Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion
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 cel...
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| Published in | Cell Vol. 176; no. 5; pp. 1026 - 1039.e15 |
|---|---|
| Main Authors | , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
21.02.2019
Elsevier |
| Subjects | |
| Online Access | Get full text |
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| 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.
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•MERS-CoV/SARS-CoV S composite glycan shields analyzed by cryo-EM and mass spectrometry•Structures of MERS-CoV/SARS-CoV S with neutralizing antibodies from survivors•LCA60 inhibits receptor binding by interacting with MERS-CoV S protein/glycans•S230 blocks receptor binding and triggers fusogenic rearrangements via functional mimicry
Structural analysis of the SARS-CoV S and MERS-CoV S glycoproteins in complex with neutralizing antibodies from human survivors sheds light into the mechanisms of membrane fusion and neutralization |
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| AbstractList | 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.
[Display omitted]
•MERS-CoV/SARS-CoV S composite glycan shields analyzed by cryo-EM and mass spectrometry•Structures of MERS-CoV/SARS-CoV S with neutralizing antibodies from survivors•LCA60 inhibits receptor binding by interacting with MERS-CoV S protein/glycans•S230 blocks receptor binding and triggers fusogenic rearrangements via functional mimicry
Structural analysis of the SARS-CoV S and MERS-CoV S glycoproteins in complex with neutralizing antibodies from human survivors sheds light into the mechanisms of membrane fusion and neutralization 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. 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. Structural analysis of the SARS-CoV S and MERS-CoV S glycoproteins in complex with neutralizing antibodies from human survivors sheds light into the mechanisms of membrane fusion and neutralization 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. 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.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. |
| Author | Lanzavecchia, Antonio Gopal, Robin Dai, Mian Veesler, David Xiong, Xiaoli Zambon, Maria Cameroni, Elisabetta Walls, Alexandra C. Snijder, Joost Tortorici, M. Alejandra Quispe, Joel Rey, Félix A. Corti, Davide Park, Young-Jun |
| Author_xml | – sequence: 1 givenname: Alexandra C. surname: Walls fullname: Walls, Alexandra C. organization: Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA – sequence: 2 givenname: Xiaoli surname: Xiong fullname: Xiong, Xiaoli organization: Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA – sequence: 3 givenname: Young-Jun surname: Park fullname: Park, Young-Jun organization: Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA – sequence: 4 givenname: M. Alejandra surname: Tortorici fullname: Tortorici, M. Alejandra organization: Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA – sequence: 5 givenname: Joost surname: Snijder fullname: Snijder, Joost organization: Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA – sequence: 6 givenname: Joel surname: Quispe fullname: Quispe, Joel organization: Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA – sequence: 7 givenname: Elisabetta surname: Cameroni fullname: Cameroni, Elisabetta organization: Humabs Biomed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 8 givenname: Robin surname: Gopal fullname: Gopal, Robin organization: National Infection Service, Public Health England, London NW9 5HT, UK – sequence: 9 givenname: Mian surname: Dai fullname: Dai, Mian organization: Crick Worldwide Influenza Centre, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK – sequence: 10 givenname: Antonio surname: Lanzavecchia fullname: Lanzavecchia, Antonio organization: Institute for Research in Biomedicine, Faculty of Biomedical Sciences, Università della Svizzera italiana, 6500 Bellinzona, Switzerland – sequence: 11 givenname: Maria surname: Zambon fullname: Zambon, Maria organization: National Infection Service, Public Health England, London NW9 5HT, UK – sequence: 12 givenname: Félix A. surname: Rey fullname: Rey, Félix A. organization: Institute Pasteur & CNRS UMR 3569, Unité de Virologie Structurale, 75015, Paris, France – sequence: 13 givenname: Davide surname: Corti fullname: Corti, Davide organization: Humabs Biomed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 14 givenname: David surname: Veesler fullname: Veesler, David email: dveesler@uw.edu organization: Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/30712865$$D View this record in MEDLINE/PubMed https://pasteur.hal.science/pasteur-02546514$$DView record in HAL |
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| SubjectTerms | Animals Antibodies, Monoclonal Antibodies, Monoclonal - immunology Antibodies, Neutralizing Antibodies, Neutralizing - immunology Antibodies, Viral Antibodies, Viral - immunology Chlorocebus aethiops class I fusion protein Coronavirus Coronavirus - immunology Coronavirus - metabolism Coronavirus Infections Coronavirus Infections - immunology glycoproteins glycoproteomics HEK293 Cells Humans humoral immunity Immunity, Humoral Immunity, Humoral - immunology Life Sciences membrane fusion MERS-CoV Middle East Respiratory Syndrome Coronavirus Middle East Respiratory Syndrome Coronavirus - immunology Middle East Respiratory Syndrome Coronavirus - metabolism Molecular Mimicry Molecular Mimicry - immunology N-linked glycosylation neutralization neutralizing antibodies pandemic Protein Binding Receptors, Virus Receptors, Virus - metabolism SARS Virus SARS Virus - immunology SARS Virus - metabolism SARS-CoV Severe acute respiratory syndrome coronavirus spike glycoprotein Spike Glycoprotein, Coronavirus Spike Glycoprotein, Coronavirus - metabolism Spike Glycoprotein, Coronavirus - physiology Spike Glycoprotein, Coronavirus - ultrastructure Vero Cells Virus Internalization viruses |
| Title | Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion |
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