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

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.

SEEK ID: https://fairdomhub.org/publications/472

DOI: 10.1126/science.abb2507

Projects: COVID-19 Disease Map

Publication type: Journal

Journal: Science

Citation: Science 367(6483):1260-1263

Date Published: 12th Mar 2020

URL: https://www.sciencemag.org/lookup/doi/10.1126/science.abb2507

Registered Mode: imported from a bibtex file

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

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Citation
Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020). Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. In Science (Vol. 367, Issue 6483, pp. 1260–1263). American Association for the Advancement of Science (AAAS). https://doi.org/10.1126/science.abb2507
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Created: 8th Apr 2020 at 22:13

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