美国斯克里普斯研究所Ian A. Wilson与中国香港大学Chris K. P. Mok等研究人员合作有了新发现。他们解析了新冠病毒（SARS-CoV-2）和SARS病毒（SARS-CoV）受体结合域中高度保守的抗原决定簇。相关论文于2020年4月3日在线发表在《科学》杂志上。
Title: A highly conserved cryptic epitope in the receptor-binding domains of SARS-CoV-2 and SARS-CoV
Author: Meng Yuan, Nicholas C. Wu, Xueyong Zhu, Chang-Chun D. Lee, Ray T. Y. So, Huibin Lv, Chris K. P. Mok, Ian A. Wilson
Abstract: Abstract The outbreak of COVID-19 caused by SARS-CoV-2 virus 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 to 3.1 . 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 RBD on the trimeric S protein are in the “up” conformation and slightly rotated. Overall, this study provides molecular insights into antibody recognition of SARS-CoV-2.