Mapping Neutralizing and Immunodominant Sites on the SARS-CoV-2 Spike Receptor-Binding Domain by Structure-Guided High-Resolution Serology
Analysis of the specificity and kinetics of neutralizing antibodies (nAbs) elicited by SARS-CoV-2 infection is crucial for understanding immune protection and identifying targets for vaccine design. In a cohort of 647 SARS-CoV-2-infected subjects, we found that both the magnitude of Ab responses to...
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| Published in | Cell Vol. 183; no. 4; pp. 1024 - 1042.e21 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
12.11.2020
Elsevier |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Analysis of the specificity and kinetics of neutralizing antibodies (nAbs) elicited by SARS-CoV-2 infection is crucial for understanding immune protection and identifying targets for vaccine design. In a cohort of 647 SARS-CoV-2-infected subjects, we found that both the magnitude of Ab responses to SARS-CoV-2 spike (S) and nucleoprotein and nAb titers correlate with clinical scores. The receptor-binding domain (RBD) is immunodominant and the target of 90% of the neutralizing activity present in SARS-CoV-2 immune sera. Whereas overall RBD-specific serum IgG titers waned with a half-life of 49 days, nAb titers and avidity increased over time for some individuals, consistent with affinity maturation. We structurally defined an RBD antigenic map and serologically quantified serum Abs specific for distinct RBD epitopes leading to the identification of two major receptor-binding motif antigenic sites. Our results explain the immunodominance of the receptor-binding motif and will guide the design of COVID-19 vaccines and therapeutics.
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•SARS-CoV-2 RBD is immunodominant and accounts for 90% of serum neutralizing activity•RBD antibodies decline with a half-life of ∼50 days, but their avidity increases•Structural definition of a SARS-CoV-2 RBD antigenic map using monoclonal antibodies•ACE2-binding site dominates SARS-CoV-2 polyclonal neutralizing antibody responses
Serological analyses of ∼650 SARS-CoV-2-exposed individuals show that 90% of the serum or plasma neutralizing activity targets the virus receptor-binding domain, with structural insights revealing how distinct types of neutralizing antibodies targeting the ACE2-binding site dominate the immune response against SARS-CoV-2 spike. |
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| AbstractList | Analysis of the specificity and kinetics of neutralizing antibodies (nAbs) elicited by SARS-CoV-2 infection is crucial for understanding immune protection and identifying targets for vaccine design. In a cohort of 647 SARS-CoV-2-infected subjects, we found that both the magnitude of Ab responses to SARS-CoV-2 spike (S) and nucleoprotein and nAb titers correlate with clinical scores. The receptor-binding domain (RBD) is immunodominant and the target of 90% of the neutralizing activity present in SARS-CoV-2 immune sera. Whereas overall RBD-specific serum IgG titers waned with a half-life of 49 days, nAb titers and avidity increased over time for some individuals, consistent with affinity maturation. We structurally defined an RBD antigenic map and serologically quantified serum Abs specific for distinct RBD epitopes leading to the identification of two major receptor-binding motif antigenic sites. Our results explain the immunodominance of the receptor-binding motif and will guide the design of COVID-19 vaccines and therapeutics. Analysis of the specificity and kinetics of neutralizing antibodies (nAbs) elicited by SARS-CoV-2 infection is crucial for understanding immune protection and identifying targets for vaccine design. In a cohort of 647 SARS-CoV-2-infected subjects, we found that both the magnitude of Ab responses to SARS-CoV-2 spike (S) and nucleoprotein and nAb titers correlate with clinical scores. The receptor-binding domain (RBD) is immunodominant and the target of 90% of the neutralizing activity present in SARS-CoV-2 immune sera. Whereas overall RBD-specific serum IgG titers waned with a half-life of 49 days, nAb titers and avidity increased over time for some individuals, consistent with affinity maturation. We structurally defined an RBD antigenic map and serologically quantified serum Abs specific for distinct RBD epitopes leading to the identification of two major receptor-binding motif antigenic sites. Our results explain the immunodominance of the receptor-binding motif and will guide the design of COVID-19 vaccines and therapeutics. [Display omitted] •SARS-CoV-2 RBD is immunodominant and accounts for 90% of serum neutralizing activity•RBD antibodies decline with a half-life of ∼50 days, but their avidity increases•Structural definition of a SARS-CoV-2 RBD antigenic map using monoclonal antibodies•ACE2-binding site dominates SARS-CoV-2 polyclonal neutralizing antibody responses Serological analyses of ∼650 SARS-CoV-2-exposed individuals show that 90% of the serum or plasma neutralizing activity targets the virus receptor-binding domain, with structural insights revealing how distinct types of neutralizing antibodies targeting the ACE2-binding site dominate the immune response against SARS-CoV-2 spike. Analysis of the specificity and kinetics of neutralizing antibodies (nAbs) elicited by SARS-CoV-2 infection is crucial for understanding immune protection and identifying targets for vaccine design. In a cohort of 647 SARS-CoV-2-infected subjects, we found that both the magnitude of Ab responses to SARS-CoV-2 spike (S) and nucleoprotein and nAb titers correlate with clinical scores. The receptor-binding domain (RBD) is immunodominant and the target of 90% of the neutralizing activity present in SARS-CoV-2 immune sera. Whereas overall RBD-specific serum IgG titers waned with a half-life of 49 days, nAb titers and avidity increased over time for some individuals, consistent with affinity maturation. We structurally defined an RBD antigenic map and serologically quantified serum Abs specific for distinct RBD epitopes leading to the identification of two major receptor-binding motif antigenic sites. Our results explain the immunodominance of the receptor-binding motif and will guide the design of COVID-19 vaccines and therapeutics. Analysis of the specificity and kinetics of neutralizing antibodies (nAbs) elicited by SARS-CoV-2 infection is crucial for understanding immune protection and identifying targets for vaccine design. In a cohort of 647 SARS-CoV-2-infected subjects, we found that both the magnitude of Ab responses to SARS-CoV-2 spike (S) and nucleoprotein and nAb titers correlate with clinical scores. The receptor-binding domain (RBD) is immunodominant and the target of 90% of the neutralizing activity present in SARS-CoV-2 immune sera. Whereas overall RBD-specific serum IgG titers waned with a half-life of 49 days, nAb titers and avidity increased over time for some individuals, consistent with affinity maturation. We structurally defined an RBD antigenic map and serologically quantified serum Abs specific for distinct RBD epitopes leading to the identification of two major receptor-binding motif antigenic sites. Our results explain the immunodominance of the receptor-binding motif and will guide the design of COVID-19 vaccines and therapeutics.Analysis of the specificity and kinetics of neutralizing antibodies (nAbs) elicited by SARS-CoV-2 infection is crucial for understanding immune protection and identifying targets for vaccine design. In a cohort of 647 SARS-CoV-2-infected subjects, we found that both the magnitude of Ab responses to SARS-CoV-2 spike (S) and nucleoprotein and nAb titers correlate with clinical scores. The receptor-binding domain (RBD) is immunodominant and the target of 90% of the neutralizing activity present in SARS-CoV-2 immune sera. Whereas overall RBD-specific serum IgG titers waned with a half-life of 49 days, nAb titers and avidity increased over time for some individuals, consistent with affinity maturation. We structurally defined an RBD antigenic map and serologically quantified serum Abs specific for distinct RBD epitopes leading to the identification of two major receptor-binding motif antigenic sites. Our results explain the immunodominance of the receptor-binding motif and will guide the design of COVID-19 vaccines and therapeutics. Analysis of the specificity and kinetics of neutralizing antibodies (nAbs) elicited by SARS-CoV-2 infection is crucial for understanding immune protection and identifying targets for vaccine design. In a cohort of 647 SARS-CoV-2-infected subjects, we found that both the magnitude of Ab responses to SARS-CoV-2 spike (S) and nucleoprotein and nAb titers correlate with clinical scores. The receptor-binding domain (RBD) is immunodominant and the target of 90% of the neutralizing activity present in SARS-CoV-2 immune sera. Whereas overall RBD-specific serum IgG titers waned with a half-life of 49 days, nAb titers and avidity increased over time for some individuals, consistent with affinity maturation. We structurally defined an RBD antigenic map and serologically quantified serum Abs specific for distinct RBD epitopes leading to the identification of two major receptor-binding motif antigenic sites. Our results explain the immunodominance of the receptor-binding motif and will guide the design of COVID-19 vaccines and therapeutics. • SARS-CoV-2 RBD is immunodominant and accounts for 90% of serum neutralizing activity • RBD antibodies decline with a half-life of ∼50 days, but their avidity increases • Structural definition of a SARS-CoV-2 RBD antigenic map using monoclonal antibodies • ACE2-binding site dominates SARS-CoV-2 polyclonal neutralizing antibody responses Serological analyses of ∼650 SARS-CoV-2-exposed individuals show that 90% of the serum or plasma neutralizing activity targets the virus receptor-binding domain, with structural insights revealing how distinct types of neutralizing antibodies targeting the ACE2-binding site dominate the immune response against SARS-CoV-2 spike. We report analysis of the specificity and kinetics of neutralizing antibodies (nAbs) elicited by SARS-CoV-2 infection is crucial for understanding immune protection and identifying targets for vaccine design. In a cohort of 647 SARS-CoV-2-infected subjects, we found that both the magnitude of Ab responses to SARS-CoV-2 spike (S) and nucleoprotein and nAb titers correlate with clinical scores. The receptor-binding domain (RBD) is immunodominant and the target of 90% of the neutralizing activity present in SARS-CoV-2 immune sera. Whereas overall RBD-specific serum IgG titers waned with a half-life of 49 days, nAb titers and avidity increased over time for some individuals, consistent with affinity maturation. We structurally defined an RBD antigenic map and serologically quantified serum Abs specific for distinct RBD epitopes leading to the identification of two major receptor-binding motif antigenic sites. Our results explain the immunodominance of the receptor-binding motif and will guide the design of COVID-19 vaccines and therapeutics. |
| Author | Snell, Gyorgy Hong, David Fink, Katja Virgin, Herbert W. Sprugasci, Nicole Bowen, John E. Czudnochowski, Nadine Rodriguez, Blanca Fernandez Sallusto, Federica Guarino, Barbara Riva, Agostino Ceschi, Alessandro Silacci-Fregni, Chiara De Marco, Anna Lepori, Valentino Park, Young-Jun Tarkowski, Maciej Lo Presti, Giorgia Nix, Jay C. Rosen, Laura E. Piumatti, Giovanni Biggiogero, Maira Elzi, Luigia Garzoni, Christian Lanzavecchia, Antonio Zatta, Fabrizia Veesler, David Jaconi, Stefano Acton, Oliver J. Beltramello, Martina Walls, Alexandra C. Tortorici, M. Alejandra Peter, Alessia Gupta, Sneha V. Havenar-Daughton, Colin Jovic, Sandra Pellanda, Alessandra Franzetti Bernasconi, Enos Ferrari, Paolo Minola, Andrea Albanese, Emiliano Cameroni, Elisabetta Pinto, Dora Jin, Feng Piccoli, Luca Corti, Davide Pizzuto, Matteo S. Bassi, Jessica Mele, Federico Smithey, Megan |
| Author_xml | – sequence: 1 givenname: Luca surname: Piccoli fullname: Piccoli, Luca organization: Humabs BioMed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 2 givenname: Young-Jun surname: Park fullname: Park, Young-Jun organization: Department of Biochemistry, University of Washington, Seattle, WA 98195, USA – sequence: 3 givenname: M. Alejandra surname: Tortorici fullname: Tortorici, M. Alejandra organization: Department of Biochemistry, University of Washington, Seattle, WA 98195, USA – sequence: 4 givenname: Nadine surname: Czudnochowski fullname: Czudnochowski, Nadine organization: Vir Biotechnology, San Francisco, CA 94158, USA – sequence: 5 givenname: Alexandra C. surname: Walls fullname: Walls, Alexandra C. organization: Department of Biochemistry, University of Washington, Seattle, WA 98195, USA – sequence: 6 givenname: Martina surname: Beltramello fullname: Beltramello, Martina organization: Humabs BioMed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 7 givenname: Chiara surname: Silacci-Fregni fullname: Silacci-Fregni, Chiara organization: Humabs BioMed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 8 givenname: Dora surname: Pinto fullname: Pinto, Dora organization: Humabs BioMed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 9 givenname: Laura E. surname: Rosen fullname: Rosen, Laura E. organization: Vir Biotechnology, San Francisco, CA 94158, USA – sequence: 10 givenname: John E. surname: Bowen fullname: Bowen, John E. organization: Department of Biochemistry, University of Washington, Seattle, WA 98195, USA – sequence: 11 givenname: Oliver J. surname: Acton fullname: Acton, Oliver J. organization: Department of Biochemistry, University of Washington, Seattle, WA 98195, USA – sequence: 12 givenname: Stefano surname: Jaconi fullname: Jaconi, Stefano organization: Humabs BioMed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 13 givenname: Barbara surname: Guarino fullname: Guarino, Barbara organization: Humabs BioMed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 14 givenname: Andrea surname: Minola fullname: Minola, Andrea organization: Humabs BioMed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 15 givenname: Fabrizia surname: Zatta fullname: Zatta, Fabrizia organization: Humabs BioMed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 16 givenname: Nicole surname: Sprugasci fullname: Sprugasci, Nicole organization: Humabs BioMed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 17 givenname: Jessica surname: Bassi fullname: Bassi, Jessica organization: Humabs BioMed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 18 givenname: Alessia surname: Peter fullname: Peter, Alessia organization: Humabs BioMed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 19 givenname: Anna surname: De Marco fullname: De Marco, Anna organization: Humabs BioMed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 20 givenname: Jay C. surname: Nix fullname: Nix, Jay C. organization: Molecular Biology Consortium, Advanced Light Source, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA – sequence: 21 givenname: Federico surname: Mele fullname: Mele, Federico organization: Institute for Research in Biomedicine, Università della Svizzera italiana, 6500 Bellinzona, Switzerland – sequence: 22 givenname: Sandra surname: Jovic fullname: Jovic, Sandra organization: Institute for Research in Biomedicine, Università della Svizzera italiana, 6500 Bellinzona, Switzerland – sequence: 23 givenname: Blanca Fernandez surname: Rodriguez fullname: Rodriguez, Blanca Fernandez organization: Institute for Research in Biomedicine, Università della Svizzera italiana, 6500 Bellinzona, Switzerland – sequence: 24 givenname: Sneha V. surname: Gupta fullname: Gupta, Sneha V. organization: Vir Biotechnology, San Francisco, CA 94158, USA – sequence: 25 givenname: Feng surname: Jin fullname: Jin, Feng organization: Vir Biotechnology, San Francisco, CA 94158, USA – sequence: 26 givenname: Giovanni surname: Piumatti fullname: Piumatti, Giovanni organization: Division of Primary Care, Geneva University Hospitals, 1205 Geneva, Switzerland – sequence: 27 givenname: Giorgia surname: Lo Presti fullname: Lo Presti, Giorgia organization: Clinic of Internal Medicine and Infectious Diseases, Clinica Luganese Moncucco, 6900 Lugano, Switzerland – sequence: 28 givenname: Alessandra Franzetti surname: Pellanda fullname: Pellanda, Alessandra Franzetti organization: Clinic of Internal Medicine and Infectious Diseases, Clinica Luganese Moncucco, 6900 Lugano, Switzerland – sequence: 29 givenname: Maira surname: Biggiogero fullname: Biggiogero, Maira organization: Clinic of Internal Medicine and Infectious Diseases, Clinica Luganese Moncucco, 6900 Lugano, Switzerland – sequence: 30 givenname: Maciej surname: Tarkowski fullname: Tarkowski, Maciej organization: III Division of Infectious Diseases, ASST Fatebenefratelli Sacco, Luigi Sacco Hospital, 20157 Milan, Italy – sequence: 31 givenname: Matteo S. surname: Pizzuto fullname: Pizzuto, Matteo S. organization: Humabs BioMed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 32 givenname: Elisabetta surname: Cameroni fullname: Cameroni, Elisabetta organization: Humabs BioMed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 33 givenname: Colin surname: Havenar-Daughton fullname: Havenar-Daughton, Colin organization: Vir Biotechnology, San Francisco, CA 94158, USA – sequence: 34 givenname: Megan surname: Smithey fullname: Smithey, Megan organization: Vir Biotechnology, San Francisco, CA 94158, USA – sequence: 35 givenname: David surname: Hong fullname: Hong, David organization: Vir Biotechnology, San Francisco, CA 94158, USA – sequence: 36 givenname: Valentino surname: Lepori fullname: Lepori, Valentino organization: Independent Physician, 6500 Bellinzona, Switzerland – sequence: 37 givenname: Emiliano surname: Albanese fullname: Albanese, Emiliano organization: Institute of Public Health, Università della Svizzera italiana, 6900 Lugano, Switzerland – sequence: 38 givenname: Alessandro surname: Ceschi fullname: Ceschi, Alessandro organization: Faculty of Biomedical Sciences, Università della Svizzera italiana, 6900 Lugano, Switzerland – sequence: 39 givenname: Enos surname: Bernasconi fullname: Bernasconi, Enos organization: Division of Infectious Diseases, Ente Ospedaliero Cantonale, Ospedale Civico and Ospedale Italiano, 6900 Lugano, Switzerland – sequence: 40 givenname: Luigia surname: Elzi fullname: Elzi, Luigia organization: Division of Infectious Diseases, Ente Ospedaliero Cantonale, Ospedale Regionale Bellinzona e Valli and Ospedale Regionale, 6600 Locarno, Switzerland – sequence: 41 givenname: Paolo surname: Ferrari fullname: Ferrari, Paolo organization: Department of Nephrology, Ospedale Civico Lugano, Ente Ospedaliero Cantonale, 6900 Lugano, Switzerland – sequence: 42 givenname: Christian surname: Garzoni fullname: Garzoni, Christian organization: Clinic of Internal Medicine and Infectious Diseases, Clinica Luganese Moncucco, 6900 Lugano, Switzerland – sequence: 43 givenname: Agostino surname: Riva fullname: Riva, Agostino organization: III Division of Infectious Diseases, ASST Fatebenefratelli Sacco, Luigi Sacco Hospital, 20157 Milan, Italy – sequence: 44 givenname: Gyorgy surname: Snell fullname: Snell, Gyorgy organization: Vir Biotechnology, San Francisco, CA 94158, USA – sequence: 45 givenname: Federica surname: Sallusto fullname: Sallusto, Federica organization: Institute for Research in Biomedicine, Università della Svizzera italiana, 6500 Bellinzona, Switzerland – sequence: 46 givenname: Katja surname: Fink fullname: Fink, Katja organization: Humabs BioMed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 47 givenname: Herbert W. surname: Virgin fullname: Virgin, Herbert W. organization: Vir Biotechnology, San Francisco, CA 94158, USA – sequence: 48 givenname: Antonio surname: Lanzavecchia fullname: Lanzavecchia, Antonio organization: Humabs BioMed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 49 givenname: Davide surname: Corti fullname: Corti, Davide email: dcorti@vir.bio organization: Humabs BioMed SA, Vir Biotechnology, 6500 Bellinzona, Switzerland – sequence: 50 givenname: David surname: Veesler fullname: Veesler, David email: dveesler@uw.edu organization: Department of Biochemistry, University of Washington, Seattle, WA 98195, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32991844$$D View this record in MEDLINE/PubMed https://pasteur.hal.science/pasteur-02984796$$DView record in HAL https://www.osti.gov/servlets/purl/1846169$$D View this record in Osti.gov |
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| Snippet | Analysis of the specificity and kinetics of neutralizing antibodies (nAbs) elicited by SARS-CoV-2 infection is crucial for understanding immune protection and... We report analysis of the specificity and kinetics of neutralizing antibodies (nAbs) elicited by SARS-CoV-2 infection is crucial for understanding immune... |
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| SubjectTerms | Angiotensin-Converting Enzyme 2 Antibodies, Monoclonal - chemistry Antibodies, Monoclonal - genetics Antibodies, Monoclonal - immunology Antibodies, Neutralizing - blood Antibodies, Neutralizing - chemistry Antibodies, Neutralizing - immunology Antibodies, Viral - blood Antibodies, Viral - chemistry Antibodies, Viral - immunology Antigen-Antibody Reactions BASIC BIOLOGICAL SCIENCES Betacoronavirus - immunology Betacoronavirus - isolation & purification Betacoronavirus - metabolism Binding Sites Biochemistry, Molecular Biology blood serum Coronavirus Infections - pathology Coronavirus Infections - virology coronaviruses COVID-19 COVID-19 infection effector functions Epitope Mapping - methods Epitopes - chemistry Epitopes - immunology half life Humans immunity Immunoglobulin A - blood Immunoglobulin A - immunology Immunoglobulin G - blood Immunoglobulin G - immunology Immunoglobulin M - blood Immunoglobulin M - immunology Kinetics Life Sciences Molecular Dynamics Simulation neutralizing antibodies nucleoproteins Pandemics Peptidyl-Dipeptidase A - chemistry Peptidyl-Dipeptidase A - metabolism Pneumonia, Viral - pathology Pneumonia, Viral - virology Protein Binding Protein Domains - immunology Protein Structure, Quaternary SARS-CoV-2 serology Severe acute respiratory syndrome coronavirus 2 Spike Glycoprotein, Coronavirus - chemistry Spike Glycoprotein, Coronavirus - genetics Spike Glycoprotein, Coronavirus - immunology Spike Glycoprotein, Coronavirus - metabolism therapeutics vaccine development |
| Title | Mapping Neutralizing and Immunodominant Sites on the SARS-CoV-2 Spike Receptor-Binding Domain by Structure-Guided High-Resolution Serology |
| URI | https://dx.doi.org/10.1016/j.cell.2020.09.037 https://www.ncbi.nlm.nih.gov/pubmed/32991844 https://www.proquest.com/docview/2447548306 https://www.proquest.com/docview/2524328527 https://pasteur.hal.science/pasteur-02984796 https://www.osti.gov/servlets/purl/1846169 https://pubmed.ncbi.nlm.nih.gov/PMC7494283 |
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