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

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

doi:10.1016/j.cell.2020.06.025

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

Journal Article · Wed Jun 24 00:00:00 EDT 2020 · Cell

DOI:https://doi.org/10.1016/j.cell.2020.06.025· OSTI ID:1816377

Barnes, Christopher O. ^[1]; West, Anthony P. ^[2]; Huey-Tubman, Kathryn E. ^[2]; Hoffmann, Magnus A. G. ^[2]; Sharaf, Naima G. ^[3]; Hoffman, Pauline R. ^[2]; Koranda, Nicholas ^[2]; Gristick, Harry B. ^[2]; Gaebler, Christian ^[4]; Muecksch, Frauke ^[5]; Lorenzi, Julio C. Cetrulo ^[4]; Finkin, Shlomo ^[4]; Hägglöf, Thomas ^[4]; Hurley, Arlene ^[6]; Millard, Katrina G. ^[4]; Weisblum, Yiska ^[5]; Schmidt, Fabian ^[5]; Hatziioannou, Theodora ^[5]; Bieniasz, Paul D. ^[7]; Caskey, Marina ^[4] more »

California Institute of Technology (CalTech), Pasadena, CA (United States). Division of Biology and Biological Engineering; OSTI
California Institute of Technology (CalTech), Pasadena, CA (United States). Division of Biology and Biological Engineering
California Institute of Technology (CalTech), Pasadena, CA (United States). Division of Chemistry and Chemical Engineering
Rockefeller Univ., New York, NY (United States). Lab. of Molecular Immunology
Rockefeller Univ., New York, NY (United States). Lab. of Retrovirology
Rockefeller Univ., New York, NY (United States). Hospital Program Direction
Rockefeller Univ., New York, NY (United States). Lab. of Retrovirology; Howard Hughes Medical Inst., Chevy Chase, MD (United States)
Rockefeller Univ., New York, NY (United States). Lab. of Molecular Immunology; Universita della Svizzera italiana, Bellinzona (Switzerland). Inst. for Research in Biomedicine
Rockefeller Univ., New York, NY (United States). Lab. of Molecular Immunology; Howard Hughes Medical Inst., Chevy Chase, MD (United States)

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 cryoelectron 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.

View Accepted Manuscript (DOE)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institutes of Health (NIH); Bill and Melinda Gates Foundation

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 1816377

Journal Information:: Cell, Journal Name: Cell Journal Issue: 4 Vol. 182; ISSN 0092-8674

Publisher:: ElsevierCopyright Statement

Country of Publication:: United States

Language:: English

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

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