Tobacco Mosaic Virus – a Model for Macromolecular Cell-to-Cell Spread

2007 ◽  
pp. 29-62 ◽  
Author(s):  
E. Waigmann ◽  
M. Curin ◽  
M. Heinlein
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Cell Spread

scholarly journals Tobacco mosaic virus (TMV) and potato virus X (PVX) coat proteins confer heterologous interference to PVX and TMV infection, respectively

2006 ◽  
Vol 87 (4) ◽  
pp. 1005-1012 ◽  
Author(s):  
A. A. Bazzini ◽  
S. Asurmendi ◽  
H. E. Hopp ◽  
R. N. Beachy
Keyword(s):  
Transgenic Plants ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Potato Virus ◽  
Quaternary Structure ◽  
Systemic Infection ◽  
Potato Virus X ◽  
Coat Proteins ◽  
Local Cell ◽  
Cell Spread

Replication of Potato virus X (PVX) was reduced in transgenic protoplasts that accumulated wild-type coat protein (CPWT) of Tobacco mosaic virus (TMV) or a mutant CP, CPT42W, that produced highly ordered states of aggregation, including pseudovirions. This reaction is referred to as heterologous CP-mediated resistance. However, protoplasts expressing a CP mutant that abolished aggregation and did not produce pseudovirions, CPT28W, did not reduce PVX replication. Similarly, in transgenic tobacco plants producing TMV CPWT or CPT42W, there was a delay in local cell-to-cell spread of PVX infection that was not observed in CPT28W plants or in non-transgenic plants. The results suggest that the quaternary structure of the TMV CP regulates the mechanism(s) of heterologous CP-mediated resistance. Similarly, transgenic protoplasts that produced PVX CP conferred transient protection against infection by TMV RNA. Transgenic plants that accumulated PVX CP reduced the cell-to-cell spread of infection and resulted in a delay in systemic infection following inoculation with TMV or TMV RNA. Heterologous CP-mediated resistance was characterized by a brief delay in systemic infection, whilst homologous CP-mediated resistance conferred reduced or no systemic infection.

scholarly journals Tobacco mosaic virus (TMV) Replicase and Movement Protein Function Synergistically in Facilitating TMV Spread by Lateral Diffusion in the Plasmodesmal Desmotubule of Nicotiana benthamiana

2008 ◽  
Vol 21 (3) ◽  
pp. 335-345 ◽  
Author(s):  
Dana Guenoune-Gelbart ◽  
Michael Elbaum ◽  
Guy Sagi ◽  
Amit Levy ◽  
Bernard L. Epel
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Protein Function ◽  
Fluorescent Protein ◽  
Lateral Diffusion ◽  
Integral Membrane Protein ◽  
Movement Proteins ◽  
Green Fluorescent ◽  
Cell Spread ◽  
Er Membrane

Virus spread through plasmodesmata (Pd) is mediated by virus-encoded movement proteins (MPs) that modify Pd structure and function. The MP of Tobacco mosaic virus (TMVMP) is an endoplasmic reticulum (ER) integral membrane protein that binds viral RNA (vRNA), forming a vRNA:MP:ER complex. It has been hypothesized that TMVMP causes Pd to dilate, thus potentiating a cytoskeletal mediated sliding of the vRNA:MP:ER complex through Pd; in the absence of MP, by contrast, the ER cannot move through Pd. An alternate model proposes that cell-to-cell spread takes place by diffusion of the MP:vRNA complex in the ER membranes which traverse Pd. To test these models, we measured the effect of TMVMP and replicase expression on cell-to-cell spread of several green fluorescent protein-fused probes: a soluble cytoplasmic protein, two ER lumen proteins, and two ER membrane-bound proteins. Our data support the diffusion model in which a complex that includes ER-embedded MP, vRNA, and other components diffuses in the ER membrane within the Pd driven by the concentration gradient between an infected cell and adjacent noninfected cells. The data also suggest that the virus replicase and MP function together in altering Pd conductivity.

scholarly journals A Dysfunctional Movement Protein of Tobacco mosaic virus Interferes with Targeting of Wild-Type Movement Protein to Microtubules

2001 ◽  
Vol 14 (7) ◽  
pp. 895-904 ◽  
Author(s):  
Guy Kotlizky ◽  
Aviva Katz ◽  
Jessica van der Laak ◽  
Vitaly Boyko ◽  
Moshe Lapidot ◽  
...  
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Fluorescent Protein ◽  
Movement Protein ◽  
Free System ◽  
Intracellular Targeting ◽  
Infected Cells ◽  
Green Fluorescent ◽  
Dependent Processes ◽  
Cell Spread

The Tobacco mosaic virus (TMV) movement protein (MPTMV) mediates cell-to-cell viral trafficking by altering properties of the plasmodesmata (Pd) in infected cells. During the infection cycle, MPTMV becomes transiently associated with endomembranes, microfilaments, and microtubules (MT). It has been shown that the cell-to-cell spread of TMV is reduced in plants expressing the dysfunctional MP mutant MPNT-1. To expand our understanding of the MP function, we analyzed events occurring during the intracellular and intercellular targeting of MPTMV and MPNT-1 when expressed as a fusion protein to green fluorescent protein (GFP), either by biolistic bombardment in a viral-free system or from a recombinant virus. The accumulation of MPTMV:GFP, when expressed in a viral-free system, is similar to MPTMV:GFP in TMV-infected tissues. Pd localization and cell-to-cell spread are late events, occurring only after accumulation of MP:GFP in aggregate bodies and on MT in the target cell. MPNT-1:GFP localizes to MT but does not target to Pd nor does it move cell to cell. The spread of transiently expressed MPTMV:GFP in leaves of transgenic plants that produce MPNT-1 is reduced, and targeting of the MPTMV:GFP to the cytoskeleton is inhibited. Although MPTMV:GFP targets to the Pd in these plants, it is partially impaired for movement. It has been suggested that MPNT-1 interferes with host-dependent processes that occur during the intracellular targeting program that makes MP movement competent.

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.

Tobacco Mosaic Virus-Infected Tissue

1985 ◽  
Vol 43 ◽  
pp. 510-511
Author(s):  
Egbert W. Henry
Keyword(s):  
Nicotiana Tabacum ◽  
Tobacco Mosaic Virus ◽  
Chlorogenic Acid ◽  
Mosaic Virus ◽  
Host Resistance ◽  
Oxidative Metabolism ◽  
Leaf Tissue ◽  
Vein Clearing ◽  
Basal Septum ◽  
Concentration Levels

Tobacco mosaic virus (TMV) infection has been studied in several investigations of Nicotiana tabacum leaf tissue. Earlier studies have suggested that TMV infection does not have precise infective selectivity vs. specific types of tissues. Also, such tissue conditions as vein banding, vein clearing, liquification and suberization may result from causes other than direct TMV infection. At the present time, it is thought that the plasmodesmata, ectodesmata and perhaps the plasmodesmata of the basal septum may represent the actual or more precise sites of TMV infection.TMV infection has been implicated in elevated levels of oxidative metabolism; also, TMV infection may have a major role in host resistance vs. concentration levels of phenolic-type enzymes. Therefore, enzymes such as polyphenol oxidase, peroxidase and phenylalamine ammonia-lyase may show an increase in activity in response to TMV infection. It has been reported that TMV infection may cause a decrease in o-dihydric phenols (chlorogenic acid) in some tissues.

Nitroxyl Modified Tobacco Mosaic Virus as a Metal-Free High-Relaxivity MRI and EPR Active Superoxide Sensor

2018 ◽  
Author(s):  
Madushani Dharmarwardana ◽  
André F. Martins ◽  
Zhuo Chen ◽  
Philip M. Palacios ◽  
Chance M. Nowak ◽  
...  
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Single Molecule ◽  
Biological Fluids ◽  
Cellular Respiration ◽  
Organic Radical ◽  
Paramagnetic Resonance ◽  
Metal Free ◽  
Disease States

Superoxide overproduction is known to occur in multiple disease states requiring critical care yet non-invasive detection of superoxide in deep tissue remains a challenge. Herein, we report a metal-free magnetic resonance imaging (MRI) and electron paramagnetic resonance (EPR) active contrast agent prepared by “click conjugating” paramagnetic organic radical contrast agents (ORCAs) to the surface of tobacco mosaic virus (TMV). While ORCAs are known to be reduced <i>in vivo</i> to an MRI/EPR silent state, their oxidation is facilitated specifically by reactive oxygen species—in particular superoxide—and are largely unaffected by peroxides and molecular oxygen. Unfortunately, single molecule ORCAs typically offer weak MRI contrast. In contrast, our data confirm that the macromolecular ORCA-TMV conjugates show marked enhancement for <i>T<sub>1</sub></i> contrast at low field (<3.0 T), and <i>T<sub>2</sub></i> contrast at high field (9.4 T). Additionally, we demonstrated that the unique topology of TMV allows for “quenchless fluorescent” bimodal probe for concurrent fluorescence and MRI/EPR imaging, which was made possible by exploiting the unique inner and outer surface of the TMV nanoparticle. <a>Finally, we show TMV-ORCAs do not respond to normal cellular respiration, minimizing the likelihood for background, yet still respond to enzymatically produced superoxide in complicated biological fluids like serum.</a>

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