ArticlePLoS pathogens2013
The stable association of virion with the triple-gene-block protein 3-based complex of Bamboo mosaic virus.
Article in PLoS pathogens, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 59 citations in OpenAlex.
- Pepino Mosaic Virus: A Globally Important Tomato Pathogen and a Rising Model in Molecular Virology.Molecular plant pathology · 2026Review
- Nucleolar fibrillarin methyltransferase regulates systemic trafficking of a plant virus satellite RNA.The Plant cell · 2025Article
- Role of the Transcription Factor NbTFIISL in Enhancing Bamboo Mosaic Virus Accumulation via Mitochondria Localisation.Molecular plant pathology · 2025Article
- NbHDR, A Host Protein Involved in the MEP Pathway, Interacts With Bamboo Mosaic Virus Replicase and Enhances Viral Accumulation.Molecular plant pathology · 2025Article
- Proviral insights of glycolytic enolase inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Alphaflexiviridae in Focus: Genomic Signatures, Conserved Elements and Viral-Driven Cellular Remodeling.Viruses · 2025Review
- Discovery and characterization of a novel carlavirus in Ligularia jaluensis plants.Virologica Sinica · 2025Article
- Protein P5 of pear chlorotic leaf spot-associated virus is a pathogenic factor that suppresses RNA silencing and enhances virus movement.Molecular plant pathology · 2024Article
- Zn2+-dependent association of cysteine-rich protein with virion orchestrates morphogenesis of rod-shaped viruses.PLoS pathogens · 2024Article
- Importin α2 participates in RNA interference against bamboo mosaic virus accumulation in Nicotiana benthamiana via NbAGO10a-mediated small RNA clearance.Molecular plant pathology · 2024Article
- A viral movement protein co-opts endoplasmic reticulum luminal-binding protein and calreticulin to promote intracellular movement.Plant physiology · 2023Article
- Trade-off between local replication and long-distance dissemination during experimental evolution of a satellite RNA.Frontiers in microbiology · 2023Article
- Interaction between Movement Proteins ofViruses · 2022Article
- Short 5' Untranslated Region Enables Optimal Translation of Plant Virus Tricistronic RNA via Leaky Scanning.Journal of virology · 2022Article
- First Report of DistinctViruses · 2022Article
- Voltage-dependent anion channel proteins associate with dynamic Bamboo mosaic virus-induced complexes.Plant physiology · 2022Article
- The C-Terminal Transmembrane Domain of Cowpea Mild Mottle Virus TGBp2 Is Critical for Plasmodesmata Localization and for Its Interaction With TGBp1 and TGBp3.Frontiers in microbiology · 2022Article
- The differential presence of human polyomaviruses, JCPyV and BKPyV, in prostate cancer and benign prostate hypertrophy tissues.BMC cancer · 2021Article
- Engineering Resistance Against Viruses in Field Crops Using CRISPR- Cas9.Current genomics · 2021Review
- NbPsbO1 Interacts Specifically with theJournal of virology · 2021Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The triple-gene-block protein 3 (TGBp3) of Bamboo mosaic virus (BaMV) is an integral endoplasmic reticulum (ER) membrane protein which is assumed to form a membrane complex to deliver the virus intracellularly. However, the virus entity that is delivered to plasmodesmata (PD) and its association with TGBp3-based complexes are not known. Results from chemical extraction and partial proteolysis of TGBp3 in membrane vesicles revealed that TGBp3 has a right-side-out membrane topology; i.e., TGBp3 has its C-terminal tail exposed to the outer surface of ER. Analyses of the TGBp3-specific immunoprecipitate of Sarkosyl-extracted TGBp3-based complex revealed that TGBp1, TGBp2, TGBp3, capsid protein (CP), replicase and viral RNA are potential constituents of virus movement complex. Substantial co-fractionation of TGBp2, TGBp3 and CP, but not TGBp1, in the early eluted gel filtration fractions in which virions were detected after TGBp3-specific immunoprecipitation suggested that the TGBp2- and TGBp3-based complex is able to stably associate with the virion. This notion was confirmed by immunogold-labeling transmission electron microscopy (TEM) of the purified virions. In addition, mutational and confocal microscopy analyses revealed that TGBp3 plays a key role in virus cell-to-cell movement by enhancing the TGBp2- and TGBp3-dependent PD localization of TGBp1. Taken together, our results suggested that the cell-to-cell movement of potexvirus requires stable association of the virion cargo with the TGBp2- and TGBp3-based membrane complex and recruitment of TGBp1 to the PD by this complex.
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