Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient
Helen ME Duyvesteyn,
Reinis R Ruza,
Pranav N.M. Shah,
Robert F Donat,
Neil G Paterson,
Gavin R Screaton,
Miles W Carroll,
Javier G Jaramillo,
Raymond J Owens,
James H. Naismith,
Elizabeth E Fry,
David I. Stuart,
Kuan-Ying A. Huang
Posted 13 Jun 2020
bioRxiv DOI: 10.1101/2020.06.12.148387 (published DOI: 10.1038/s41594-020-0480-y)
Posted 13 Jun 2020
The COVID-19 pandemic has had unprecedented health and economic impact, but currently there are no approved therapies. We have isolated an antibody, EY6A, from a late-stage COVID-19 patient and show it neutralises SARS-CoV-2 and cross-reacts with SARS-CoV-1. EY6A Fab binds tightly (KD of 2 nM) the receptor binding domain (RBD) of the viral Spike glycoprotein and a 2.6Å crystal structure of an RBD/EY6A Fab complex identifies the highly conserved epitope, away from the ACE2 receptor binding site. Residues of this epitope are key to stabilising the pre-fusion Spike. Cryo-EM analyses of the pre-fusion Spike incubated with EY6A Fab reveal a complex of the intact trimer with three Fabs bound and two further multimeric forms comprising destabilized Spike attached to Fab. EY6A binds what is probably a major neutralising epitope, making it a candidate therapeutic for COVID-19. ### Competing Interest Statement The authors have declared no competing interest.
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