Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation

Author:

Wrapp Daniel1ORCID,Wang Nianshuang1ORCID,Corbett Kizzmekia S.2ORCID,Goldsmith Jory A.1,Hsieh Ching-Lin1,Abiona Olubukola2ORCID,Graham Barney S.2ORCID,McLellan Jason S.1ORCID

Affiliation:

1. Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.

2. Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

Abstract

Structure of the nCoV trimeric spike The World Health Organization has declared the outbreak of a novel coronavirus (2019-nCoV) to be a public health emergency of international concern. The virus binds to host cells through its trimeric spike glycoprotein, making this protein a key target for potential therapies and diagnostics. Wrapp et al. determined a 3.5-angstrom-resolution structure of the 2019-nCoV trimeric spike protein by cryo–electron microscopy. Using biophysical assays, the authors show that this protein binds at least 10 times more tightly than the corresponding spike protein of severe acute respiratory syndrome (SARS)–CoV to their common host cell receptor. They also tested three antibodies known to bind to the SARS-CoV spike protein but did not detect binding to the 2019-nCoV spike protein. These studies provide valuable information to guide the development of medical counter-measures for 2019-nCoV. Science , this issue p. 1260

Funder

National Institute of Allergy and Infectious Diseases

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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