Статья

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

Daniel WrappDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USANianshuang WangDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USAKizzmekia S. CorbettVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USAJory A. GoldsmithDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USAChing‐Lin HsiehDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USAOlubukola M. AbionaVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USABarney S. GrahamVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USAJason S. McLellanDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA

2020en

ABI

Аннотация

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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Идентификаторы

DOI: 10.1126/science.abb2507

Цитирования и источники

Цитирований: 5Использованных источников: 0

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