tetano
Editor, Senior Moderator
Cell
. 2020 Sep 6;S0092-8674(20)31159-4.
doi: 10.1016/j.cell.2020.09.018. Online ahead of print.
Molecular Architecture of the SARS-CoV-2 Virus
Hangping Yao[SUP] 1 [/SUP], Yutong Song[SUP] 2 [/SUP], Yong Chen[SUP] 2 [/SUP], Nanping Wu[SUP] 1 [/SUP], Jialu Xu[SUP] 3 [/SUP], Chujie Sun[SUP] 3 [/SUP], Jiaxing Zhang[SUP] 2 [/SUP], Tianhao Weng[SUP] 1 [/SUP], Zheyuan Zhang[SUP] 2 [/SUP], Zhigang Wu[SUP] 1 [/SUP], Linfang Cheng[SUP] 1 [/SUP], Danrong Shi[SUP] 1 [/SUP], Xiangyun Lu[SUP] 1 [/SUP], Jianlin Lei[SUP] 2 [/SUP], Max Crispin[SUP] 4 [/SUP], Yigong Shi[SUP] 5 [/SUP], Lanjuan Li[SUP] 6 [/SUP], Sai Li[SUP] 7 [/SUP]
Affiliations
Abstract
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, the detailed architecture of the intact virus remains to be unveiled. Here we report the molecular assembly of the authentic SARS-CoV-2 virus using cryoelectron tomography (cryo-ET) and subtomogram averaging (STA). Native structures of the S proteins in pre- and postfusion conformations were determined to average resolutions of 8.7-11 ?. Compositions of the N-linked glycans from the native spikes were analyzed by mass spectrometry, which revealed overall processing states of the native glycans highly similar to that of the recombinant glycoprotein glycans. The native conformation of the ribonucleoproteins (RNPs) and their higher-order assemblies were revealed. Overall, these characterizations revealed the architecture of the SARS-CoV-2 virus in exceptional detail and shed light on how the virus packs its ∼30-kb-long single-segmented RNA in the ∼80-nm-diameter lumen.
Keywords: SARS-CoV-2; coronavirus; cryo-EM; cryo-electron tomography; ribonucleoprotein; spike glycoprotein; subtomogram averaging; virus assembly; virus structure.
. 2020 Sep 6;S0092-8674(20)31159-4.
doi: 10.1016/j.cell.2020.09.018. Online ahead of print.
Molecular Architecture of the SARS-CoV-2 Virus
Hangping Yao[SUP] 1 [/SUP], Yutong Song[SUP] 2 [/SUP], Yong Chen[SUP] 2 [/SUP], Nanping Wu[SUP] 1 [/SUP], Jialu Xu[SUP] 3 [/SUP], Chujie Sun[SUP] 3 [/SUP], Jiaxing Zhang[SUP] 2 [/SUP], Tianhao Weng[SUP] 1 [/SUP], Zheyuan Zhang[SUP] 2 [/SUP], Zhigang Wu[SUP] 1 [/SUP], Linfang Cheng[SUP] 1 [/SUP], Danrong Shi[SUP] 1 [/SUP], Xiangyun Lu[SUP] 1 [/SUP], Jianlin Lei[SUP] 2 [/SUP], Max Crispin[SUP] 4 [/SUP], Yigong Shi[SUP] 5 [/SUP], Lanjuan Li[SUP] 6 [/SUP], Sai Li[SUP] 7 [/SUP]
Affiliations
- PMID: 32979942
- DOI: 10.1016/j.cell.2020.09.018
Abstract
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, the detailed architecture of the intact virus remains to be unveiled. Here we report the molecular assembly of the authentic SARS-CoV-2 virus using cryoelectron tomography (cryo-ET) and subtomogram averaging (STA). Native structures of the S proteins in pre- and postfusion conformations were determined to average resolutions of 8.7-11 ?. Compositions of the N-linked glycans from the native spikes were analyzed by mass spectrometry, which revealed overall processing states of the native glycans highly similar to that of the recombinant glycoprotein glycans. The native conformation of the ribonucleoproteins (RNPs) and their higher-order assemblies were revealed. Overall, these characterizations revealed the architecture of the SARS-CoV-2 virus in exceptional detail and shed light on how the virus packs its ∼30-kb-long single-segmented RNA in the ∼80-nm-diameter lumen.
Keywords: SARS-CoV-2; coronavirus; cryo-EM; cryo-electron tomography; ribonucleoprotein; spike glycoprotein; subtomogram averaging; virus assembly; virus structure.