• Emilie Seydoux, Leah J Homad, Anna J MacCamy, K Rachael Parks, Nicholas K Hurlburt, Madeleine F Jennewein, Nicholas R Akins, Andrew B Stuart, Yu-Hsin Wan, Junli Feng, Rachael E Whaley, Suruchi Singh, Michael Boeckh, Kristen W Cohen, M Juliana McElrath, Janet A Englund, Helen Y Chu, Marie Pancera, Andrew T McGuire, and Leonidas Stamatatos.
• Fred Hutchinson Cancer Research Center, Vaccines and Infectious Disease Division, Seattle, WA, USA.
• Immunity. 2020 Jul 14; 53 (1): 98-105.e5.

AbstractAntibody responses develop following SARS-CoV-2 infection, but little is known about their epitope specificities, clonality, binding affinities, epitopes, and neutralizing activity. We isolated B cells specific for the SARS-CoV-2 envelope glycoprotein spike (S) from a COVID-19-infected subject 21 days after the onset of clinical disease. 45 S-specific monoclonal antibodies were generated. They had undergone minimal somatic mutation with limited clonal expansion, and three bound the receptor-binding domain (RBD). Two antibodies neutralized SARS-CoV-2. The most potent antibody bound the RBD and prevented binding to the ACE2 receptor, while the other bound outside the RBD. Thus, most anti-S antibodies that were generated in this patient during the first weeks of COVID-19 infection were non-neutralizing and target epitopes outside the RBD. Antibodies that disrupt the SARS-CoV-2 S-ACE2 interaction can potently neutralize the virus without undergoing extensive maturation. Such antibodies have potential preventive and/or therapeutic potential and can serve as templates for vaccine design.Copyright © 2020 Elsevier Inc. All rights reserved.

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