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

Issued Date

2020-01-01

Resource Type

Article

ISSN

15459985
15459993

DOI

10.1038/s41594-020-0480-y

Other identifier(s)

2-s2.0-85088842557

Rights

Mahidol University

Rights Holder(s)

SCOPUS

Bibliographic Citation

Nature Structural and Molecular Biology. (2020)

Suggested Citation

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. 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 Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient. Nature Structural and Molecular Biology. (2020). doi:10.1038/s41594-020-0480-y Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/57771

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Title

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

Author(s)

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. 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

Other Contributor(s)

Public Health England
 Diamond Light Source
 Academia Sinica, Genomics Research Center
 National Yang-Ming University Taiwan
 Chang Gung Memorial Hospital
 University of Oxford
 Taipei Medical University
 Chang Gung University
 Sir William Dunn School of Pathology
 Faculty of Medicine, Siriraj Hospital, Mahidol University
 Nuffield Department of Medicine
 MRC Weatherall Institute of Molecular Medicine
 The Rosalind Franklin Institute
 Research Complex

Abstract

© 2020, The Author(s), under exclusive licence to Springer Nature America, Inc. 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.

Keyword(s)

Biochemistry, Genetics and Molecular Biology

Availability

URI

https://repository.li.mahidol.ac.th/handle/20.500.14594/57771

Collections

Scopus 2020