RNA Binding Sensitivity of Nonstructural Protein 8 Revealed by Small-Angle Neutron Scattering and Alphafold2 Prediction

The flexible structure enables nonstructural protein 8 (nsp8) to respond quickly to environmental changes, which are essential for RNA replication and transcription of SARS-CoV-2. In this work, small-angle neutron scattering and AlphaFold2 prediction were applied to characterize the structural change of SARS-CoV-2 nsp8 dimers and tetramers. The results demonstrated that the nsp8 tetramer with a more exposed core domain shows a low thermal stability. The exposed core domain increases its sensitivity to RNA and adapts its structure to interact with RNA. Our work reveals the structural difference between the two forms of SARS-CoV-2 nsp8s in the RNA synthesis process, which partly elucidates the molecular mechanism behind RNA replication of the RNA virus.

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Publication Details

Journal
ACS Nano
Published
2025-10-17
DOI
https://doi.org/10.1021/acsnano.4c16790
Primary Topic
Enzyme Structure and Function
Type
article
Field-Weighted Citation Impact
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article

RNA Binding Sensitivity of Nonstructural Protein 8 Revealed by Small-Angle Neutron Scattering and Alphafold2 Prediction

Jun Fan, Changli Ma, Taisen Zuo, Xin Jiang et al.
ACS Nano
Enzyme Structure and Function
article

RNA Binding Sensitivity of Nonstructural Protein 8 Revealed by Small-Angle Neutron Scattering and Alphafold2 Prediction

Jun Fan, Changli Ma, Taisen Zuo, Xin Jiang, Jinxin Xu, He Cheng, Zhenyu Liao, Yubin Ke, Jinkui Zhao, Howard Wang, Hanqiu Jiang, Xiang-qiang Chu, Na Wang, Jinsong Liu
article en

Abstract

The flexible structure enables nonstructural protein 8 (nsp8) to respond quickly to environmental changes, which are essential for RNA replication and transcription of SARS-CoV-2. In this work, small-angle neutron scattering and AlphaFold2 prediction were applied to characterize the structural change of SARS-CoV-2 nsp8 dimers and tetramers. The results demonstrated that the nsp8 tetramer with a more exposed core domain shows a low thermal stability. The exposed core domain increases its sensitivity to RNA and adapts its structure to interact with RNA. Our work reveals the structural difference between the two forms of SARS-CoV-2 nsp8s in the RNA synthesis process, which partly elucidates the molecular mechanism behind RNA replication of the RNA virus.

ACS NanoVol. 19(42)
City University of Hong Kong (HK), Chinese Academy of Sciences (CN), Guangzhou Institutes of Biomedicine and Health (CN), BC Platforms (Finland) (FI), City University of Hong Kong, Shenzhen Research Institute (CN), China Spallation Neutron Source (CN), Guangdong-Hongkong-Macau Joint Laboratory of Collaborative Innovation for Environmental Quality (CN), Tianjin International Joint Academy of Biomedicine (CN), Songshan Lake Materials Laboratory (CN), FZU ‒ Institute of Physics of the Academy of Sciences of the Czech Republic (CZ), Biocom (US), State Key Laboratory of Respiratory Disease (CN), Institute of Physics (CN), National Laboratory for Superconductivity (CN), Spallation Neutron Source
Openalex Percentile: Top 77%
Enzyme Structure and Function
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