4.8 Article

Voltage-dependent anion channel proteins associate with dynamic Bamboo mosaic virus-induced complexes

期刊

PLANT PHYSIOLOGY
卷 188, 期 2, 页码 1061-1080

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OXFORD UNIV PRESS INC
DOI: 10.1093/plphys/kiab519

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  1. Ministry of Science and Technology, Taiwan [MOST-109-2313-B-005-050]
  2. Advanced Plant Biotechnology Center from the Featured Areas Research Center Program

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This study reveals the involvement of mitochondrial voltage-dependent anion channel proteins in the dynamic Bamboo mosaic virus (BaMV)-induced complex, which supports BaMV accumulation in Nicotiana benthamiana. The study also demonstrates that interaction with BaMV triple gene block protein 1 (TGBp1) can induce aggregation of the NbVDAC proteins and promote BaMV replication. These findings highlight the importance of mitochondrial proteins in viral complex formation and virus infection.
Mitochondrial voltage-dependent anion channel proteins associate with the dynamic Bamboo mosaic virus (BaMV)-induced complex and support BaMV accumulation in Nicotiana benthamiana. 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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