Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies | Zendy

Christopher O. Barnes | Zendy; Anthony P. West | Zendy; Kathryn E. HueyTubman | Zendy; Magnus A. G. Hoffmann | Zendy; Naima G. Sharaf | Zendy; Pauline R. Hoffman | Zendy; Nicholas Koranda | Zendy; Harry B. Gristick | Zendy; Christian Gaebler | Zendy; Frauke Muecksch | Zendy; Julio C. C. Lorenzi | Zendy; Shlomo Finkin | Zendy; Thomas Hägglöf | Zendy; Arlene Hurley | Zendy; Katrina G. Millard | Zendy; Yiska Weisblum | Zendy; Fabian Schmidt | Zendy; Théodora Hatziioannou | Zendy; Paul D. Bieniasz | Zendy; Marina Caskey | Zendy; Davide F. Robbiani | Zendy; Michel C. Nussenzweig | Zendy; Pamela J. Björkman | Zendy

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Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies

Author(s) -

Christopher O. Barnes,

Anthony P. West,

Kathryn E. HueyTubman,

Magnus A. G. Hoffmann,

Naima G. Sharaf,

Pauline R. Hoffman,

Nicholas Koranda,

Harry B. Gristick,

Christian Gaebler,

Frauke Muecksch,

Julio C. C. Lorenzi,

Shlomo Finkin,

Thomas Hägglöf,

Arlene Hurley,

Katrina G. Millard,

Yiska Weisblum,

Fabian Schmidt,

Théodora Hatziioannou,

Paul D. Bieniasz,

Marina Caskey,

Davide F. Robbiani,

Michel C. Nussenzweig,

Pamela J. Björkman

Publication year - 2020

Publication title -

cell

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 26.304

H-Index - 776

eISSN - 1097-4172

pISSN - 0092-8674

DOI - 10.1016/j.cell.2020.06.025

Subject(s) - epitope , polyclonal antibodies , avidity , antibody , biology , virology , monoclonal antibody , neutralization , epitope mapping , linear epitope , spike protein , spike (software development) , immunoglobulin g , polyclonal b cell response , coronavirus , immunology , covid-19 , b cell , b cell receptor , medicine , disease , management , pathology , economics , infectious disease (medical specialty)

Neutralizing antibody responses to coronaviruses mainly target the receptor-binding domain (RBD) of the trimeric spike. Here, we characterized polyclonal immunoglobulin Gs (IgGs) and Fabs from COVID-19 convalescent individuals for recognition of coronavirus spikes. Plasma IgGs differed in their focus on RBD epitopes, recognition of alpha- and beta-coronaviruses, and contributions of avidity to increased binding/neutralization of IgGs over Fabs. Using electron microscopy, we examined specificities of polyclonal plasma Fabs, revealing recognition of both S1 A and RBD epitopes on SARS-CoV-2 spike. Moreover, a 3.4 Å cryo-electron microscopy (cryo-EM) structure of a neutralizing monoclonal Fab-spike complex revealed an epitope that blocks ACE2 receptor binding. Modeling based on these structures suggested different potentials for inter-spike crosslinking by IgGs on viruses, and characterized IgGs would not be affected by identified SARS-CoV-2 spike mutations. Overall, our studies structurally define a recurrent anti-SARS-CoV-2 antibody class derived from VH3-53/VH3-66 and similarity to a SARS-CoV VH3-30 antibody, providing criteria for evaluating vaccine-elicited antibodies.

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