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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/57771
Title: Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient
Authors: 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
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
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Jan-2020
Citation: Nature Structural and Molecular Biology. (2020)
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.
URI: http://repository.li.mahidol.ac.th/dspace/handle/123456789/57771
metadata.dc.identifier.url: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85088842557&origin=inward
ISSN: 15459985
15459993
Appears in Collections:Scopus 2020

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