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

Nicholas K. Hurlburt, Emilie Seydoux, Yu-Hsin Wan and 7 more

Nature Communications · 2020 · CC BY

doi:10.1038/s41467-020-19231-9

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.

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