MersV1, PubMed, Curation, bibRecord, 000653

Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion.

Identifieur interne : 000653 ( PubMed/Curation ); précédent : 000652; suivant : 000654

Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion.

Auteurs : Alexandra C. Walls [États-Unis] ; Xiaoli Xiong [États-Unis] ; Young-Jun Park [États-Unis] ; M Alejandra Tortorici [France] ; Joost Snijder [États-Unis] ; Joel Quispe [États-Unis] ; Elisabetta Cameroni [Suisse] ; Robin Gopal [Royaume-Uni] ; Mian Dai [Royaume-Uni] ; Antonio Lanzavecchia [Suisse] ; Maria Zambon [Royaume-Uni] ; Félix A. Rey [France] ; Davide Corti [Suisse] ; David Veesler [États-Unis]

Source :

Cell [ 1097-4172 ] ; 2019.

RBID : pubmed:30712865

Descripteurs français

English descriptors

KwdEn :
- Animals, Antibodies, Monoclonal (immunology), Antibodies, Neutralizing (immunology), Antibodies, Viral (immunology), Chlorocebus aethiops, Coronavirus (immunology), Coronavirus (metabolism), Coronavirus Infections (immunology), HEK293 Cells, Humans, Immunity, Humoral (immunology), Middle East Respiratory Syndrome Coronavirus (immunology), Middle East Respiratory Syndrome Coronavirus (metabolism), Molecular Mimicry (immunology), Protein Binding, Receptors, Virus (metabolism), SARS Virus (immunology), SARS Virus (metabolism), Spike Glycoprotein, Coronavirus (metabolism), Spike Glycoprotein, Coronavirus (physiology), Spike Glycoprotein, Coronavirus (ultrastructure), Vero Cells, Virus Internalization.
MESH :
- chemical , immunology : Antibodies, Monoclonal, Antibodies, Neutralizing, Antibodies, Viral.
- immunology : Coronavirus, Coronavirus Infections, Immunity, Humoral, Middle East Respiratory Syndrome Coronavirus, Molecular Mimicry, SARS Virus.
- metabolism : Coronavirus, Middle East Respiratory Syndrome Coronavirus, Receptors, Virus, SARS Virus, Spike Glycoprotein, Coronavirus.
- chemical , physiology : Spike Glycoprotein, Coronavirus.
- chemical , ultrastructure : Spike Glycoprotein, Coronavirus.
- Animals, Chlorocebus aethiops, HEK293 Cells, Humans, Protein Binding, Vero Cells, Virus Internalization.

Abstract

Recent outbreaks of severe acute respiratory syndrome and Middle East respiratory syndrome, along with the threat of a future coronavirus-mediated pandemic, underscore the importance of finding ways to combat these viruses. The trimeric spike transmembrane glycoprotein S mediates entry into host cells and is the major target of neutralizing antibodies. To understand the humoral immune response elicited upon natural infections with coronaviruses, we structurally characterized the SARS-CoV and MERS-CoV S glycoproteins in complex with neutralizing antibodies isolated from human survivors. Although the two antibodies studied blocked attachment to the host cell receptor, only the anti-SARS-CoV S antibody triggered fusogenic conformational changes via receptor functional mimicry. These results provide a structural framework for understanding coronavirus neutralization by human antibodies and shed light on activation of coronavirus membrane fusion, which takes place through a receptor-driven ratcheting mechanism.

DOI: 10.1016/j.cell.2018.12.028
PubMed: 30712865

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<front><div type="abstract" xml:lang="en">Recent outbreaks of severe acute respiratory syndrome and Middle East respiratory syndrome, along with the threat of a future coronavirus-mediated pandemic, underscore the importance of finding ways to combat these viruses. The trimeric spike transmembrane glycoprotein S mediates entry into host cells and is the major target of neutralizing antibodies. To understand the humoral immune response elicited upon natural infections with coronaviruses, we structurally characterized the SARS-CoV and MERS-CoV S glycoproteins in complex with neutralizing antibodies isolated from human survivors. Although the two antibodies studied blocked attachment to the host cell receptor, only the anti-SARS-CoV S antibody triggered fusogenic conformational changes via receptor functional mimicry. These results provide a structural framework for understanding coronavirus neutralization by human antibodies and shed light on activation of coronavirus membrane fusion, which takes place through a receptor-driven ratcheting mechanism.</div>
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<Issue>5</Issue>
<PubDate><Year>2019</Year>
<Month>02</Month>
<Day>21</Day>
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<Title>Cell</Title>
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<ArticleTitle>Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion.</ArticleTitle>
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<ELocationID EIdType="pii" ValidYN="Y">S0092-8674(18)31642-8</ELocationID>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.cell.2018.12.028</ELocationID>
<Abstract><AbstractText>Recent outbreaks of severe acute respiratory syndrome and Middle East respiratory syndrome, along with the threat of a future coronavirus-mediated pandemic, underscore the importance of finding ways to combat these viruses. The trimeric spike transmembrane glycoprotein S mediates entry into host cells and is the major target of neutralizing antibodies. To understand the humoral immune response elicited upon natural infections with coronaviruses, we structurally characterized the SARS-CoV and MERS-CoV S glycoproteins in complex with neutralizing antibodies isolated from human survivors. Although the two antibodies studied blocked attachment to the host cell receptor, only the anti-SARS-CoV S antibody triggered fusogenic conformational changes via receptor functional mimicry. These results provide a structural framework for understanding coronavirus neutralization by human antibodies and shed light on activation of coronavirus membrane fusion, which takes place through a receptor-driven ratcheting mechanism.</AbstractText>
<CopyrightInformation>Copyright © 2018 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, Washington 98195, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Xiong</LastName>
<ForeName>Xiaoli</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, University of Washington, Seattle, Washington 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, Washington 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, Washington 98195, USA; Institute Pasteur & CNRS UMR 3569, Unité de Virologie Structurale, 75015, Paris, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Snijder</LastName>
<ForeName>Joost</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Quispe</LastName>
<ForeName>Joel</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Cameroni</LastName>
<ForeName>Elisabetta</ForeName>
<Initials>E</Initials>
<AffiliationInfo><Affiliation>Humabs Biomed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Gopal</LastName>
<ForeName>Robin</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>National Infection Service, Public Health England, London NW9 5HT, UK.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Dai</LastName>
<ForeName>Mian</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Crick Worldwide Influenza Centre, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lanzavecchia</LastName>
<ForeName>Antonio</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Institute for Research in Biomedicine, Faculty of Biomedical Sciences, Università della Svizzera italiana, 6500 Bellinzona, Switzerland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zambon</LastName>
<ForeName>Maria</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>National Infection Service, Public Health England, London NW9 5HT, UK.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Rey</LastName>
<ForeName>Félix A</ForeName>
<Initials>FA</Initials>
<AffiliationInfo><Affiliation>Institute Pasteur & CNRS UMR 3569, Unité de Virologie Structurale, 75015, Paris, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Corti</LastName>
<ForeName>Davide</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>Humabs Biomed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Veesler</LastName>
<ForeName>David</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA. Electronic address: dveesler@uw.edu.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>R01 GM120553</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>S10 OD021832</GrantID>
<Acronym>OD</Acronym>
<Agency>NIH HHS</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2019</Year>
<Month>01</Month>
<Day>31</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Cell</MedlineTA>
<NlmUniqueID>0413066</NlmUniqueID>
<ISSNLinking>0092-8674</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000911">Antibodies, Monoclonal</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D057134">Antibodies, Neutralizing</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000914">Antibodies, Viral</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011991">Receptors, Virus</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000911" MajorTopicYN="N">Antibodies, Monoclonal</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D057134" MajorTopicYN="N">Antibodies, Neutralizing</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000914" MajorTopicYN="N">Antibodies, Viral</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002522" MajorTopicYN="N">Chlorocebus aethiops</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017934" MajorTopicYN="N">Coronavirus</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018352" MajorTopicYN="N">Coronavirus Infections</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D056724" MajorTopicYN="N">Immunity, Humoral</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D065207" MajorTopicYN="N">Middle East Respiratory Syndrome Coronavirus</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018716" MajorTopicYN="N">Molecular Mimicry</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011991" MajorTopicYN="N">Receptors, Virus</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
<QualifierName UI="Q000648" MajorTopicYN="Y">ultrastructure</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014709" MajorTopicYN="N">Vero Cells</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053586" MajorTopicYN="N">Virus Internalization</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">MERS-CoV</Keyword>
<Keyword MajorTopicYN="Y">N-linked glycosylation</Keyword>
<Keyword MajorTopicYN="Y">SARS-CoV</Keyword>
<Keyword MajorTopicYN="Y">class I fusion protein</Keyword>
<Keyword MajorTopicYN="Y">coronavirus</Keyword>
<Keyword MajorTopicYN="Y">glycoproteomics</Keyword>
<Keyword MajorTopicYN="Y">membrane fusion</Keyword>
<Keyword MajorTopicYN="Y">neutralizing antibodies</Keyword>
<Keyword MajorTopicYN="Y">spike glycoprotein</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year>
<Month>07</Month>
<Day>19</Day>
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<PubMedPubDate PubStatus="revised"><Year>2018</Year>
<Month>10</Month>
<Day>29</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2018</Year>
<Month>12</Month>
<Day>17</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2019</Year>
<Month>2</Month>
<Day>5</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion.

Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion.

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