Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein.
Identifieur interne : 000163 ( PubMed/Checkpoint ); précédent : 000162; suivant : 000164Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein.
Auteurs : Alexandra C. Walls [États-Unis] ; Young-Jun Park [États-Unis] ; M Alejandra Tortorici [France] ; Abigail Wall [États-Unis] ; Andrew T. Mcguire [États-Unis] ; David Veesler [États-Unis]Source :
- 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
Affiliations:
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Walls</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, University of Washington, Seattle, WA 98195</wicri:regionArea><placeName><region type="state">Washington (État)</region><settlement type="city">Seattle</settlement></placeName><orgName type="university">Université de Washington</orgName></affiliation></author><author><name sortKey="Park, Young Jun" sort="Park, Young Jun" uniqKey="Park Y" first="Young-Jun" last="Park">Young-Jun Park</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, University of Washington, Seattle, WA 98195</wicri:regionArea><placeName><region type="state">Washington (État)</region><settlement type="city">Seattle</settlement></placeName><orgName type="university">Université de Washington</orgName></affiliation></author><author><name sortKey="Tortorici, M Alejandra" sort="Tortorici, M Alejandra" uniqKey="Tortorici M" first="M Alejandra" last="Tortorici">M Alejandra Tortorici</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute Pasteur & CNRS UMR 3569, Unité de Virologie Structurale, Paris 75015, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute Pasteur & CNRS UMR 3569, Unité de Virologie Structurale, Paris 75015</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region></placeName><orgName type="university">Université de Washington</orgName></affiliation></author><author><name sortKey="Wall, Abigail" sort="Wall, Abigail" uniqKey="Wall A" first="Abigail" last="Wall">Abigail Wall</name><affiliation wicri:level="2"><nlm:affiliation>Vaccines and Infectious Diseases Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98195, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Vaccines and Infectious Diseases Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98195</wicri:regionArea><placeName><region type="state">Washington (État)</region></placeName></affiliation></author><author><name sortKey="Mcguire, Andrew T" sort="Mcguire, Andrew T" uniqKey="Mcguire A" first="Andrew T" last="Mcguire">Andrew T. Mcguire</name><affiliation wicri:level="4"><nlm:affiliation>Vaccines and Infectious Diseases Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98195, USA; Department of Global Health, University of Washington, Seattle, WA 98195, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Vaccines and Infectious Diseases Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98195, USA; Department of Global Health, University of Washington, Seattle, WA 98195</wicri:regionArea><placeName><region type="state">Washington (État)</region><settlement type="city">Seattle</settlement></placeName><orgName type="university">Université de Washington</orgName></affiliation></author><author><name sortKey="Veesler, David" sort="Veesler, David" uniqKey="Veesler D" first="David" last="Veesler">David Veesler</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry, University of Washington, Seattle, WA 98195, USA. Electronic address: dveesler@uw.edu.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, University of Washington, Seattle, WA 98195</wicri:regionArea><placeName><region type="state">Washington (État)</region><settlement type="city">Seattle</settlement></placeName><orgName type="university">Université de Washington</orgName></affiliation></author></analytic><series><title level="j">Cell</title><idno type="eISSN">1097-4172</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><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></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">32155444</PMID><DateRevised><Year>2020</Year><Month>04</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1097-4172</ISSN><JournalIssue CitedMedium="Internet"><Volume>181</Volume><Issue>2</Issue><PubDate><Year>2020</Year><Month>Apr</Month><Day>16</Day></PubDate></JournalIssue><Title>Cell</Title><ISOAbbreviation>Cell</ISOAbbreviation></Journal><ArticleTitle>Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein.</ArticleTitle><Pagination><MedlinePgn>281-292.e6</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0092-8674(20)30262-2</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.cell.2020.02.058</ELocationID><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><AffiliationInfo><Affiliation>Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Park</LastName><ForeName>Young-Jun</ForeName><Initials>YJ</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tortorici</LastName><ForeName>M Alejandra</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, University of Washington, Seattle, WA 98195, USA; Institute Pasteur & CNRS UMR 3569, Unité de Virologie Structurale, Paris 75015, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wall</LastName><ForeName>Abigail</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Vaccines and Infectious Diseases Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98195, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>McGuire</LastName><ForeName>Andrew T</ForeName><Initials>AT</Initials><AffiliationInfo><Affiliation>Vaccines and Infectious Diseases Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98195, USA; Department of Global Health, University of Washington, Seattle, WA 98195, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Veesler</LastName><ForeName>David</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, University of Washington, Seattle, WA 98195, USA. Electronic address: dveesler@uw.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>03</Month><Day>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Cell</MedlineTA><NlmUniqueID>0413066</NlmUniqueID><ISSNLinking>0092-8674</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><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></KeywordList><CoiStatement>Declaration of Interests The authors declare no competing financial interests.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>02</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>02</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>02</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>3</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>3</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>3</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32155444</ArticleId><ArticleId IdType="pii">S0092-8674(20)30262-2</ArticleId><ArticleId IdType="doi">10.1016/j.cell.2020.02.058</ArticleId><ArticleId IdType="pmc">PMC7102599</ArticleId></ArticleIdList></PubmedData></pubmed><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="Park, Young Jun" sort="Park, Young Jun" uniqKey="Park Y" first="Young-Jun" last="Park">Young-Jun Park</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>Pour manipuler ce document sous Unix (Dilib)
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