Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion.
Identifieur interne : 000653 ( PubMed/Corpus ); précédent : 000652; suivant : 000654Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion.
Auteurs : Alexandra C. Walls ; Xiaoli Xiong ; Young-Jun Park ; M Alejandra Tortorici ; Joost Snijder ; Joel Quispe ; Elisabetta Cameroni ; Robin Gopal ; Mian Dai ; Antonio Lanzavecchia ; Maria Zambon ; Félix A. Rey ; Davide Corti ; David VeeslerSource :
- Cell [ 1097-4172 ] ; 2019.
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 to Exploration step
pubmed:30712865Le document en format XML
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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>
</front>
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<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>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Walls</LastName>
<ForeName>Alexandra C</ForeName>
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