ArticleJournal of virology2015
Cotranslational coat protein-mediated inhibition of potyviral RNA translation.
Article in Journal of virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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.
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Who cites it
18 citing papers in PubMed, 39 citations in OpenAlex.
- Species-specific structural adaptation of the potyviral coat protein in virions and virus-like particles.Communications biology · 2026Article
- From structural polymorphism to structural metamorphosis of the coat protein of flexuous filamentous potato virus Y.Communications chemistry · 2024Article
- Interplay of HCPro and CP in the Regulation of Potato Virus A RNA Expression and Encapsidation.Viruses · 2022Article
- Review
- Article
- The potyviral silencing suppressor HCPro recruits and employs host ARGONAUTE1 in pro-viral functions.PLoS pathogens · 2020Article
- Functional Characterization of Pepper Vein Banding Virus-Encoded Proteins and Their Interactions: Implications inViruses · 2020Review
- Article
- Dynamics of Protein Accumulation from the 3' End of Viral RNA Are Different from Those in the Rest of the Genome in Potato Virus A Infection.Journal of virology · 2019Article
- Structural basis for the multitasking nature of the potato virus Y coat protein.Science advances · 2019Article
- Triticum aestivum heat shock protein 23.6 interacts with the coat protein of wheat yellow mosaic virus.Virus genes · 2019Article
- Susceptibility Genes to Plant Viruses.Viruses · 2018Review
- Reovirus Nonstructural Protein σNS Acts as an RNA Stability Factor Promoting Viral Genome Replication.Journal of virology · 2018Article
- Phosphorylation coexists with O-GlcNAcylation in a plant virus protein and influences viral infection.Molecular plant pathology · 2018Article
- A Functional Link between RNA Replication and Virion Assembly in the PotyvirusJournal of virology · 2018Article
- Cucumber mosaic virus coat protein modulates the accumulation of 2b protein and antiviral silencing that causes symptom recovery in planta.PLoS pathogens · 2017Article
- Coat Protein Regulation by CK2, CPIP, HSP70, and CHIP Is Required for Potato Virus A Replication and Coat Protein Accumulation.Journal of virology · 2017Article
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
unlabelledPotato virus A (PVA) is a single-stranded positive-sense RNA virus and a member of the family Potyviridae. The PVA coat protein (CP) has an intrinsic capacity to self-assemble into filamentous virus-like particles, but the mechanism responsible for the initiation of viral RNA encapsidation in vivo remains unclear. Apart from virion assembly, PVA CP is also involved in the inhibition of viral RNA translation. In this study, we show that CP inhibits PVA RNA translation in a dose-dependent manner, through a mechanism involving the CP-encoding region. Analysis of this region, however, failed to identify any RNA secondary structure(s) preferentially recognized by CP, suggesting that the inhibition depends on CP-CP rather than CP-RNA interactions. In agreement with this possibility, insertion of an in-frame stop codon upstream of the CP sequence led to a marked decrease in the inhibition of viral RNA translation. Based on these results, we propose a model in which the cotranslational interactions between excess CP accumulating in trans and CP translated from viral RNA in cis are required to initiate the translational repression. This model suggests a mechanism for how viral RNA can be sequestered from translation and specifically selected for encapsidation at the late stages of viral infection. IMPORTANCE: The main functions of the CP during potyvirus infection are to protect viral RNA from degradation and to transport it locally, systemically, and from host to host. Although virion assembly is a key step in the potyviral infectious cycle, little is known about how it is initiated and how viral RNA is selected for encapsidation. The results presented here suggest that CP-CP rather than CP-RNA interactions are predominantly involved in the sequestration of viral RNA away from translation. We propose that the cotranslational nature of these interactions may represent a mechanism for the selection of viral RNA for encapsidation. A better understanding of the mechanism of virion assembly may lead to development of crops resistant to potyviruses at the level of viral RNA encapsidation, thereby reducing the detrimental effects of potyvirus infections on food production.
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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.