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

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

Year of Publication: 2020
Contained in: Nature structural & molecular biology Vol. 27, No. 10 (2020), p. 950-958
All journal articles: Search for all articles in this journal
Language: English
Contributors: Zhou, Daming | Author
Duyvesteyn, Helen M E
Chen, Cheng-Pin
Huang, Chung-Guei
Chen, Ting-Hua
Shih, Shin-Ru
Lin, Yi-Chun
Cheng, Chien-Yu
Cheng, Shu-Hsing
Huang, Yhu-Chering
Lin, Tzou-Yien
Ma, Che
Huo, Jiandong
Carrique, Loic
Malinauskas, Tomas
Ruza, Reinis R
Shah, Pranav N M
Tan, Tiong Kit
Rijal, Pramila
Donat, Robert F
Godwin, Kerry
Buttigieg, Karen R
Tree, Julia A
Radecke, Julika
Paterson, Neil G
Supasa, Piyada
Mongkolsapaya, Juthathip
Screaton, Gavin R
Carroll, Miles W
Gilbert-Jaramillo, Javier
Knight, Michael L
James, William
Owens, Raymond J
Naismith, James H
Townsend, Alain R
Fry, Elizabeth E
Zhao, Yuguang
Ren, Jingshan
Stuart, David I
Huang, Kuan-Ying A
Full text access:
Electronic availability is being checked...
Links: Full Text (dx.doi.org)
Keywords: Journal Article
Research Support, Non-U.S. Gov't
ISSN: 1545-9985
Note: Copyright: From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Notes: Date Revised 21.10.2020
published: Print-Electronic
Citation Status In-Process
Copyright: From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
PMID:
    32737466
Physical Description: Online-Ressource
ID (e.g. DOI, URN): 10.1038/s41594-020-0480-y
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520 |a 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 
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700 1 |a Lin, Yi-Chun 
700 1 |a Cheng, Chien-Yu 
700 1 |a Cheng, Shu-Hsing 
700 1 |a Huang, Yhu-Chering 
700 1 |a Lin, Tzou-Yien 
700 1 |a Ma, Che 
700 1 |a Huo, Jiandong 
700 1 |a Carrique, Loic 
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700 1 |a Ruza, Reinis R 
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700 1 |a Buttigieg, Karen R 
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700 1 |a Screaton, Gavin R 
700 1 |a Carroll, Miles W 
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700 1 |a Naismith, James H 
700 1 |a Townsend, Alain R 
700 1 |a Fry, Elizabeth E 
700 1 |a Zhao, Yuguang 
700 1 |a Ren, Jingshan 
700 1 |a Stuart, David I 
700 1 |a Huang, Kuan-Ying A 
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