H. Yao, Y. Song, Yong Chen, N. Wu, Jialu Xu, Chujie Sun, Jiaxing Zhang, Tianhao Weng, Zheyuan Zhang, Z. Wu, L. Cheng, Danrong Shi, Xiangyun Lu, Jianlin Lei, M. Crispin, Yigong Shi, Lanjuan Li, Sai Li
Cell, 2020
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, 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 exceptional detail, and shed lights on how the virus packs its ∼30 kb long single-segmented RNA in the ∼80 nm diameter lumen.
Cited by 127 publications.
Field of study: Biology