作者
Daming Zhou, Helen ME Duyvesteyn, Cheng-Pin Chen, Chung-Guei Huang, Ting-Hua Chen, Shin-Ru Shih, Yi-Chun Lin, Chien-Yu Cheng, Shu-Hsing Cheng, Yhu-Chering Huang, Tzou-Yien Lin, Che Ma, Jiandong Huo, Loic Carrique, Tomas Malinauskas, Reinis R Ruza, Pranav NM Shah, Tiong Kit Tan, Pramila Rijal, Robert F Donat, Kerry Godwin, Karen R Buttigieg, Julia A Tree, Julika Radecke, Neil G Paterson, Piyada Supasa, Juthathip Mongkolsapaya, Gavin R Screaton, Miles W Carroll, Javier Gilbert-Jaramillo, Michael L Knight, William James, Raymond J Owens, James H Naismith, Alain R Townsend, Elizabeth E Fry, Yuguang Zhao, Jingshan Ren, David I Stuart, Kuan-Ying A Huang
发表日期
2020/10
期刊
Nature structural & molecular biology
卷号
27
期号
10
页码范围
950-958
出版商
Nature Publishing Group
简介
The COVID-19 pandemic has had an unprecedented health and economic impact and there are currently no approved therapies. We have isolated an antibody, EY6A, from an individual convalescing from COVID-19 and have shown that it neutralizes SARS-CoV-2 and cross-reacts with SARS-CoV-1. EY6A Fab binds the receptor binding domain (RBD) of the viral spike glycoprotein tightly (KD of 2 nM), and a 2.6-Å-resolution crystal structure of an RBD–EY6A Fab complex identifies the highly conserved epitope, away from the ACE2 receptor binding site. Residues within this footprint are key to stabilizing the pre-fusion spike. Cryo-EM analyses of the pre-fusion spike incubated with EY6A Fab reveal a complex of the intact spike trimer with three Fabs bound and two further multimeric forms comprising the destabilized spike attached to Fab. EY6A binds what is probably a major neutralizing epitope, making it a …
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D Zhou, HME Duyvesteyn, CP Chen, CG Huang… - Nature structural & molecular biology, 2020