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

Corresponding author: Jason S. McLellan

Affiliations: Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

Publication date: this article was published online on March 13, 2020

DOI: 10.1126/science.abb2507

Highlights

The researchers 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. They also provide biophysical and structural evidence 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. Additionally, they tested three 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.

Nomination Reasons

The authors determined the structure of 2019-nCoV S, which should support precision vaccine design and the discovery of antiviral therapeutics, accelerating medical countermeasure development.

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