scholarly journals Arg-16 and Arg-21 in the N-terminal region of the triple-gene-block protein 1 of Bamboo mosaic virus are essential for virus movement

2004 ◽  
Vol 85 (1) ◽  
pp. 251-259 ◽  
Author(s):  
Ming-Kuem Lin ◽  
Ban-Yang Chang ◽  
Jia-Teh Liao ◽  
Na-Sheng Lin ◽  
Yau-Heiu Hsu
Keyword(s):  
Mosaic Virus ◽  
Triple Gene Block ◽  
Terminal Region ◽  
Virus Movement ◽  
Gene Block ◽  
Triple Gene Block Protein

scholarly journals A Thioredoxin Domain-Containing Protein Interacts with Pepino mosaic virus Triple Gene Block Protein 1

2018 ◽  
Vol 19 (12) ◽  
pp. 3747
Author(s):  
Matthaios Mathioudakis ◽  
Souheyla Khechmar ◽  
Carolyn Owen ◽  
Vicente Medina ◽  
Karima Ben Mansour ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Triple Gene Block ◽  
Polyclonal Antiserum ◽  
Post Inoculation ◽  
Mrna Levels ◽  
In Planta ◽  
Pepino Mosaic Virus ◽  
Gene Block ◽  
Triple Gene Block Protein

Pepino mosaic virus (PepMV) is a mechanically-transmitted tomato pathogen of importance worldwide. Interactions between the PepMV coat protein and triple gene block protein (TGBp1) with the host heat shock cognate protein 70 and catalase 1 (CAT1), respectively, have been previously reported by our lab. In this study, a novel tomato interactor (SlTXND9) was shown to bind the PepMV TGBp1 in yeast-two-hybrid screening, in vitro pull-down and bimolecular fluorescent complementation (BiFC) assays. SlTXND9 possesses part of the conserved thioredoxin (TRX) active site sequence (W__PC vs. WCXPC), and TXND9 orthologues cluster within the TRX phylogenetic superfamily closest to phosducin-like protein-3. In PepMV-infected and healthy Nicotiana benthamiana plants, NbTXND9 mRNA levels were comparable, and expression levels remained stable in both local and systemic leaves for 10 days post inoculation (dpi), as was also the case for catalase 1 (CAT1). To localize the TXND9 in plant cells, a polyclonal antiserum was produced. Purified α-SlTXND9 immunoglobulin (IgG) consistently detected a set of three protein bands in the range of 27–35 kDa, in the 1000 and 30,000 g pellets, and the soluble fraction of extracts of healthy and PepMV-infected N. benthamiana leaves, but not in the cell wall. These bands likely consist of the homologous protein NbTXND9 and its post-translationally modified derivatives. On electron microscopy, immuno-gold labelling of ultrathin sections of PepMV-infected N. benthamiana leaves using α-SlTXND9 IgG revealed particle accumulation close to plasmodesmata, suggesting a role in virus movement. Taken together, this study highlights a novel tomato-PepMV protein interaction and provides data on its localization in planta. Currently, studies focusing on the biological function of this interaction during PepMV infection are in progress.

scholarly journals Transient Coexpression of Individual Genes Encoded by the Triple Gene Block of Potato mop-top virus Reveals Requirements for TGBp1 Trafficking

2004 ◽  
Vol 17 (8) ◽  
pp. 921-930 ◽  
Author(s):  
Andrey A. Zamyatnin ◽  
Andrey G. Solovyev ◽  
Eugene I. Savenkov ◽  
Anna Germundsson ◽  
Maria Sandgren ◽  
...  
Keyword(s):  
Cell Wall ◽  
Fluorescent Protein ◽  
Triple Gene Block ◽  
Terminal Region ◽  
Virus Movement ◽  
Cell Periphery ◽  
Movement Proteins ◽  
Gene Block ◽  
Potato Mop Top Virus ◽  
Green Fluorescent

TGBp1, TGBp2, and TGBp3, three plant virus movement proteins encoded by the “triple gene block” (TGB), may act in concert to facilitate cell-to-cell transport of viral RNA genomes. Transient expression of Potato mop-top virus (genus Pomovirus) movement proteins was used as a model to reconstruct interactions between TGB proteins. In bombarded epidermal cells of Nicotiana benthamiana, green fluorescent protein (GFP)-TGBp1 was distributed uniformly. However, in the presence of TGBp2 and TGBp3, GFP-TGBp1 was directed to intermediate bodies at the cell periphery, and to cell wall-embedded punctate bodies. Moreover, GFP-TGBp1 migrated into cells immediately adjacent to the bombarded cell. These data suggest that TGBp2 and TGBp3 mediate transport of GFP-TGBp1 to and through plasmodesmata. Mutagenesis of TGBp1 suggested that the NTPase and helicase activities of TGBp1 were not required for its transport to intermediate bodies directed by TGBp2 and TGBp3, but these activities were essential for the protein association with cell wall-embedded punctate bodies and translocation of TGBp1 to neighboring cells. The C-terminal region of TGBp1 was critical for trafficking mediated by TGBp2 and TGBp3. Mutation analysis also suggested an involvement of the TGBp2 C-terminal region in interactions with TGBp1.

scholarly journals Topological properties of the triple gene block protein 2 of Bamboo mosaic virus

Virology ◽  
2008 ◽  
Vol 379 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Hsiu-Ting Hsu ◽  
Yuan-Lin Chou ◽  
Yang-Hao Tseng ◽  
Yu-Hsing Lin ◽  
Tzung-Min Lin ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Triple Gene Block ◽  
Topological Properties ◽  
Gene Block ◽  
Triple Gene Block Protein

scholarly journals Characterization of the RNA-binding properties of the triple-gene-block protein 2 of Bamboo mosaic virus

2009 ◽  
Vol 6 (1) ◽  
pp. 50 ◽  
Author(s):  
Hsiu-Ting Hsu ◽  
Yang-Hao Tseng ◽  
Yuan-Lin Chou ◽  
Shiaw-Hwa Su ◽  
Yau-Heiu Hsu ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Rna Binding ◽  
Triple Gene Block ◽  
Binding Properties ◽  
Gene Block ◽  
Triple Gene Block Protein

scholarly journals The Stable Association of Virion with the Triple-gene-block Protein 3-based Complex of Bamboo mosaic virus

2013 ◽  
Vol 9 (6) ◽  
pp. e1003405 ◽  
Author(s):  
Yuan-Lin Chou ◽  
Yi-Jing Hung ◽  
Yang-Hao Tseng ◽  
Hsiu-Ting Hsu ◽  
Jun-Yi Yang ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Triple Gene Block ◽  
Gene Block ◽  
Stable Association ◽  
Triple Gene Block Protein

scholarly journals The cysteine residues at the C-terminal tail of Bamboo mosaic virus triple gene block protein 2 are critical for efficient plasmodesmata localization of protein 1 in the same block

Virology ◽  
2017 ◽  
Vol 501 ◽  
pp. 47-53 ◽  
Author(s):  
Tsai-Ling Ho ◽  
Hsiang-Chi Lee ◽  
Yuan-Lin Chou ◽  
Yang-Hao Tseng ◽  
Wei-Cheng Huang ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Triple Gene Block ◽  
Cysteine Residues ◽  
Gene Block ◽  
Triple Gene Block Protein

scholarly journals Actin Cytoskeleton and Golgi Involvement in Barley stripe mosaic virus Movement and Cell Wall Localization of Triple Gene Block Proteins

2013 ◽  
Vol 29 (1) ◽  
pp. 17-30 ◽  
Author(s):  
Hyoun-Sub Lim ◽  
Mi Yeon Lee ◽  
Jae Sun Moon ◽  
Jung-Kyung Moon ◽  
Yong-Man Yu ◽  
...  
Keyword(s):  
Cell Wall ◽  
Actin Cytoskeleton ◽  
Mosaic Virus ◽  
Triple Gene Block ◽  
Barley Stripe Mosaic Virus ◽  
Virus Movement ◽  
Gene Block

scholarly journals The Two Conserved Cysteine Residues of the Triple Gene Block Protein 2 Are Critical for Both Cell-to-Cell and Systemic Movement of Bamboo mosaic virus

2009 ◽  
Vol 22 (11) ◽  
pp. 1379-1388 ◽  
Author(s):  
Yang-Hao Tseng ◽  
Hsiu-Ting Hsu ◽  
Yuan-Lin Chou ◽  
Chung-Chi Hu ◽  
Na-Sheng Lin ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Mosaic Virus ◽  
Outer Surface ◽  
Transmembrane Protein ◽  
Triple Gene Block ◽  
Cell Movement ◽  
Gene Block ◽  
Systemic Movement ◽  
Granular Vesicles ◽  
Triple Gene Block Protein

The triple gene block protein 2 (TGBp2) of Bamboo mosaic virus (BaMV) is a transmembrane protein which is known to be required for the cell-to-cell movement of potexviruses. This protein has two conserved Cys residues, Cys-109 and Cys-112, at its C-terminal tail, which is supposed to be exposed on the outer surface of the endoplasmic reticulum (ER) membrane and ER-derived granular vesicles. In this study, we investigated the importance of these two Cys residues on the cell-to-cell and systemic movement of BaMV. Our results indicate that the Cys-to-Ala substitutions in TGBp2 make the cell-to-cell movement of BaMV relatively inefficient and the systemic movement of BaMV severely inhibited. Moreover, the defect in systemic movement is attributed to the inefficient transport of viral RNA in the phloem of petiole. Clearly, TGBp2 is critical not only for the cell-to-cell but also for the systemic movement of BaMV. In addition, the conserved Cys residues are important for the functioning of TGBp2.

scholarly journals Molecular biology of potexviruses: recent advances

2007 ◽  
Vol 88 (6) ◽  
pp. 1643-1655 ◽  
Author(s):  
Jeanmarie Verchot-Lubicz ◽  
Chang-Ming Ye ◽  
Devinka Bamunusinghe
Keyword(s):  
Gene Silencing ◽  
Rna Synthesis ◽  
Triple Gene Block ◽  
Potato Virus X ◽  
Future Research ◽  
Virus Movement ◽  
Suppressor Activity ◽  
Gene Block ◽  
Recent Advances

Recent advances in potexvirus research have produced new models describing virus replication, cell-to-cell movement, encapsidation, R gene-mediated resistance and gene silencing. Interactions between distant RNA elements are a central theme in potexvirus replication. The 5′ non-translated region (NTR) regulates genomic and subgenomic RNA synthesis and encapsidation, as well as virus plasmodesmal transport. The 3′ NTR regulates both plus- and minus-strand RNA synthesis. How the triple gene-block proteins interact for virus movement is still elusive. As the potato virus X (PVX) TGBp1 protein gates plasmodesmata, regulates virus translation and is a suppressor of RNA silencing, further research is needed to determine how these properties contribute to propelling virus through the plasmodesmata. Specifically, TGBp1 suppressor activity is required for virus movement, but how the silencing machinery relates to plasmodesmata is not known. The TGBp2 and TGBp3 proteins are endoplasmic reticulum (ER)-associated proteins required for virus movement. TGBp2 associates with ER-derived vesicles that traffic along the actin network. Future research will determine whether the virus-induced vesicles are cytopathic structures regulating events along the ER or are vehicles carrying virus to the plasmodesmata for transfer into neighbouring cells. Efforts to assemble virions in vitro identified a single-tailed particle (STP) comprising RNA, coat protein (CP) and TGBp1. It has been proposed that TGBp1 aids in transport of virions or STP between cells and ensures translation of RNA in the receiving cells. PVX is also a tool for studying Avr–R gene interactions and gene silencing in plants. The PVX CP is the elicitor for the Rx gene. Recent reports of the PVX CP reveal how CP interacts with the Rx gene product.

scholarly journals Subcellular Localization of the Barley Stripe Mosaic Virus Triple Gene Block Proteins

2009 ◽  
Vol 83 (21) ◽  
pp. 11413-11413 ◽  
Author(s):  
Hyoun-Sub Lim ◽  
Jennifer N. Bragg ◽  
Uma Ganesan ◽  
Steven Ruzin ◽  
Denise Schichnes ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Mosaic Virus ◽  
Triple Gene Block ◽  
Barley Stripe Mosaic Virus ◽  
Gene Block
Sign in / Sign up

Export Citation Format

Share Document