Asymmetric Reconstruction of the Aquareovirus Core at Near-Atomic Resolution and Mechanism of Transcription Initiation. Stevens, A., Cui, Y., Shivakoti, S., & Zhou, Z H. Protein & Cell, 14(7):546–550, July, 2023. doi abstract bibtex Dear Editor,Aquareovirus (ARV, Reoviridae) causes hemorrhagic disease in the economically important golden shiner and grass carp of America and China, respectively (Nason et al., 2000; Fang et al., 2005). Reoviridae members are characterized by endogenous transcription of their multipartite genomes within capsids of 1–3 layers and are further classified based on the presence (Spinareovirinae subfamily, 9 genera) or absence (Sedoreovirinae subfamily, 6 genera) of mRNA-capping turrets along the innermost layer (King et al., 2012). The innermost layer of reoviruses is always an icosahedral, T = 2*, inner capsid particle (ICP) or core, which is transcriptionally competent (Farsetta et al., 2000). Among turreted reoviruses, cytoplasmic polyhedrosis virus (CPV) has a single-layered capsid, which is equivalent to the ICP within double- or triple-layered reoviruses (Hill et al., 1999; Zhang et al., 1999; Yu et al., 2011). This simple structural organization makes CPV an attractive model to study turreted reoviruses, but renders it inadequate to describe possible impacts of shedding the external layers from the numerous, multi-layered Spinareovirinae members (Zhang et al., 2022). Here we used a sequential symmetry expansion and relaxation approach to resolve the first asymmetric reconstruction of the ARV ICP by cryoEM to 3.3 Å (Fig. S2). Comparison with existing ARV virion and infectious subvirion particle (ISVP) structures (Ding et al., 2018) reveals expansion of the ICP and concomitant conformational changes to the transcription related proteins.
@article{stevensAsymmetricReconstructionAquareovirus2023,
title = {Asymmetric Reconstruction of the Aquareovirus Core at Near-Atomic Resolution and Mechanism of Transcription Initiation},
author = {Stevens, Alexander and Cui, Yanxiang and Shivakoti, Sakar and Zhou, Z Hong},
year = {2023},
month = jul,
journal = {Protein \& Cell},
volume = {14},
number = {7},
pages = {546--550},
issn = {1674-800X},
doi = {10.1093/procel/pwad002},
urldate = {2024-06-13},
abstract = {Dear Editor,Aquareovirus (ARV, Reoviridae) causes hemorrhagic disease in the economically important golden shiner and grass carp of America and China, respectively (Nason et al., 2000; Fang et al., 2005). Reoviridae members are characterized by endogenous transcription of their multipartite genomes within capsids of 1--3 layers and are further classified based on the presence (Spinareovirinae subfamily, 9 genera) or absence (Sedoreovirinae subfamily, 6 genera) of mRNA-capping turrets along the innermost layer (King et al., 2012). The innermost layer of reoviruses is always an icosahedral, T = 2*, inner capsid particle (ICP) or core, which is transcriptionally competent (Farsetta et al., 2000). Among turreted reoviruses, cytoplasmic polyhedrosis virus (CPV) has a single-layered capsid, which is equivalent to the ICP within double- or triple-layered reoviruses (Hill et al., 1999; Zhang et al., 1999; Yu et al., 2011). This simple structural organization makes CPV an attractive model to study turreted reoviruses, but renders it inadequate to describe possible impacts of shedding the external layers from the numerous, multi-layered Spinareovirinae members (Zhang et al., 2022). Here we used a sequential symmetry expansion and relaxation approach to resolve the first asymmetric reconstruction of the ARV ICP by cryoEM to 3.3 {\AA} (Fig. S2). Comparison with existing ARV virion and infectious subvirion particle (ISVP) structures (Ding et al., 2018) reveals expansion of the ICP and concomitant conformational changes to the transcription related proteins.},
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}
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