ArticleMolecular plant pathology2020
The cis-expression of the coat protein of turnip mosaic virus is essential for viral intercellular movement in plants.
Article in Molecular plant pathology, 2020. 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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Who cites it
26 citing papers in PubMed, 55 citations in OpenAlex.
- Turnip mosaic virus utilizes the lipid droplet biogenesis machinery to facilitate its propagation in plants.The New phytologist · 2026Article
- Contrasting Effects of Tagging Turnip Mosaic Virus Proteins.Pathogens (Basel, Switzerland) · 2026Article
- Review
- Functionality of potato virus Y coat protein in cell-to-cell movement dynamics is defined by its N-terminal region.Journal of virology · 2025Article
- The PSRP2/4 Proteins Promote Viral Infection by Interacting with the VPg Protein of TuMV.Plants (Basel, Switzerland) · 2025Article
- Oligomeric SWEET1g of Solanum tuberosum confers resistance to potato virus Y and Potato virus X.The Plant journal : for cell and molecular biology · 2025Article
- Cytokinesis-Defective 1 (CYT1) Positively Regulates Plant Antiviral Immunity by Promoting Callose Deposition and Ascorbic Acid Biosynthesis.Molecular plant pathology · 2025Article
- Turnip mosaic virus selectively subverts a PR-5 thaumatin-like, plasmodesmal protein to promote viral infection.The New phytologist · 2025Article
- Identification of a novel mild isolate of areca palm necrotic spindle-spot virus (ANSSVm) lacking two cysteine proteases (HC-Pro1 and HC-Pro2).Frontiers in microbiology · 2025Article
- Two plant membrane-shaping reticulon-like proteins play contrasting complex roles in turnip mosaic virus infection.Molecular plant pathology · 2024Article
- AtHVA22a, a plant-specific homologue of Reep/DP1/Yop1 family proteins is involved in turnip mosaic virus propagation.Molecular plant pathology · 2024Article
- Umbravirus-like RNA viruses are capable of independent systemic plant infection in the absence of encoded movement proteins.PLoS biology · 2024Article
- Rubisco small subunit (RbCS) is co-opted by potyvirids as the scaffold protein in assembling a complex for viral intercellular movement.PLoS pathogens · 2024Article
- The mystery remains: How do potyviruses move within and between cells?Molecular plant pathology · 2023Review
- Host Factors GenesPlants (Basel, Switzerland) · 2023Article
- Role of Plant Virus Movement Proteins in Suppression of Host RNAi Defense.International journal of molecular sciences · 2023Review
- Cotyledon peeling method for passion fruit protoplasts: a versatile cell system for transient gene expression in passion fruitFrontiers in plant science · 2023Article
- A sword or a buffet: plant endomembrane system in viral infections.Frontiers in plant science · 2023Review
- Plant production of a virus-like particle-based vaccine candidate against porcine reproductive and respiratory syndrome.Frontiers in plant science · 2023Article
- Article
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4 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
To establish infection, plant viruses are evolutionarily empowered with the ability to spread intercellularly. Potyviruses represent the largest group of known plant-infecting RNA viruses, including many agriculturally important viruses. To better understand intercellular movement of potyviruses, we used turnip mosaic virus (TuMV) as a model and constructed a double-fluorescent (green and mCherry) protein-tagged TuMV infectious clone, which allows distinct observation of primary and secondary infected cells. We conducted a series of deletion and mutation analyses to characterize the role of TuMV coat protein (CP) in viral intercellular movement. TuMV CP has 288 amino acids and is composed of three domains: the N-terminus (amino acids 1-97), the core (amino acids 98-245), and the C-terminus (amino acids 246-288). We found that deletion of CP or its segments amino acids 51-199, amino acids 200-283, or amino acids 265-274 abolished the ability of TuMV to spread intercellularly but did not affect virus replication. Interestingly, deletion of amino acids 6-50 in the N-terminus domain resulted in the formation of aberrant virions but did not significantly compromise TuMV cell-to-cell and systemic movement. We identified the charged residues R178 and D222 within the core domain that are essential for virion formation and TuMV local and systemic transport in plants. Moreover, we found that trans-expression of the wild-type CP either by TuMV or through genetic transformation-based stable expression could not rescue the movement defect of CP mutants. Taken together these results suggest that TuMV CP is not essential for viral genome replication but is indispensable for viral intercellular transport where only the cis-expressed CP is functional.
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