Structural basis of a public antibody response to SARS-CoV-2
Nicholas C. Wu,
Chang-Chun D. Lee,
Thomas F Rogers,
Joseph G Jardine,
Dennis R Burton,
Ian A. Wilson
Posted 09 Jun 2020
bioRxiv DOI: 10.1101/2020.06.08.141267 (published DOI: 10.1126/science.abd2321)
Posted 09 Jun 2020
Molecular-level understanding of human neutralizing antibody responses to SARS-CoV-2 could accelerate vaccine design and facilitate drug discovery. We analyzed 294 SARS-CoV-2 antibodies and found that IGHV3-53 is the most frequently used IGHV gene for targeting the receptor binding domain (RBD) of the spike (S) protein. We determined crystal structures of two IGHV3-53 neutralizing antibodies +/- Fab CR3022 ranging from 2.33- to 3.11-angstrom resolution. The germline-encoded residues of IGHV3-53 dominate binding to the ACE2 binding site epitope with no overlap with the CR3022 epitope. Moreover, IGHV3-53 is used in combination with a very short CDR H3 and different light chains. Overall, IGHV3-53 represents a versatile public VH in neutralizing SARS-CoV-2 antibodies, where their specific germline features and minimal affinity maturation provide important insights for vaccine design and assessing outcomes. ### Competing Interest Statement The authors have declared no competing interest.
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