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Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient
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 Shah; Tiong Kit Tan; Pramila Rijal; Robert F Donat; Kerry Godwin; Karen Buttigieg; Julia Tree; Julika Radecke; Neil G Paterson; Piyasa Supasa; Juthathip Mongkolsapaya; Gavin R Screaton; Miles W Carroll; Javier G Jaramillo; MIchael Knight; William S James; Raymond J Owens; James H Naismith; Alain Townsend; Elizabeth E Fry; Yuguang Zhao; Jingshan Ren; David I Stuart; Kuan-Ying A Huang.
Afiliación
  • Daming Zhou; University of Oxford
  • Helen M E Duyvesteyn; University of Oxford
  • Cheng-Pin Chen; Taoyuan General Hospital
  • Chung-Guei Huang; Chang Gung University
  • Ting-Hua Chen; Genomics Research Center, Academia Sinica, Taipei
  • Shin-Ru Shih; Chang Gung University
  • Yi-Chun Lin; Taoyuan General Hospital
  • Chien-Yu Cheng; Taoyuan General Hospital
  • Shu-Hsing Cheng; Taoyuan General Hospital
  • Yhu-Chering Huang; Chang Gung Memorial Hospital
  • Tzou-Yien Lin; Chang Gung Memorial Hospital
  • Che Ma; Genomics Research Center, Academia Sinica, Taipei
  • Jiandong Huo; University of Oxford
  • Loic Carrique; University of Oxford
  • Tomas Malinauskas; University of Oxford
  • Reinis R Ruza; University of Oxford
  • Pranav Shah; University of Oxford
  • Tiong Kit Tan; University of Oxford
  • Pramila Rijal; University of Oxford
  • Robert F Donat; University of Oxford
  • Kerry Godwin; PHE, Porton Down
  • Karen Buttigieg; PHE Porton Down
  • Julia Tree; PHE Porton Down
  • Julika Radecke; Diamond Light Source
  • Neil G Paterson; Diamond Light Source
  • Piyasa Supasa; University of Oxford
  • Juthathip Mongkolsapaya; University of Oxford
  • Gavin R Screaton; University of Oxford
  • Miles W Carroll; PHE Porton Down
  • Javier G Jaramillo; University of Oxford
  • MIchael Knight; University of Oxford
  • William S James; University of Oxford
  • Raymond J Owens; University of Oxford
  • James H Naismith; University of Oxford
  • Alain Townsend; University of Oxford
  • Elizabeth E Fry; University of Oxford
  • Yuguang Zhao; University of Oxford
  • Jingshan Ren; University of Oxford
  • David I Stuart; University of Oxford
  • Kuan-Ying A Huang; Chang Gung University
Preprint en En | PREPRINT-BIORXIV | ID: ppbiorxiv-148387
Artículo de revista
Un artículo publicado en revista científica está disponible y probablemente es basado en este preprint, por medio del reconocimiento de similitud realizado por una máquina. La confirmación humana aún está pendiente.
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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 (KD of 2 nM) the receptor binding domain (RBD) of the viral Spike glycoprotein and a 2.6[A] 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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Texto completo: 1 Colección: 09-preprints Base de datos: PREPRINT-BIORXIV Tipo de estudio: Rct Idioma: En Año: 2020 Tipo del documento: Preprint
Texto completo: 1 Colección: 09-preprints Base de datos: PREPRINT-BIORXIV Tipo de estudio: Rct Idioma: En Año: 2020 Tipo del documento: Preprint