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HGNC Genes

SARS-CoV-2 proteins

ProteinS (1)


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    Cryo-EM Structure of the 2019-nCoV Spike in the Prefusion Conformation

    Authors: Daniel Wrapp; Nianshuang Wang; Kizzmekia S Corbett; Jory A Goldsmith; Ching-Lin Hsieh; Olubukola Abiona; Barney S Graham; Jason S McLellan

    doi:10.1101/2020.02.11.944462 Date: 2020-02-15 Source: bioRxiv

    The outbreak of a novel betacoronavirus (2019-nCov) represents a pandemic threat that has been declared a public health emergency of international concern. The CoV spike ( S) glycoprotein PROTEIN is a key target for urgently needed vaccines, therapeutic antibodies, and diagnostics. To facilitate medical countermeasure ( MCM HGNC) development we determined a 3.5 [A]-resolution cryo-EM 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 show biophysical and structural evidence that the 2019-nCoV S binds ACE2 HGNC with higher affinity than SARS-CoV S MESHD. Additionally we tested several published SARS-CoV RBD-specific monoclonal antibodies and found that they do not have appreciable binding to nCoV-2019 S, suggesting antibody cross-reactivity may be limited between the two virus RBDs. The atomic-resolution structure of 2019-nCoV S should enable rapid development and evaluation of MCMs to address the ongoing public health crisis.

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MeSH Disease
HGNC Genes
SARS-CoV-2 Proteins


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