Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion.
Identifieur interne : 000A78 ( Main/Merge ); précédent : 000A77; suivant : 000A79Unexpected 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.
Descripteurs français
- KwdFr :
- Animaux, Anticorps antiviraux (immunologie), Anticorps monoclonaux (immunologie), Anticorps neutralisants (immunologie), Cellules HEK293, Cellules Vero, Coronavirus (immunologie), Coronavirus (métabolisme), Coronavirus du syndrome respiratoire du Moyen-Orient (immunologie), Coronavirus du syndrome respiratoire du Moyen-Orient (métabolisme), Glycoprotéine de spicule des coronavirus (métabolisme), Glycoprotéine de spicule des coronavirus (physiologie), Glycoprotéine de spicule des coronavirus (ultrastructure), Humains, Immunité humorale (immunologie), Infections à coronavirus (immunologie), Liaison aux protéines, Mimétisme moléculaire (immunologie), Pénétration virale, Récepteurs viraux (métabolisme), Virus du SRAS (immunologie), Virus du SRAS (métabolisme).
- MESH :
- immunologie : Anticorps antiviraux, Anticorps monoclonaux, Anticorps neutralisants, Coronavirus, Coronavirus du syndrome respiratoire du Moyen-Orient, Immunité humorale, Infections à coronavirus, Mimétisme moléculaire, Virus du SRAS.
- métabolisme : Coronavirus, Coronavirus du syndrome respiratoire du Moyen-Orient, Glycoprotéine de spicule des coronavirus, Récepteurs viraux, Virus du SRAS.
- physiologie : Glycoprotéine de spicule des coronavirus.
- ultrastructure : Animaux, Cellules HEK293, Cellules Vero, Glycoprotéine de spicule des coronavirus, Humains, Liaison aux protéines, Pénétration virale.
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
Links toward previous steps (curation, corpus...)
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pubmed:30712865Le document en format XML
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion.</title>
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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>
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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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<country xml:lang="fr">France</country>
<wicri:regionArea>Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA; Institute Pasteur & CNRS UMR 3569, Unité de Virologie Structurale, 75015, Paris</wicri:regionArea>
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<author><name sortKey="Snijder, Joost" sort="Snijder, Joost" uniqKey="Snijder J" first="Joost" last="Snijder">Joost Snijder</name>
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<author><name sortKey="Quispe, Joel" sort="Quispe, Joel" uniqKey="Quispe J" first="Joel" last="Quispe">Joel Quispe</name>
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<country xml:lang="fr">États-Unis</country>
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<author><name sortKey="Cameroni, Elisabetta" sort="Cameroni, Elisabetta" uniqKey="Cameroni E" first="Elisabetta" last="Cameroni">Elisabetta Cameroni</name>
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<country xml:lang="fr">Suisse</country>
<wicri:regionArea>Humabs Biomed SA, Vir Biotechnology, 6500 Bellinzona</wicri:regionArea>
<wicri:noRegion>6500 Bellinzona</wicri:noRegion>
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</author>
<author><name sortKey="Gopal, Robin" sort="Gopal, Robin" uniqKey="Gopal R" first="Robin" last="Gopal">Robin Gopal</name>
<affiliation wicri:level="1"><nlm:affiliation>National Infection Service, Public Health England, London NW9 5HT, UK.</nlm:affiliation>
<country xml:lang="fr">Royaume-Uni</country>
<wicri:regionArea>National Infection Service, Public Health England, London NW9 5HT</wicri:regionArea>
<wicri:noRegion>London NW9 5HT</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Dai, Mian" sort="Dai, Mian" uniqKey="Dai M" first="Mian" last="Dai">Mian Dai</name>
<affiliation wicri:level="1"><nlm:affiliation>Crick Worldwide Influenza Centre, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.</nlm:affiliation>
<country xml:lang="fr">Royaume-Uni</country>
<wicri:regionArea>Crick Worldwide Influenza Centre, The Francis Crick Institute, 1 Midland Road, London NW1 1AT</wicri:regionArea>
<wicri:noRegion>London NW1 1AT</wicri:noRegion>
</affiliation>
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<author><name sortKey="Lanzavecchia, Antonio" sort="Lanzavecchia, Antonio" uniqKey="Lanzavecchia A" first="Antonio" last="Lanzavecchia">Antonio Lanzavecchia</name>
<affiliation wicri:level="1"><nlm:affiliation>Institute for Research in Biomedicine, Faculty of Biomedical Sciences, Università della Svizzera italiana, 6500 Bellinzona, Switzerland.</nlm:affiliation>
<country xml:lang="fr">Suisse</country>
<wicri:regionArea>Institute for Research in Biomedicine, Faculty of Biomedical Sciences, Università della Svizzera italiana, 6500 Bellinzona</wicri:regionArea>
<wicri:noRegion>6500 Bellinzona</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Zambon, Maria" sort="Zambon, Maria" uniqKey="Zambon M" first="Maria" last="Zambon">Maria Zambon</name>
<affiliation wicri:level="1"><nlm:affiliation>National Infection Service, Public Health England, London NW9 5HT, UK.</nlm:affiliation>
<country xml:lang="fr">Royaume-Uni</country>
<wicri:regionArea>National Infection Service, Public Health England, London NW9 5HT</wicri:regionArea>
<wicri:noRegion>London NW9 5HT</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Rey, Felix A" sort="Rey, Felix A" uniqKey="Rey F" first="Félix A" last="Rey">Félix A. Rey</name>
<affiliation wicri:level="3"><nlm:affiliation>Institute Pasteur & CNRS UMR 3569, Unité de Virologie Structurale, 75015, Paris, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Institute Pasteur & CNRS UMR 3569, Unité de Virologie Structurale, 75015, Paris</wicri:regionArea>
<placeName><region type="region" nuts="2">Île-de-France</region>
<settlement type="city">Paris</settlement>
</placeName>
</affiliation>
</author>
<author><name sortKey="Corti, Davide" sort="Corti, Davide" uniqKey="Corti D" first="Davide" last="Corti">Davide Corti</name>
<affiliation wicri:level="1"><nlm:affiliation>Humabs Biomed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland.</nlm:affiliation>
<country xml:lang="fr">Suisse</country>
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<wicri:noRegion>6500 Bellinzona</wicri:noRegion>
</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, Washington 98195, USA. Electronic address: dveesler@uw.edu.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
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<placeName><settlement type="city">Seattle</settlement>
<region type="state">Washington (État)</region>
</placeName>
</affiliation>
</author>
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<series><title level="j">Cell</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Antibodies, Monoclonal (immunology)</term>
<term>Antibodies, Neutralizing (immunology)</term>
<term>Antibodies, Viral (immunology)</term>
<term>Chlorocebus aethiops</term>
<term>Coronavirus (immunology)</term>
<term>Coronavirus (metabolism)</term>
<term>Coronavirus Infections (immunology)</term>
<term>HEK293 Cells</term>
<term>Humans</term>
<term>Immunity, Humoral (immunology)</term>
<term>Middle East Respiratory Syndrome Coronavirus (immunology)</term>
<term>Middle East Respiratory Syndrome Coronavirus (metabolism)</term>
<term>Molecular Mimicry (immunology)</term>
<term>Protein Binding</term>
<term>Receptors, Virus (metabolism)</term>
<term>SARS Virus (immunology)</term>
<term>SARS Virus (metabolism)</term>
<term>Spike Glycoprotein, Coronavirus (metabolism)</term>
<term>Spike Glycoprotein, Coronavirus (physiology)</term>
<term>Spike Glycoprotein, Coronavirus (ultrastructure)</term>
<term>Vero Cells</term>
<term>Virus Internalization</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Anticorps antiviraux (immunologie)</term>
<term>Anticorps monoclonaux (immunologie)</term>
<term>Anticorps neutralisants (immunologie)</term>
<term>Cellules HEK293</term>
<term>Cellules Vero</term>
<term>Coronavirus (immunologie)</term>
<term>Coronavirus (métabolisme)</term>
<term>Coronavirus du syndrome respiratoire du Moyen-Orient (immunologie)</term>
<term>Coronavirus du syndrome respiratoire du Moyen-Orient (métabolisme)</term>
<term>Glycoprotéine de spicule des coronavirus (métabolisme)</term>
<term>Glycoprotéine de spicule des coronavirus (physiologie)</term>
<term>Glycoprotéine de spicule des coronavirus (ultrastructure)</term>
<term>Humains</term>
<term>Immunité humorale (immunologie)</term>
<term>Infections à coronavirus (immunologie)</term>
<term>Liaison aux protéines</term>
<term>Mimétisme moléculaire (immunologie)</term>
<term>Pénétration virale</term>
<term>Récepteurs viraux (métabolisme)</term>
<term>Virus du SRAS (immunologie)</term>
<term>Virus du SRAS (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term>
<term>Antibodies, Neutralizing</term>
<term>Antibodies, Viral</term>
</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps antiviraux</term>
<term>Anticorps monoclonaux</term>
<term>Anticorps neutralisants</term>
<term>Coronavirus</term>
<term>Coronavirus du syndrome respiratoire du Moyen-Orient</term>
<term>Immunité humorale</term>
<term>Infections à coronavirus</term>
<term>Mimétisme moléculaire</term>
<term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Coronavirus</term>
<term>Coronavirus Infections</term>
<term>Immunity, Humoral</term>
<term>Middle East Respiratory Syndrome Coronavirus</term>
<term>Molecular Mimicry</term>
<term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Coronavirus</term>
<term>Middle East Respiratory Syndrome Coronavirus</term>
<term>Receptors, Virus</term>
<term>SARS Virus</term>
<term>Spike Glycoprotein, Coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Coronavirus</term>
<term>Coronavirus du syndrome respiratoire du Moyen-Orient</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Récepteurs viraux</term>
<term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Glycoprotéine de spicule des coronavirus</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Spike Glycoprotein, Coronavirus</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Spike Glycoprotein, Coronavirus</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Chlorocebus aethiops</term>
<term>HEK293 Cells</term>
<term>Humans</term>
<term>Protein Binding</term>
<term>Vero Cells</term>
<term>Virus Internalization</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Animaux</term>
<term>Cellules HEK293</term>
<term>Cellules Vero</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Pénétration virale</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<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>
</front>
</TEI>
</record>
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