Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient

Daming Zhou, Helen M.E. 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 N.M. Shah, Tiong Kit Tan, Pramila Rijal, Robert F. DonatKerry 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

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166 引文 斯高帕斯(Scopus)


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 candidate therapeutic for COVID-19.

頁(從 - 到)950-958
期刊Nature Structural and Molecular Biology
出版狀態已發佈 - 10月 1 2020

ASJC Scopus subject areas

  • 結構生物學
  • 分子生物學


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