ArticleViruses2018
The RNA Capping Enzyme Domain in Protein A is Essential for Flock House Virus Replication.
Article in Viruses, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Genetic complementation reveals structure-function links in nodavirus RNA replication complex crowns.PLoS pathogens · 2026Article
- Nodavirus protein A's interdomain elbow controls RNA replication organelle formation and function.Nucleic acids research · 2026Article
- Positive-strand RNA virus genome replication organelles: structure, assembly, control.Trends in genetics : TIG · 2024Review
- 1mΨ influences the performance of various positive-stranded RNA virus-based replicons.Scientific reports · 2024Article
- Nodavirus RNA replication crown architecture reveals proto-crown precursor and viral protein A conformational switching.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Multifunctional Protein A Is the Only Viral Protein Required for Nodavirus RNA Replication Crown Formation.Viruses · 2022Article
- Cryo-electron microscopy of nodavirus RNA replication organelles illuminates positive-strand RNA virus genome replication.Current opinion in virology · 2021Review
- Short and Sweet: Viral 5`-UTR as a Canonical and Non-Canonical Translation Initiation Switch.Journal of cellular immunology · 2021Article
- Subdomain cryo-EM structure of nodaviral replication protein A crown complex provides mechanistic insights into RNA genome replication.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Design and Use of Chikungunya Virus Replication Templates Utilizing Mammalian and Mosquito RNA Polymerase I-Mediated Transcription.Journal of virology · 2019Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
The nodavirus flock house virus (FHV) and the alphavirus Semliki Forest virus (SFV) show evolutionarily intriguing similarities in their replication complexes and RNA capping enzymes. In this study, we first established an efficient FHV trans-replication system in mammalian cells, which disjoins protein expression from viral RNA synthesis. Following transfection, FHV replicase protein A was associated with mitochondria, whose outer surface displayed pouch-like invaginations with a 'neck' structure opening towards the cytoplasm. In mitochondrial pellets from transfected cells, high-level synthesis of both genomic and subgenomic RNA was detected in vitro and the newly synthesized RNA was of positive polarity. Secondly, we initiated the study of the putative RNA capping enzyme domain in protein A by mutating the conserved amino acids H93, R100, D141, and W215. RNA replication was abolished for all mutants inside cells and in vitro except for W215A, which showed reduced replication. Transfection of capped RNA template did not rescue the replication activity of the mutants. Comparing the efficiency of SFV and FHV trans-replication systems, the FHV system appeared to produce more RNA. Using fluorescent marker proteins, we demonstrated that both systems could replicate in the same cell. This work may facilitate the comparative analysis of FHV and SFV replication.
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