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

  1. Daming Zhou
  2. Helen ME Duyvesteyn
  3. Cheng-Pin Chen
  4. Chung-Guei Huang
  5. Ting-Hua Chen
  6. Shin-Ru Shih
  7. Yi-Chun Lin
  8. Chien-Yu Cheng
  9. Shu-Hsing Cheng
  10. Yhu-Chering Huang
  11. Tzou-Yien Lin
  12. Che Ma
  13. Jiandong Huo
  14. Loic Carrique
  15. Tomas Malinauskas
  16. Reinis R Ruza
  17. Pranav NM Shah
  18. Tiong Kit Tan
  19. Pramila Rijal
  20. Robert F. Donat
  21. Kerry Godwin
  22. Karen Buttigieg
  23. Julia Tree
  24. Julika Radecke
  25. Neil G Paterson
  26. Piyasa Supasa
  27. Juthathip Mongkolsapaya
  28. Gavin R Screaton
  29. Miles W. Carroll
  30. Javier G. Jaramillo
  31. Michael Knight
  32. William James
  33. Raymond J Owens
  34. James H. Naismith
  35. Alain Townsend
  36. Elizabeth E Fry
  37. Yuguang Zhao
  38. Jingshan Ren
  39. David I Stuart
  40. Kuan-Ying A. Huang
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Abstract

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 (KDof 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.

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