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Preparation of High-Temperature Sample Grids for Cryo-EM
Published on: July 26, 2021
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Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structure.
Lihong Chen1,2,3, Ming Wang2, Dongjie Zhu1,4
1National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 100101, Beijing, People's Republic of China.
Nature Communications
|December 16, 2018
Summary
Researchers reveal the high-resolution cryo-EM structure of Sindbis virus, a significant alphavirus. This breakthrough identifies key conserved residues and a novel pocket, aiding in understanding virus assembly and informing drug and vaccine design.
Area of Science:
- Virology
- Structural Biology
- Cryo-Electron Microscopy
Background:
- Alphaviruses are enveloped RNA viruses, including significant human pathogens.
- High-resolution structures of alphaviruses are limited due to particle heterogeneity.
Purpose of the Study:
- To determine the high-resolution cryo-electron microscopy (cryo-EM) structure of Sindbis virus.
- To identify conserved residues and structural features critical for alphavirus life cycle and assembly.
Main Methods:
- Utilized a block-based reconstruction method in cryo-EM to address particle heterogeneity.
- Analyzed the 3.5 Å structure of Sindbis virus.
Main Results:
- Provided a 3.5 Å cryo-EM structure of Sindbis virus, overcoming heterogeneity challenges.
- Identified conserved residues crucial for the virus life cycle.
- Discovered a novel hydrophobic pocket in the E2 protein's subdomain D, stabilized by an unknown factor near the viral membrane.
Conclusions:
- The identified pocket strengthens E1/E2 heterodimer interactions, potentially facilitating virus assembly.
- Structural insights into Sindbis virus can guide the development of novel antiviral drugs and vaccines.
- This study advances the structural understanding of alphaviruses.
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