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Molecular architecture of the SARS-CoV-2 virus

By Hangping Yao, Yutong Song, Yong Chen, Nanping Wu, Jialu Xu, Chujie Sun, Jiaxing Zhang, Tianhao Weng, Zheyuan Zhang, Zhigang Wu, Linfang Cheng, Danrong Shi, Xiangyun Lu, Jianlin Lei, Max Crispin, Yigong Shi, Lanjuan Li, Sai Li

Posted 09 Jul 2020
bioRxiv DOI: 10.1101/2020.07.08.192104 (published DOI: 10.1016/j.cell.2020.09.018)

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an enveloped virus responsible for the COVID-19 pandemic. Despite recent advances in the structural elucidation of SARS-CoV-2 proteins and the complexes of the spike (S) proteins with the cellular receptor ACE2 or neutralizing antibodies, detailed architecture of the intact virus remains to be unveiled. Here we report the molecular assembly of the authentic SARS-CoV-2 virus using cryo-electron tomography (cryo-ET) and subtomogram averaging (STA). Native structures of the S proteins in both pre- and postfusion conformations were determined to average resolutions of 8.7-11 Å. Compositions of the N-linked glycans from the native spikes were analyzed by mass-spectrometry, which revealed highly similar overall processing states of the native glycans to that of the recombinant glycoprotein glycans. The native conformation of the ribonucleoproteins (RNP) and its higher-order assemblies were revealed. Overall, these characterizations have revealed the architecture of the SARS-CoV-2 virus in unprecedented detail, and shed lights on how the virus packs its ∼30 kb long single-segmented RNA in the ∼80 nm diameter lumen. ### Competing Interest Statement The authors have declared no competing interest.

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