Broad cross-reactivity across sarbecoviruses exhibited by a subset of COVID-19 donor-derived neutralizing antibodies
Claudia A. Jette, Alexander A. Cohen, Priyanthi N.P. Gnanapragasam, Frauke Muecksch, Yu E. Lee, Kathryn E. Huey‐Tubman, Fabian Schmidt, Théodora Hatziioannou, Paul D. Bieniasz, Michel C. Nussenzweig, Anthony P. West, Jennifer R. Keeffe, Pamela J. Björkman, Christopher O. Barnes
Abstract
(Cell Reports 36, 109760-1–109760-15.e1-e7; September 28, 2021) In the originally published version of this article, the key in Figure 1C was inverted, with the green shade as the greatest binding AUC and the red shade as the lowest binding AUC. The correct key should have the red shade as the greatest binding AUC and the green shade as lowest binding AUC. Figure 1 has been corrected online and appears below. The authors regret this error.Figure 1. C118 and C022 show diverse binding and neutralization of sarbecoviruses (original)View Large Image Figure ViewerDownload Hi-res image Download (PPT) Broad cross-reactivity across sarbecoviruses exhibited by a subset of COVID-19 donor-derived neutralizing antibodiesJette et al.Cell ReportsSeptember 16, 2021In BriefJette et al. characterize antibodies derived from convalescent COVID-19 donors that broadly recognize sarbecoviruses and neutralize ACE2-tropic strains, including all SARS-CoV-2 variants of concern. Structures reveal binding to a highly conserved RBD epitope using long CDRH3 loops, with an orientation that inhibits ACE2 binding to the RBD and allows IgG avidity. Full-Text PDF Open Access