Your browser doesn't support javascript.
Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient.
Zhou, Daming; 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.
  • Zhou D; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.
  • Duyvesteyn HME; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.
  • Chen CP; Department of Infectious Diseases, Taoyuan General Hospital, Ministry of Health and Welfare, Taoyuan, and National Yang-Ming University, Taipei, Taiwan.
  • Huang CG; Research Center for Emerging Viral Infections, College of Medicine, Chang Gung University, Taoyuan, Taiwan.
  • Chen TH; Department of Laboratory Medicine, Chang Gung Memorial Hospital, Taoyuan, Taiwan.
  • Shih SR; Genomics Research Center, Academia Sinica, Taipei, Taiwan.
  • Lin YC; Research Center for Emerging Viral Infections, College of Medicine, Chang Gung University, Taoyuan, Taiwan.
  • Cheng CY; Department of Laboratory Medicine, Chang Gung Memorial Hospital, Taoyuan, Taiwan.
  • Cheng SH; Department of Infectious Diseases, Taoyuan General Hospital, Ministry of Health and Welfare, Taoyuan, and Taipei Medical University, Taipei, Taiwan.
  • Huang YC; Department of Infectious Diseases, Taoyuan General Hospital, Ministry of Health and Welfare, Taoyuan, and National Yang-Ming University, Taipei, Taiwan.
  • Lin TY; Department of Infectious Diseases, Taoyuan General Hospital, Ministry of Health and Welfare, Taoyuan, and Taipei Medical University, Taipei, Taiwan.
  • Ma C; Division of Pediatric Infectious Diseases, Department of Pediatrics, Chang Gung Memorial Hospital, Taoyuan, Taiwan.
  • Huo J; Division of Pediatric Infectious Diseases, Department of Pediatrics, Chang Gung Memorial Hospital, Taoyuan, Taiwan.
  • Carrique L; Genomics Research Center, Academia Sinica, Taipei, Taiwan.
  • Malinauskas T; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.
  • Ruza RR; The Rosalind Franklin Institute, Harwell Campus, Didcot, UK.
  • Shah PNM; Protein Production UK, Research Complex at Harwell, Harwell Science & Innovation Campus, Didcot, UK.
  • Tan TK; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.
  • Rijal P; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.
  • Donat RF; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.
  • Godwin K; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.
  • Buttigieg KR; MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, UK.
  • Tree JA; MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, UK.
  • Radecke J; Centre for Translational Immunology, Chinese Academy of Medical Sciences Oxford Institute, University of Oxford, Oxford, UK.
  • Paterson NG; MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, UK.
  • Supasa P; National Infection Service, Public Health England, Porton Down, Salisbury, UK.
  • Mongkolsapaya J; National Infection Service, Public Health England, Porton Down, Salisbury, UK.
  • Screaton GR; National Infection Service, Public Health England, Porton Down, Salisbury, UK.
  • Carroll MW; Diamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
  • Gilbert-Jaramillo J; Diamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
  • Knight ML; Nuffield Department of Medicine, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK.
  • James W; Nuffield Department of Medicine, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK.
  • Owens RJ; Dengue Hemorrhagic Fever Research Unit, Office for Research and Development, Faculty of Medicine, Siriraj Hospital, Mahidol University, Bangkok, Thailand.
  • Naismith JH; Nuffield Department of Medicine, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK.
  • Townsend AR; National Infection Service, Public Health England, Porton Down, Salisbury, UK.
  • Fry EE; Nuffield Department of Medicine, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK.
  • Zhao Y; William Dunn School of Pathology, University of Oxford, Oxford, UK.
  • Ren J; William Dunn School of Pathology, University of Oxford, Oxford, UK.
  • Stuart DI; William Dunn School of Pathology, University of Oxford, Oxford, UK.
  • Huang KA; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.
Nat Struct Mol Biol ; 27(10): 950-958, 2020 10.
Article in English | MEDLINE | ID: covidwho-691341
Preprint
This scientific journal article is probably based on a previously available preprint. It has been identified through a machine matching algorithm, human confirmation is still pending.
See preprint
ABSTRACT
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.
Subject(s)

Full text: Available Collection: International databases Database: MEDLINE Main subject: Pneumonia, Viral / Coronavirus Infections / Spike Glycoprotein, Coronavirus / Betacoronavirus / Antibodies, Viral Type of study: Randomized controlled trials Limits: Adult / Animals / Humans / Male Language: English Journal: Nat Struct Mol Biol Journal subject: Molecular Biology Year: 2020 Document Type: Article Affiliation country: S41594-020-0480-y

Similar

MEDLINE

...
LILACS

LIS


Full text: Available Collection: International databases Database: MEDLINE Main subject: Pneumonia, Viral / Coronavirus Infections / Spike Glycoprotein, Coronavirus / Betacoronavirus / Antibodies, Viral Type of study: Randomized controlled trials Limits: Adult / Animals / Humans / Male Language: English Journal: Nat Struct Mol Biol Journal subject: Molecular Biology Year: 2020 Document Type: Article Affiliation country: S41594-020-0480-y