ArticleJournal of virology2009
Insertion of enhanced green fluorescent protein in a hinge region of vesicular stomatitis virus L polymerase protein creates a temperature-sensitive virus that displays no virion-associated polymerase activity in vitro.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed, 40 citations in OpenAlex.
- Palmitoylation of glycoproteins under low temperature enhances SVCV replication.PLoS pathogens · 2026Article
- Optical Control of Mononegavirus Gene Expression and Replication.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Labeling Ebola Virus with a Self-Splicing Fluorescent Reporter.Microorganisms · 2022Article
- Article
- Locations and in situ structure of the polymerase complex inside the virion of vesicular stomatitis virus.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Rice Stripe Mosaic Disease: Characteristics and Control Strategies.Frontiers in microbiology · 2021Review
- Stable Attenuation of Human Respiratory Syncytial Virus for Live Vaccines by Deletion and Insertion of Amino Acids in the Hinge Region between the mRNA Capping and Methyltransferase Domains of the Large Polymerase Protein.Journal of virology · 2020Article
- A comprehensive global perspective on phylogenomics and evolutionary dynamics of Small ruminant morbillivirus.Scientific reports · 2020Article
- Article
- Specificity of Plant Rhabdovirus Cell-to-Cell Movement.Journal of virology · 2019Article
- Phase Transitions Drive the Formation of Vesicular Stomatitis Virus Replication Compartments.mBio · 2018Article
- Molecular Function Analysis of Rabies Virus RNA Polymerase L Protein by Using an L Gene-Deficient Virus.Journal of virology · 2017Article
- Organization, Function, and Therapeutic Targeting of the Morbillivirus RNA-Dependent RNA Polymerase Complex.Viruses · 2016Review
- HSP90 Chaperoning in Addition to Phosphoprotein Required for Folding but Not for Supporting Enzymatic Activities of Measles and Nipah Virus L Polymerases.Journal of virology · 2016Article
- A Druggable Pocket at the Nucleocapsid/Phosphoprotein Interaction Site of Human Respiratory Syncytial Virus.Journal of virology · 2015Article
- Interactome analysis of the human respiratory syncytial virus RNA polymerase complex identifies protein chaperones as important cofactors that promote L-protein stability and RNA synthesis.Journal of virology · 2015Article
- Putative domain-domain interactions in the vesicular stomatitis virus L polymerase protein appendage region.Journal of virology · 2014Article
- A single amino acid mutation (I1012F) of the RNA polymerase of marine viral hemorrhagic septicemia virus changes in vitro virulence to rainbow trout gill epithelial cells.Journal of virology · 2014Article
- Development and application of reporter-expressing mononegaviruses: current challenges and perspectives.Antiviral research · 2014Review
- Asymmetric packaging of polymerases within vesicular stomatitis virus.Biochemical and biophysical research communications · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The RNA-dependent RNA polymerase of viruses belonging to the order Mononegavirales is part of a large multifunctional L protein that also catalyzes viral mRNA capping and cap methylation. The L protein of this diverse group of agents displays six blocks of conserved sequences. The precise relationship between these conserved regions and individual functions is largely unknown, except for "domain" VI that clearly encodes a viral mRNA cap methylase. The L protein of morbilliviruses (family Paramyxoviridae) was reported to tolerate insertion of the enhanced green fluorescent protein (EGFP) in a region just upstream of domain VI. Recombinant viruses with this insertion grow well in cell culture but are highly attenuated in animal hosts. We show here that the L protein of vesicular stomatitis virus (VSV), the prototype of the Rhabdoviridae family, also tolerates insertion of EGFP at a similar site. The modified protein (L(EGFP)) and the resultant recombinant virus both demonstrated a sharp temperature-sensitive phenotype for polymerase activity, with reduced activity at 37 degrees C and no activity at 37.5 degrees C. Neither translation nor methylation of mutant virus transcripts was affected at 37 degrees C. Curiously, mutant virus grown at permissive temperature contained about threefold-less L protein than the wild-type virus did and displayed no virion-associated polymerase activity in vitro. These findings support the notion that a flexible "hinge" region separates the cap methylase domain of L proteins from upstream functions and open up a number of avenues for studies of L-protein function in the more-tractable VSV model system.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.