntpara0015">Lead Contact</p>
</fn>
</author-notes>
<pub-date pub-type="pmc-release"><day>9</day>
<month>3</month>
<year>2020</year>
</pub-date>
<pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="epub"><day>9</day>
<month>3</month>
<year>2020</year>
</pub-date>
<elocation-id></elocation-id>
<history><date date-type="received"><day>19</day>
<month>2</month>
<year>2020</year>
</date>
<date date-type="rev-recd"><day>24</day>
<month>2</month>
<year>2020</year>
</date>
<date date-type="accepted"><day>26</day>
<month>2</month>
<year>2020</year>
</date>
</history>
<permissions><copyright-statement>© 2020 Elsevier Inc.</copyright-statement>
<copyright-year>2020</copyright-year>
<copyright-holder>Elsevier Inc.</copyright-holder>
<license><license-p>Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.</license-p>
</license>
</permissions>
<abstract id="abs0010"><title>Summary</title>
<p>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.</p>
</abstract>
<abstract abstract-type="graphical" id="abs0015"><title>Graphical Abstract</title>
<fig id="undfig1" position="anchor"><graphic xlink:href="fx1_lrg"></graphic>
</fig>
</abstract>
<abstract abstract-type="author-highlights" id="abs0020"><title>Highlights</title>
<p><list list-type="simple" id="ulist0010"><list-item id="u0010"><label>•</label>
<p id="p0010">SARS-CoV-2 uses ACE2 to enter target cells</p>
</list-item>
<list-item id="u0015"><label>•</label>
<p id="p0015">SARS-CoV-2 and SARS-CoV bind with similar affinities to ACE2</p>
</list-item>
<list-item id="u0020"><label>•</label>
<p id="p0020">Structures of SARS-CoV-2 spike glycoprotein in two conformations</p>
</list-item>
<list-item id="u0025"><label>•</label>
<p id="p0025">SARS-CoV polyclonal antibodies inhibit SARS-CoV-2 spike-mediated entry into cells</p>
</list-item>
</list>
</p>
</abstract>
<abstract abstract-type="teaser" id="abs0025"><p>SARS-CoV-2, a newly emerged pathogen spreading worldwide, binds with high affinity to human ACE2 and uses it as an entry receptor to invade target cells. Cryo-EM structures of the SARS-CoV-2 spike glycoprotein in two distinct conformations, along with inhibition of spike-mediated entry by SARS-CoV polyclonal antibodies, provide a blueprint for the design of vaccines and therapeutics.</p>
</abstract>
<kwd-group id="kwrds0010"><title>Keywords</title>
<kwd>coronavirus</kwd>
<kwd>SARS-CoV-2</kwd>
<kwd>SARS-CoV</kwd>
<kwd>spike glycoprotein</kwd>
<kwd>antibodies</kwd>
<kwd>neutralizing antibodies</kwd>
<kwd>viral receptor</kwd>
<kwd>cryo-EM</kwd>
</kwd-group>
</article-meta>
<notes><p id="misc0010">Published: March 9, 2020</p>
</notes>
</front>
</pmc>
<affiliations><list><country><li>France</li>
<li>États-Unis</li>
</country>
<region><li>Washington (État)</li>
<li>Île-de-France</li>
</region>
<settlement><li>Seattle</li>
</settlement>
<orgName><li>Université de Washington</li>
</orgName>
</list>
<tree><country name="États-Unis"><region name="Washington (État)"><name sortKey="Walls, Alexandra C" sort="Walls, Alexandra C" uniqKey="Walls A" first="Alexandra C." last="Walls">Alexandra C. Walls</name>
</region>
<name sortKey="Mcguire, Andrew T" sort="Mcguire, Andrew T" uniqKey="Mcguire A" first="Andrew T." last="Mcguire">Andrew T. Mcguire</name>
<name sortKey="Mcguire, Andrew T" sort="Mcguire, Andrew T" uniqKey="Mcguire A" first="Andrew T." last="Mcguire">Andrew T. Mcguire</name>
<name sortKey="Park, Young Jun" sort="Park, Young Jun" uniqKey="Park Y" first="Young-Jun" last="Park">Young-Jun Park</name>
<name sortKey="Tortorici, M Alejandra" sort="Tortorici, M Alejandra" uniqKey="Tortorici M" first="M. Alejandra" last="Tortorici">M. Alejandra Tortorici</name>
<name sortKey="Veesler, David" sort="Veesler, David" uniqKey="Veesler D" first="David" last="Veesler">David Veesler</name>
<name sortKey="Wall, Abigail" sort="Wall, Abigail" uniqKey="Wall A" first="Abigail" last="Wall">Abigail Wall</name>
</country>
<country name="France"><region name="Île-de-France"><name sortKey="Tortorici, M Alejandra" sort="Tortorici, M Alejandra" uniqKey="Tortorici M" first="M. Alejandra" last="Tortorici">M. Alejandra Tortorici</name>
</region>
</country>
</tree>
</affiliations>
</record>
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