Molecular Architecture of the SARS-CoV-2 Virus
Author(s) -
HangPing Yao,
Yutong Song,
Yong Chen,
Nanping Wu,
Jialu Xu,
Chujie Sun,
Jiaxing Zhang,
Tian-Hao Weng,
Zheyuan Zhang,
Zhigang Wu,
Linfang Cheng,
Danrong Shi,
Xiangyun Lu,
Jianlin Lei,
Max Crispin,
Yigong Shi,
Lanjuan Li,
Sai Li
Publication year - 2020
Publication title -
cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 26.304
H-Index - 776
eISSN - 1097-4172
pISSN - 0092-8674
DOI - 10.1016/j.cell.2020.09.018
Subject(s) - biology , virus , glycan , virology , ribonucleoprotein , recombinant dna , glycoprotein , rna , viral envelope , covid-19 , microbiology and biotechnology , biochemistry , gene , medicine , disease , pathology , infectious disease (medical specialty)
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 Å. 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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom