In Planta production of immunogenic poliovirus peptide using tobacco mosaic virus-based vector system

2006 ◽  
Vol 101 (5) ◽  
pp. 398-402 ◽  
Author(s):  
Kazuhito Fujiyama ◽  
Wanida Saejung ◽  
Itaru Yanagihara ◽  
Junko Nakado ◽  
Ryo Misaki ◽  
...  
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Vector System ◽  
In Planta

scholarly journals The Use of a Tobacco mosaic virus-Based Expression Vector System in Chrysanthemum

2017 ◽  
Vol 33 (4) ◽  
pp. 429-433 ◽  
Author(s):  
Minju Park ◽  
Eseul Baek ◽  
Ju-Yeon Yoon ◽  
Peter Palukaitis
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Expression Vector ◽  
Vector System

scholarly journals Dimerization of Recombinant Tobacco Mosaic Virus Movement Protein

2004 ◽  
Vol 78 (7) ◽  
pp. 3372-3377 ◽  
Author(s):  
Laurence M. Brill ◽  
Songpon Dechongkit ◽  
Byron DeLaBarre ◽  
Jonathon Stroebel ◽  
Roger N. Beachy ◽  
...  
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Electrostatic Interactions ◽  
Analytical Ultracentrifugation ◽  
Movement Protein ◽  
Hydrophobic Interactions ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
In Planta ◽  
Native Page

ABSTRACT The p30 movement protein (MP) is essential for cell-to-cell spread of tobacco mosaic virus in planta. We used anion-exchange chromatography and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to obtain highly purified 30-kDa MP, which migrated as a single band in native PAGE. Analytical ultracentrifugation suggested that the protein was monodisperse and dimeric in the nonionic detergent n-octyl-β-d-glucopyranoside. Circular dichroism (CD) spectroscopy showed that the detergent-solubilized protein contained significant α-helical secondary structure. Proteolysis of the C-tail generated a trypsin-resistant core that was a mixture of primarily monomers and some dimers. We propose that MP dimers are stabilized by electrostatic interactions in the C terminus as well as hydrophobic interactions between putative transmembrane α-helical coiled coils.

scholarly journals Development of Tobacco Mosaic Virus Infection Sites in Nicotiana benthamiana

1999 ◽  
Vol 12 (2) ◽  
pp. 143-152 ◽  
Author(s):  
Judit Szécsi ◽  
Xin Shun Ding ◽  
Chae Oh Lim ◽  
Mohammed Bendahmane ◽  
Moo Je Cho ◽  
...  
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Nicotiana Benthamiana ◽  
Fluorescent Protein ◽  
Leading Edge ◽  
Subcellular Location ◽  
Cell Types ◽  
Adjacent Cell ◽  
In Planta ◽  
Cytoplasmic Bodies

To monitor infection of Nicotiana benthamiana by tobacco mosaic virus (TMV), leaves were inoculated with viral constructs expressing the green fluorescent protein (GFP) from jellyfish (Aequorea victoria) fused to the movement protein (MP) of TMV (MP:GFP) or as a free GFP in place of the coat protein (CP). Infection sites produced by TMV expressing the MP:GFP appeared as fluorescent rings larger in diameter and less fluorescent than fluorescent disks induced by constructs encoding free GFP. These results suggest that protein expression driven by the MP subgenomic promoter (sgp) initiates and ends earlier and is at lower level than that observed for proteins driven by the CP sgp. Similarly, analyses of cross sections through the infection sites revealed that in different cell types the accumulation of MP:GFP was regulated differently than the accumulation of free GFP. Immunocytochemistry and electron microscopy showed that near the leading edge of the fluorescent ring the MP:GFP and the viral 126 kDa and 183 kDa replicase proteins accumulated in paired cytoplasmic bodies that formed often on opposite sides of adjacent cell walls containing plasmodesmata. In the dimly fluorescent center of the rings the 126 kDa and 183 kDa proteins, but not the MP:GFP, were localized in unpaired cytoplasmic bodies containing ropelike, fibrillar structures. The paired bodies were similar to previously described viroplasms, while the unpaired bodies were similar to X-bodies. These data indicate that the accumulation of proteins expressed from different sgps of TMV has a specific spatial and temporal pattern in planta. In addition, the cytoplasmic bodies containing the 126 kDa and 183 kDa proteins are dynamic entities whose protein content and subcellular location change during infection.

scholarly journals The p122 Subunit of Tobacco Mosaic Virus Replicase Is a Potent Silencing Suppressor and Compromises both Small Interfering RNA- and MicroRNA-Mediated Pathways

2007 ◽  
Vol 81 (21) ◽  
pp. 11768-11780 ◽  
Author(s):  
Tibor Csorba ◽  
Aurelie Bovi ◽  
Tamás Dalmay ◽  
József Burgyán
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Nuclear Export ◽  
Rna Silencing ◽  
Plant Viruses ◽  
Silencing Suppressor ◽  
Small Interfering Rnas ◽  
In Planta ◽  
Interfering Rna

ABSTRACT One of the functions of RNA silencing in plants is to defend against molecular parasites, such as viruses, retrotransposons, and transgenes. Plant viruses are inducers, as well as targets, of RNA silencing-based antiviral defense. Replication intermediates or folded viral RNAs activate RNA silencing, generating small interfering RNAs (siRNAs), which are the key players in the antiviral response. Viruses are able to counteract RNA silencing by expressing silencing-suppressor proteins. It has been shown that many of the identified silencing-suppressor proteins bind long double-stranded RNA or siRNAs and thereby prevent assembly of the silencing effector complexes. In this study, we show that the 122-kDa replicase subunit (p122) of crucifer-infecting Tobacco mosaic virus (cr-TMV) is a potent silencing-suppressor protein. We found that the p122 protein preferentially binds to double-stranded 21-nucleotide (nt) siRNA and microRNA (miRNA) intermediates with 2-nt 3′ overhangs inhibiting the incorporation of siRNA and miRNA into silencing-related complexes (e.g., RNA-induced silencing complex [RISC]) both in vitro and in planta but cannot interfere with previously programmed RISCs. In addition, our results also suggest that the virus infection and/or sequestration of the siRNA and miRNA molecules by p122 enhances miRNA accumulation despite preventing its methylation. However, the p122 silencing suppressor does not prevent the methylation of certain miRNAs in hst-15 mutants, in which the nuclear export of miRNAs is compromised.

Expression of human hepatitis C virus core antigen in tobacco plants by tobacco mosaic virus-based vector system

2000 ◽  
Vol 45 (1) ◽  
pp. 44-48
Author(s):  
Aidong Han ◽  
Yule Liu ◽  
Li Xiao ◽  
Liangyi Kang ◽  
Yuman Zhang ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Vector System ◽  
Core Antigen ◽  
Tobacco Plants ◽  
Virus Core ◽  
Human Hepatitis

Engineered Tobacco mosaic virus mutants with distinct physical characteristics in planta and enhanced metallization properties

2011 ◽  
Vol 157 (1) ◽  
pp. 35-46 ◽  
Author(s):  
Anan Kadri ◽  
Edgar Maiß ◽  
Nadja Amsharov ◽  
Alexander M. Bittner ◽  
Sinan Balci ◽  
...  
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Physical Characteristics ◽  
In Planta

Quantitative Measurements on the Ion Etching of TMV

1973 ◽  
Vol 31 ◽  
pp. 336-337
Author(s):  
Irwin Bendet ◽  
Nabil Rizk
Keyword(s):  
Electron Microscope ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Ion Current ◽  
Beam Diameter ◽  
Ion Etching ◽  
Preliminary Results ◽  
Quantitative Measurements ◽  
Monitoring Devices

Preliminary results reported last year on the ion etching of tobacco mosaic virus indicated that the diameter of the virus decreased more rapidly at 10KV than at 5KV, perhaps reaching a constant value before disappearing completely.In order to follow the effects of ion etching on TMV more quantitatively we have designed and built a second apparatus (Fig. 1), which incorporates monitoring devices for measuring ion current and vacuum as well as accelerating voltage. In addition, the beam diameter has been increased to approximately 1 cm., so that ten electron microscope grids can be exposed to the beam simultaneously.

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