Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation

Nicholas K. Hurlburt, Emilie Seydoux, Yu-Hsin Wan, Venkata Viswanadh Edara, Andrew B. Stuart, Junli Feng, Mehul S. Suthar, Andrew T. McGuire, Leonidas Stamatatos and Marie Pancera ()
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Nicholas K. Hurlburt: Vaccines and Infectious Diseases Division
Emilie Seydoux: Vaccines and Infectious Diseases Division
Yu-Hsin Wan: Vaccines and Infectious Diseases Division
Venkata Viswanadh Edara: Emory University School of Medicine
Andrew B. Stuart: Vaccines and Infectious Diseases Division
Junli Feng: Vaccines and Infectious Diseases Division
Mehul S. Suthar: Emory University School of Medicine
Andrew T. McGuire: Vaccines and Infectious Diseases Division
Leonidas Stamatatos: Vaccines and Infectious Diseases Division
Marie Pancera: Vaccines and Infectious Diseases Division

Nature Communications, 2020, vol. 11, issue 1, 1-7

Abstract: Abstract SARS-CoV-2 is a betacoronavirus virus responsible for the COVID-19 pandemic. Here, we determine the X-ray crystal structure of a potent neutralizing monoclonal antibody, CV30, isolated from a patient infected with SARS-CoV-2, in complex with the receptor binding domain. The structure reveals that CV30 binds to an epitope that overlaps with the human ACE2 receptor binding motif providing a structural basis for its neutralization. CV30 also induces shedding of the S1 subunit, indicating an additional mechanism of neutralization. A germline reversion of CV30 results in a substantial reduction in both binding affinity and neutralization potential indicating the minimal somatic mutation is needed for potently neutralizing antibodies against SARS-CoV-2.

Date: 2020
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DOI: 10.1038/s41467-020-19231-9

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