PT  - JOURNAL ARTICLE
AU  - Hangping Yao
AU  - Yutong Song
AU  - Yong Chen
AU  - Nanping Wu
AU  - Jialu Xu
AU  - Chujie Sun
AU  - Jiaxing Zhang
AU  - Tianhao Weng
AU  - Zheyuan Zhang
AU  - Zhigang Wu
AU  - Linfang Cheng
AU  - Danrong Shi
AU  - Xiangyun Lu
AU  - Jianlin Lei
AU  - Max Crispin
AU  - Yigong Shi
AU  - Lanjuan Li
AU  - Sai Li
TI  - Molecular architecture of the SARS-CoV-2 virus
AID  - 10.1101/2020.07.08.192104
DP  - 2020 Jan 01
TA  - bioRxiv
PG  - 2020.07.08.192104
4099  - http://biorxiv.org/content/early/2020/08/12/2020.07.08.192104.short
4100  - http://biorxiv.org/content/early/2020/08/12/2020.07.08.192104.full
AB  - 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 StatementThe authors have declared no competing interest.