Molecular Architecture of the SARS-CoV-2 Virus
| Autor: | Jiaxing Zhang, Sai Li, Danrong Shi, Nanping Wu, Yigong Shi, Yong Chen, Max Crispin, Xiangyun Lu, Jianlin Lei, Tianhao Weng, Zhigang Wu, Hangping Yao, Linfang Cheng, Lanjuan Li, Zheyuan Zhang, Chujie Sun, Yutong Song, Jialu Xu |
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| Rok vydání: | 2020 |
| Předmět: |
Models
Molecular Cryo-electron microscopy Protein Conformation viruses coronavirus medicine.disease_cause Mass Spectrometry 0302 clinical medicine Pandemic Chlorocebus aethiops Native state spike glycoprotein Coronavirus Ribonucleoprotein 0303 health sciences biology Chemistry Cellular receptor cryo-electron tomography Cell biology Biochemistry Cryo-electron tomography Antibody Glycan Virus Cultivation Coronavirus disease 2019 (COVID-19) Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Context (language use) Computational biology Article ribonucleoprotein General Biochemistry Genetics and Molecular Biology Virus 03 medical and health sciences Betacoronavirus Viral Proteins Viral envelope medicine subtomogram averaging Animals Humans Vero Cells 030304 developmental biology SARS-CoV-2 Virus Assembly Cryoelectron Microscopy RNA biology.protein cryo-EM virus structure 030217 neurology & neurosurgery |
| Zdroj: | Cell |
| ISSN: | 1097-4172 |
| Popis: | 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. Graphical Abstract Highlights • Molecular architecture of the authentic SARS-CoV-2 virus • Native structures of S in RBD down, one RBD up, and postfusion conformations • Compositions of the glycans from the native S are characterized by mass spectrometry • Structure and assembly of the RNPs are revealed in situ Combined imaging analyses of 2,294 intact virions from the authentic SARS-CoV-2 virus resolve the S protein in pre- and postfusion conformations and characterize the molecular architecture of SARS-CoV-2 at high resolution. |
| Databáze: | OpenAIRE |
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