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A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV

Meng Yuan, Sciprofile linkNicholas C. Wu, Sciprofile linkXueyong Zhu, Sciprofile linkChang-Chun D. Lee, Ray T. Y. So, Huibin Lv, Sciprofile linkChris K.P. Mok, Sciprofile linkIan A. Wilson
Science , Volume 368, pp 630-633; doi:10.1126/science.abb7269

Abstract: The outbreak of coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome–coronavirus 2 (SARS-CoV-2) has now become a pandemic, but there is currently very little understanding of the antigenicity of the virus. We therefore determined the crystal structure of CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient, in complex with the receptor binding domain (RBD) of the SARS-CoV-2 spike (S) protein at 3.1-angstrom resolution. CR3022 targets a highly conserved epitope, distal from the receptor binding site, that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding epitope can only be accessed by CR3022 when at least two RBDs on the trimeric S protein are in the “up” conformation and slightly rotated. These results provide molecular insights into antibody recognition of SARS-CoV-2.
Keywords: Antibody / Conformation / Protein / Epitope / structural / Receptor binding / Coronavirus / COV

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