Emilie Seydoux, L. Homad, A. MacCamy, K. R. Parks, N. Hurlburt, M. Jennewein, Nicholas R. Akins, A. Stuart, Yu-Hsin Wan, Junli Feng, Rachael E. Whaley, Suruchi Singh, M. Boeckh, K. Cohen, M. McElrath, J. Englund, H. Chu, M. Pancera, A. McGuire, L. Stamatatos
Immunity, 2020
Abstract Antibody 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 twenty-one days after the onset of clinical disease. Forty-five 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.
Cited by 183 publications.
Field of study: Biology