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 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 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 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 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 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 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

scholarly journals Complete Genome Sequence of aLily virus XIsolate from Japan

2018 ◽  
Vol 6 (4) ◽  
Author(s):  
Takamichi Nijo ◽  
Yukari Okano ◽  
Masayoshi Kondo ◽  
Hiroaki Okuhara ◽  
Hiroyo Sekimura ◽  
...  
Keyword(s):  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Complete Genome ◽  
Triple Gene Block ◽  
Start Codon ◽  
Gene Block ◽  
First Time ◽  
Triple Gene Block Protein

ABSTRACTThe complete genome sequence ofLily virus X(LVX), which infects lilies, was determined for the first time from lilies in Japan. As with previous reports, the genome of the Japanese LVX isolate lacked an AUG start codon for the triple gene block protein 3-like region.

scholarly journals Functional Analyses and Identification of Two Arginine Residues Essential to the ATP-Utilizing Activity of the Triple Gene Block Protein 1 of Bamboo Mosaic Potexvirus

Virology ◽  
2000 ◽  
Vol 277 (2) ◽  
pp. 336-344 ◽  
Author(s):  
Dann-Ying Liou ◽  
Yau-Heiu Hsu ◽  
Chiung-Hua Wung ◽  
Wen-Horng Wang ◽  
Na-Sheng Lin ◽  
...  
Keyword(s):  
Triple Gene Block ◽  
Gene Block ◽  
Arginine Residues ◽  
Functional Analyses ◽  
Triple Gene Block Protein

scholarly journals Triple Gene Block Protein Interactions Involved in Movement of Barley Stripe Mosaic Virus

2008 ◽  
Vol 82 (10) ◽  
pp. 4991-5006 ◽  
Author(s):  
Hyoun-Sub Lim ◽  
Jennifer N. Bragg ◽  
Uma Ganesan ◽  
Diane M. Lawrence ◽  
Jialin Yu ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Triple Gene Block ◽  
Cell Movement ◽  
Wild Type Virus ◽  
Barley Stripe Mosaic Virus ◽  
Wild Type ◽  
In Planta ◽  
Gene Block ◽  
Physical Interactions

ABSTRACT Barley stripe mosaic virus (BSMV) encodes three movement proteins in an overlapping triple gene block (TGB), but little is known about the physical interactions of these proteins. We have characterized a ribonucleoprotein (RNP) complex consisting of the TGB1 protein and plus-sense BSMV RNAs from infected barley plants and have identified TGB1 complexes in planta and in vitro. Homologous TGB1 binding was disrupted by site-specific mutations in each of the first two N-terminal helicase motifs but not by mutations in two C-terminal helicase motifs. The TGB2 and TGB3 proteins were not detected in the RNP, but affinity chromatography and yeast two-hybrid experiments demonstrated that TGB1 binds to TGB3 and that TGB2 and TGB3 form heterologous interactions. These interactions required the TGB2 glycine 40 and the TGB3 isoleucine 108 residues, and BSMV mutants containing these amino acid substitution were unable to move from cell to cell. Infectivity experiments indicated that TGB1 separated on a different genomic RNA from TGB2 and TGB3 could function in limited cell-to-cell movement but that the rates of movement depended on the levels of expression of the proteins and the contexts in which they are expressed. Moreover, elevated expression of the wild-type TGB3 protein interfered with cell-to-cell movement but movement was not affected by the similar expression of a TGB3 mutant that fails to interact with TGB2. These experiments suggest that BSMV movement requires physical interactions of TGB2 and TGB3 and that substantial deviation from the TGB protein ratios expressed by the wild-type virus compromises movement.

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