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 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 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 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 Identification of the RNA-binding sites of the triple gene block protein 1 of bamboo mosaic potexvirus.

1999 ◽  
Vol 80 (5) ◽  
pp. 1119-1126 ◽  
Author(s):  
C H Wung ◽  
Y H Hsu ◽  
D Y Liou ◽  
W C Huang ◽  
N S Lin ◽  
...  
Keyword(s):  
Binding Sites ◽  
Rna Binding ◽  
Triple Gene Block ◽  
Gene Block ◽  
Triple Gene Block Protein ◽  
Rna Binding Sites

scholarly journals RNA-binding properties of the 63 kDa protein encoded by the triple gene block of poa semilatent hordeivirus

2001 ◽  
Vol 82 (10) ◽  
pp. 2569-2578 ◽  
Author(s):  
N. O. Kalinina ◽  
D. A. Rakitina ◽  
N. E. Yelina ◽  
A. A. Zamyatnin ◽  
T. A. Stroganova ◽  
...  
Keyword(s):  
Rna Binding ◽  
Triple Gene Block ◽  
Helicase Domain ◽  
Sequence Motifs ◽  
Long Distance ◽  
Binding Properties ◽  
Gene Block ◽  
Extension Domain ◽  
Positively Charged

The 63 kDa ‘63K’ movement protein encoded by the triple gene block of poa semilatent virus (PSLV) comprises the C-terminal NTPase/helicase domain and the N-terminal extension domain, which contains two positively charged sequence motifs, A and B. In this study, the in vitro RNA-binding properties of PSLV 63K and its mutants were analysed. Membrane-immobilized 63K and N-63K (isolated N-terminal extension domain) bound RNA at high NaCl concentrations. In contrast, C-63K (isolated NTPase/helicase domain) was able to bind RNA only at NaCl concentrations of up to 50 mM. In gel-shift assays, C-63K bound RNA to form complexes that were unable to enter an agarose gel, whereas complexes formed by N-63K could enter the gel. Full-length 63K formed both types of complexes. Visualization of the RNA–protein complexes formed by 63K, N-63K and C-63K by atomic force microscopy demonstrated that each complex had a different shape. Collectively, these data indicate that 63K has two distinct RNA-binding activities associated with the NTPase/helicase domain and the N-terminal extension domain. Mutations in either of the positively charged sequence motifs A and B had little effect on the RNA binding of the N-terminal extension domain, whereas mutations in both motifs together inhibited RNA binding. Hybrid viruses with mutations in motifs A and B were able to infect inoculated leaves of Nicotiana benthamiana plants, but were unable to move systemically to uninoculated leaves, suggesting that the RNA-binding activity of the N-terminal extension domain of PSLV 63K is associated with virus long-distance movement.

scholarly journals Characterization of Lagenaria mild mosaic virus, a New Potexvirus from Bottle Gourd in Myanmar

Plant Disease ◽  
2010 ◽  
Vol 94 (10) ◽  
pp. 1225-1230 ◽  
Author(s):  
Ok-Kyung Kim ◽  
Tadasuke Mizutani ◽  
Khin Soe ◽  
Key-Woon Lee ◽  
Keiko T. Natsuaki
Keyword(s):  
Mosaic Virus ◽  
Triple Gene Block ◽  
Bottle Gourd ◽  
Mild Mosaic ◽  
Sequence Analyses ◽  
Gene Block ◽  
Mild Mosaic Virus ◽  
Papaya Mosaic Virus ◽  
A New Species

A putative Potexvirus was detected from bottle gourd (Lagenaria siceraria) showing mosaic and mottle symptoms in Myanmar in 2007. The virus was designated Lagenaria mild mosaic virus (LaMMoV) and was further characterized. In artificial inoculation tests, infectivity of LaMMoV was limited to two families: Chenopodiaceae and Cucurbitaceae. The host range of LaMMoV differs from those of the two cucurbit-infecting potexviruses, Alternanthera mosaic virus (AltMV) and Papaya mosaic virus (PapMV). Sequence analyses of LaMMoV showed that the C-terminal 3,859 nucleotides, excluding the poly-A tail, includes the C-terminal region of an RNA-dependent RNA polymerase (RdRp), a triple gene block (TGB), a coat protein (CP), and a 3′ untranslated region (UTR), all of which are typical of potexviruses. Although LaMMoV is related closely to AltMV and PapMV, its nucleotide sequences differ from those of other previously reported potexviruses. Therefore, we report LaMMoV as a new species of the genus Potexvirus that occurs in the cucurbit bottle gourd.

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
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