ArticleJournal of virology2003
An umbraviral protein, involved in long-distance RNA movement, binds viral RNA and forms unique, protective ribonucleoprotein complexes.
Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.
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.
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
31 citing papers in PubMed, 1 synthesis or guideline pooled it, 77 citations in OpenAlex.
- Pooled it
- Blurred Boundaries: Functional Overlap Between Coat Protein and 30K Movement Proteins in Systemic Movement.The plant pathology journal · 2026Review
- Viral condensates formed by Pea enation mosaic virus 2 sequester ribosomal components and suppress translation.Virology · 2025Article
- Review
- Dimerization of an umbravirus RNA genome activates subgenomic mRNA transcription.Nucleic acids research · 2023Article
- Dissecting dynamic plant virus synergism in mixed infections of poleroviruses, umbraviruses, and tombusvirus-like associated RNAs.Frontiers in microbiology · 2023Article
- Gain-of-function mutant of movement protein allows systemic transport of a defective tobacco mosaic virus.iScience · 2022Article
- Article
- A plant-infecting subviral RNA associated with poleroviruses produces a subgenomic RNA which resists exonuclease XRN1 in vitro.Virology · 2022Article
- Phase separation of a plant virus movement protein and cellular factors support virus-host interactions.PLoS pathogens · 2021Article
- The HIV-1 Antisense Gene ASP: The New Kid on the Block.Vaccines · 2021Review
- Plant viral proteins and fibrillarin: the link to complete the infective cycle.Molecular biology reports · 2021Review
- Structural Analysis and Whole Genome Mapping of a New Type of Plant Virus Subviral RNA: Umbravirus-Like Associated RNAs.Viruses · 2021Article
- New insights into the evolutionary features of viral overlapping genes by discriminant analysis.Virology · 2020Article
- Article
- Unusual dicistronic expression from closely spaced initiation codons in an umbravirus subgenomic RNA.Nucleic acids research · 2018Article
- The Torradovirus-specific RNA2-ORF1 protein is necessary for plant systemic infection.Molecular plant pathology · 2018Article
- Article
- Cajal bodies and their role in plant stress and disease responses.RNA biology · 2017Review
- Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Umbraviruses are different from most other viruses in that they do not encode a conventional capsid protein (CP); therefore, no recognizable virus particles are formed in infected plants. Their lack of a CP is compensated for by the ORF3 protein, which fulfils functions that are provided by the CPs of other viruses, such as protection and long-distance movement of viral RNA. When the Groundnut rosette virus (GRV) ORF3 protein was expressed from Tobacco mosaic virus (TMV) in place of the TMV CP [TMV(ORF3)], in infected cells it interacted with the TMV RNA to form filamentous ribonucleoprotein (RNP) particles that had elements of helical structure but were not as uniform as classical virions. These RNP particles were observed in amorphous inclusions in the cytoplasm, where they were embedded within an electron-dense matrix material. The inclusions were detected in all types of cells and were abundant in phloem-associated cells, in particular companion cells and immature sieve elements. RNP-containing complexes similar in appearance to the inclusions were isolated from plants infected with TMV(ORF3) or with GRV itself. In vitro, the ORF3 protein formed oligomers and bound RNA in a manner consistent with its role in the formation of RNP complexes. It is suggested that the cytoplasmic RNP complexes formed by the ORF3 protein serve to protect viral RNA and may be the form in which it moves through the phloem. Thus, the RNP particles detected here represent a novel structure which may be used by umbraviruses as an alternative to classical virions.
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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.