ArticleJournal of virology2000
Cellular targets of functional and dysfunctional mutants of tobacco mosaic virus movement protein fused to green fluorescent protein.
Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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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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
29 citing papers in PubMed, 81 citations in OpenAlex.
- dsRNA-induced immunity targets plasmodesmata and is suppressed by viral movement proteins.The Plant cell · 2023Article
- In Vivo Visualization of Mobile mRNA Particles in Plants Using BglG.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Function of Plasmodesmata in the Interaction of Plants with Microbes and Viruses.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Intercellular trafficking via plasmodesmata: molecular layers of complexity.Cellular and molecular life sciences : CMLS · 2021Review
- Article
- An aromatic amino acid and associated helix in the C-terminus of the potato leafroll virus minor capsid protein regulate systemic infection and symptom expression.PLoS pathogens · 2018Article
- Identification and characterization of privet leaf blotch-associated virus, a novel idaeovirus.Molecular plant pathology · 2017Article
- Antiviral Resistance Protein Tm-2Plant physiology · 2017Article
- The rubisco small subunit is involved in tobamovirus movement and Tm-2²-mediated extreme resistance.Plant physiology · 2013Article
- Control of Tobacco mosaic virus movement protein fate by CELL-DIVISION-CYCLE protein48.Plant physiology · 2012Article
- RNA transport during TMV cell-to-cell movement.Frontiers in plant science · 2012Article
- Cellular pathways for viral transport through plasmodesmata.Protoplasma · 2011Review
- The Role of Microtubule Association in Plasmodesmal Targeting of Potato mop-top virus Movement Protein TGBp1.The open virology journal · 2011Article
- ANK, a host cytoplasmic receptor for the Tobacco mosaic virus cell-to-cell movement protein, facilitates intercellular transport through plasmodesmata.PLoS pathogens · 2010Article
- Interaction of the Tobacco mosaic virus movement protein with microtubules during the cell cycle in tobacco BY-2 cells.Protoplasma · 2009Article
- Tobacco mosaic virus movement protein interacts with green fluorescent protein-tagged microtubule end-binding protein 1.Plant physiology · 2008Article
- Tobacco mosaic virus movement protein enhances the spread of RNA silencing.PLoS pathogens · 2008Article
- MPB2C, a microtubule-associated plant factor, is required for microtubular accumulation of tobacco mosaic virus movement protein in plants.Plant physiology · 2007Article
- Microtubule-associated proteins in higher plants.Journal of plant research · 2007Review
- Tobacco mosaic virus movement protein functions as a structural microtubule-associated protein.Journal of virology · 2006Article
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 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intercellular transport of tobacco mosaic virus (TMV) RNA involves the accumulation of virus-encoded movement protein (MP) in plasmodesmata (Pd), in endoplasmic reticulum (ER)-derived inclusion bodies, and on microtubules. The functional significance of these interactions in viral RNA (vRNA) movement was tested in planta and in protoplasts with TMV derivatives expressing N- and C-terminal deletion mutants of MP fused to the green fluorescent protein. Deletion of 55 amino acids from the C terminus of MP did not interfere with the vRNA transport function of MP:GFP but abolished its accumulation in inclusion bodies, indicating that accumulation of MP at these ER-derived sites is not a requirement for function in vRNA intercellular movement. Deletion of 66 amino acids from the C terminus of MP inactivated the protein, and viral infection occurred only upon complementation in plants transgenic for MP. The functional deficiency of the mutant protein correlated with its inability to associate with microtubules and, independently, with its absence from Pd at the leading edge of infection. Inactivation of MP by N-terminal deletions was correlated with the inability of the protein to target Pd throughout the infection site, whereas its associations with microtubules and inclusion bodies were unaffected. The observations support a role of MP-interacting microtubules in TMV RNA movement and indicate that MP targets microtubules and Pd by independent mechanisms. Moreover, accumulation of MP in Pd late in infection is insufficient to support viral movement, confirming that intercellular transport of vRNA relies on the presence of MP in Pd at the leading edge of infection.
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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.