@article{efe7fc9c3c5e412697103fdc52f89ffb,
title = "A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV",
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 = "COVID-19, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)",
author = "Meng Yuan and Wu, {Nicholas C.} and Xueyong Zhu and Lee, {Chang Chun D.} and So, {Ray T.Y.} and Huibin Lv and Mok, {Chris K.P.} and Wilson, {Ian A.}",
note = "Funding Information: This work was supported by National Institutes of Health grant K99 AI139445 (N.C.W.); a Calmette and Yersin scholarship from the Pasteur International Network Association (H.L.); Bill and Melinda Gates Foundation grant OPP1170236 (I.A.W.); Guangzhou Medical University High-level University Innovation Team Training Program (Guangzhou Medical University released [2017] no. 159) (C.K.P.M.); and National Natural Science Foundation of China (NSFC)/ Research Grants Council (RGC) Joint Research Scheme (N_HKU737/18) (C.K.P.M.). General Medical Sciences and Cancer Institutes Structural Biology Facility at the Advanced Photon Source (APS) has been funded by federal funds from the National Cancer Institute (ACB-12002) and the National Institute of General Medical Sciences (AGM-12006). This research used resources of the APS, a U.S. Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Argonne National Laboratory under contract DE-AC02-06CH11357.",
year = "2020",
month = may,
day = "8",
doi = "10.1126/science.abb7269",
language = "English (US)",
volume = "368",
pages = "630--633",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "6491",
}