ArticlePlant physiology2022
Voltage-dependent anion channel proteins associate with dynamic Bamboo mosaic virus-induced complexes.
Article in Plant physiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Bamboo mosaic virus-induced metabolic reprogramming engages mitochondrial function to regulate redox homeostasis and defense responses in Nicotiana benthamiana.BMC plant biology · 2025Article
- Role of the Transcription Factor NbTFIISL in Enhancing Bamboo Mosaic Virus Accumulation via Mitochondria Localisation.Molecular plant pathology · 2025Article
- Live-cell imaging of a plant virus replicase during infection using a genetically encoded, antibody-based probe.Plant physiology · 2025Article
- Proviral insights of glycolytic enolase inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Cucumber Green Mottle Mosaic Virus Coat Protein Hijacks Mitochondrial ATPδ to Promote Viral Infection.Molecular plant pathology · 2024Article
- Unveiling the viroporin arsenal in plant viruses: Implications for the future.PLoS pathogens · 2024Review
- The 6-kilodalton peptide 1 in plant viruses of the family Potyviridae is a viroporin.Proceedings of the National Academy of Sciences of the United States of America · 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
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Infection cycles of viruses are highly dependent on membrane-associated host factors. To uncover the infection cycle of Bamboo mosaic virus (BaMV) in detail, we purified the membrane-associated viral complexes from infected Nicotiana benthamiana plants and analyzed the involved host factors. Four isoforms of voltage-dependent anion channel (VDAC) proteins on the outer membrane of mitochondria were identified due to their upregulated expression in the BaMV complex-enriched membranous fraction. Results from loss- and gain-of-function experiments indicated that NbVDAC2, -3, and -4 are essential for efficient BaMV accumulation. During BaMV infection, all NbVDACs concentrated into larger aggregates, which overlapped and trafficked with BaMV virions to the structure designated as the "dynamic BaMV-induced complex." Besides the endoplasmic reticulum and mitochondria, BaMV replicase and double-stranded RNAs were also found in this complex, suggesting the dynamic BaMV-induced complex is a replication complex. Yeast two-hybrid and pull-down assays confirmed that BaMV triple gene block protein 1 (TGBp1) could interact with NbVDACs. Confocal microscopy revealed that TGBp1 is sufficient to induce NbVDAC aggregates, which suggests that TGBp1 may play a pivotal role in the NbVDAC-virion complex. Collectively, these findings indicate that NbVDACs may associate with the dynamic BaMV-induced complex via TGBp1 and NbVDAC2, -3, or -4 and can promote BaMV accumulation. This study reveals the involvement of mitochondrial proteins in a viral complex and virus infection.
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