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Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation.
Wrapp, Daniel; Wang, Nianshuang; Corbett, Kizzmekia S; Goldsmith, Jory A; Hsieh, Ching-Lin; Abiona, Olubukola; Graham, Barney S; McLellan, Jason S.
  • Wrapp D; Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.
  • Wang N; Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.
  • Corbett KS; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
  • Goldsmith JA; Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.
  • Hsieh CL; Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.
  • Abiona O; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
  • Graham BS; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
  • McLellan JS; Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA. jmclellan@austin.utexas.edu.
Science ; 367(6483): 1260-1263, 2020 03 13.
Article in English | MEDLINE | ID: covidwho-1461
Preprint
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ABSTRACT
The outbreak of a novel coronavirus (2019-nCoV) represents a pandemic threat that has been declared a public health emergency of international concern. The CoV spike (S) glycoprotein is a key target for vaccines, therapeutic antibodies, and diagnostics. To facilitate medical countermeasure development, we determined a 3.5-angstrom-resolution cryo-electron microscopy structure of the 2019-nCoV S trimer in the prefusion conformation. The predominant state of the trimer has one of the three receptor-binding domains (RBDs) rotated up in a receptor-accessible conformation. We also provide biophysical and structural evidence that the 2019-nCoV S protein binds angiotensin-converting enzyme 2 (ACE2) with higher affinity than does severe acute respiratory syndrome (SARS)-CoV S. Additionally, we tested several published SARS-CoV RBD-specific monoclonal antibodies and found that they do not have appreciable binding to 2019-nCoV S, suggesting that antibody cross-reactivity may be limited between the two RBDs. The structure of 2019-nCoV S should enable the rapid development and evaluation of medical countermeasures to address the ongoing public health crisis.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Spike Glycoprotein, Coronavirus / Betacoronavirus Type of study: Experimental Studies / Randomized controlled trials Topics: Vaccines Language: English Journal: Science Year: 2020 Document Type: Article Affiliation country: Science.abb2507

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Spike Glycoprotein, Coronavirus / Betacoronavirus Type of study: Experimental Studies / Randomized controlled trials Topics: Vaccines Language: English Journal: Science Year: 2020 Document Type: Article Affiliation country: Science.abb2507