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In situ structures of the segmented genome and RNA polymerase complex inside a dsRNA virus
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In situ structures of the segmented genome and RNA polymerase complex inside a dsRNA virus
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Journal Article
In situ structures of the segmented genome and RNA polymerase complex inside a dsRNA virus
2015
Overview
This study visualizes the interior of a dsRNA virus using cryo-electron microscopy, revealing the organization of the genome of cytoplasmic polyhedrosis virus together with its transcriptional enzyme complex in both quiescent and transcribing states.
Genome packing in a dsRNA virus
Genome packaging in double-stranded RNA viruses is poorly understood. Using direct electron-counting cryoelectron microscopy and asymmetric reconstruction, Hong Zhou and colleagues visualize
in situ
structures of the genome of insect cytoplasmic polyhedrosis virus (CPV) in quiescent and transcribing states. The structures reveal that each CPV capsid contains ten segmented dsRNAs, organized with ten transcriptional enzyme complexes in a specific, non-symmetric manner, with each dsRNA segment attached directly to a transcriptional enzyme complex.
Viruses in the
Reoviridae
, like the triple-shelled human rotavirus and the single-shelled insect cytoplasmic polyhedrosis virus (CPV), all package a genome of segmented double-stranded RNAs (dsRNAs) inside the viral capsid and carry out endogenous messenger RNA synthesis through a transcriptional enzyme complex (TEC)
1
. By direct electron-counting cryoelectron microscopy and asymmetric reconstruction, we have determined the organization of the dsRNA genome inside quiescent CPV (q-CPV) and the
in situ
atomic structures of TEC within CPV in both quiescent and transcribing (t-CPV) states. We show that the ten segmented dsRNAs in CPV are organized with ten TECs in a specific, non-symmetric manner, with each dsRNA segment attached directly to a TEC. The TEC consists of two extensively interacting subunits: an RNA-dependent RNA polymerase (RdRP) and an NTPase VP4. We find that the bracelet domain of RdRP undergoes marked conformational change when q-CPV is converted to t-CPV, leading to formation of the RNA template entry channel and access to the polymerase active site. An amino-terminal helix from each of two subunits of the capsid shell protein (CSP) interacts with VP4 and RdRP. These findings establish the link between sensing of environmental cues by the external proteins and activation of endogenous RNA transcription by the TEC inside the virus.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Capsid Proteins - metabolism
/ Capsid Proteins - ultrastructure
/ Enzymes
/ Genomes
/ Humanities and Social Sciences
/ Kinases
/ letter
/ Multienzyme Complexes - chemistry
/ Multienzyme Complexes - metabolism
/ Multienzyme Complexes - ultrastructure
/ Nucleoside-Triphosphatase - metabolism
/ Nucleoside-Triphosphatase - ultrastructure
/ Protein Subunits - chemistry
/ Protein Subunits - metabolism
/ Proteins
/ RNA
/ RNA Replicase - ultrastructure
/ RNA, Double-Stranded - genetics
/ RNA, Double-Stranded - ultrastructure
/ RNA, Messenger - biosynthesis
/ RNA, Messenger - ultrastructure
/ Science
/ Viruses
