ArticlePLoS pathogens2016
Initiation of RNA Polymerization and Polymerase Encapsidation by a Small dsRNA Virus.
Article in PLoS pathogens, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
26 citing papers in PubMed, 47 citations in OpenAlex.
- Utilization of Bacteriophage phi6 for the Production of High-Quality Double-Stranded RNA Molecules.Viruses · 2024Review
- Viral pathogen detection in U.S. game-farm mallard (Frontiers in veterinary science · 2024Article
- Capsid structure of a fungal dsRNA megabirnavirus reveals its previously unidentified surface architecture.PLoS pathogens · 2023Article
- The giant mimivirus 1.2 Mb genome is elegantly organized into a 30-nm diameter helical protein shield.eLife · 2022Article
- Genetic diversity, frequency and concurrent infections of picobirnaviruses in diarrhoeic calves in Turkey.Tropical animal health and production · 2022Article
- RdRp (RNA-dependent RNA polymerase): A key target providing anti-virals for the management of various viral diseases.Journal of molecular structure · 2022Review
- Emergence of a Distinct Picobirnavirus Genotype Circulating in Patients Hospitalized with Acute Respiratory Illness.Viruses · 2021Article
- SARS-COV-2, infection, transmission, transcription, translation, proteins, and treatment: A review.International journal of biological macromolecules · 2021Review
- RdRp or RT, That is the Question.Molecular biology and evolution · 2021Article
- RNA-Dependent RNA Polymerase from Heterobasidion RNA Virus 6 Is an Active Replicase In Vitro.Viruses · 2021Article
- Proof of Concept of the Yadokari Nature: a Capsidless Replicase-Encoding but Replication-Dependent Positive-Sense Single-Stranded RNA Virus Hosted by an Unrelated Double-Stranded RNA Virus.Journal of virology · 2021Article
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- Article
- Molecular epidemiology and phylogenetic analysis of bovine picobirnaviruses causing calf diarrhea, in Iran.Veterinary research forum : an international quarterly journal · 2021Article
- Cryo-electron Microscopy Structure, Assembly, and Mechanics Show Morphogenesis and Evolution of Human Picobirnavirus.Journal of virology · 2020Article
- Arrangement of the Polymerase Complexes inside a Nine-Segmented dsRNA Virus.Structure (London, England : 1993) · 2020Article
- Article
- The True Host/s of Picobirnaviruses.Frontiers in veterinary science · 2020Review
- In situ structures of rotavirus polymerase in action and mechanism of mRNA transcription and release.Nature communications · 2019Article
- The 13th International Double-Stranded RNA Virus Symposium, Houffalize, Belgium, 24 to 28 September 2018.Journal of virology · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
During the replication cycle of double-stranded (ds) RNA viruses, the viral RNA-dependent RNA polymerase (RdRP) replicates and transcribes the viral genome from within the viral capsid. How the RdRP molecules are packaged within the virion and how they function within the confines of an intact capsid are intriguing questions with answers that most likely vary across the different dsRNA virus families. In this study, we have determined a 2.4 Å resolution structure of an RdRP from the human picobirnavirus (hPBV). In addition to the conserved polymerase fold, the hPBV RdRP possesses a highly flexible 24 amino acid loop structure located near the C-terminus of the protein that is inserted into its active site. In vitro RNA polymerization assays and site-directed mutagenesis showed that: (1) the hPBV RdRP is fully active using both ssRNA and dsRNA templates; (2) the insertion loop likely functions as an assembly platform for the priming nucleotide to allow de novo initiation; (3) RNA transcription by the hPBV RdRP proceeds in a semi-conservative manner; and (4) the preference of virus-specific RNA during transcription is dictated by the lower melting temperature associated with the terminal sequences. Co-expression of the hPBV RdRP and the capsid protein (CP) indicated that, under the conditions used, the RdRP could not be incorporated into the recombinant capsids in the absence of the viral genome. Additionally, the hPBV RdRP exhibited higher affinity towards the conserved 5'-terminal sequence of the viral RNA, suggesting that the RdRP molecules may be encapsidated through their specific binding to the viral RNAs during assembly.
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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.