Plasmodesmata and intercellular transport of viral RNA

2007 ◽  
Vol 35 (1) ◽  
pp. 142-145 ◽  
Author(s):  
C. Hofmann ◽  
A. Sambade ◽  
M. Heinlein
Keyword(s):  
Cell Wall ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Plant Cell Wall ◽  
Movement Protein ◽  
Cell Communication ◽  
Viral Rna ◽  
Intercellular Transport ◽  
Cytoplasmic Bridges ◽  
Spread Of Infection

Cell-to-cell communication in plants involves the symplastic trafficking of informational protein and RNA macromolecules through cytoplasmic bridges in the plant cell wall known as plasmodesmata. Viruses exploit this route for the spread of infection and are used as a model to study the mechanisms by which macromolecules are targeted to the pore. Studies using tobacco mosaic virus have led to the identification of host components that participate in plasmodesmal targeting of viral RNA and movement protein.

scholarly journals Challenging the Role of Microtubules in Tobacco Mosaic Virus Movement by Drug Treatments Is Disputable

2006 ◽  
Vol 80 (13) ◽  
pp. 6712-6715 ◽  
Author(s):  
Mark Seemanpillai ◽  
Rabab Elamawi ◽  
Christophe Ritzenthaler ◽  
Manfred Heinlein
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Viral Rna ◽  
Virus Movement ◽  
Direct Role ◽  
Microtubule Inhibitors ◽  
Microtubule Polymerization ◽  
Drug Treatments

ABSTRACT The movement protein (MP) of Tobacco mosaic virus interacts with microtubules during infection. Although this interaction is correlated with the function of MP in the cell-to-cell transport of viral RNA, a direct role of microtubules in the movement process was recently challenged by studies involving the treatment of plants with inhibitors of microtubule polymerization. Here, we report evidence suggesting that such treatments may not efficiently disrupt all microtubules. Thus, results obtained from studies using microtubule inhibitors may have to remain open to interpretation with regard to the involvement of microtubules in viral RNA trafficking.

scholarly journals Tobacco mosaic virus: a pioneer to cell–to–cell movement

1999 ◽  
Vol 354 (1383) ◽  
pp. 637-643 ◽  
Author(s):  
Vitaly Citovsky
Keyword(s):  
Cell Wall ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Cell Movement ◽  
Host Cells ◽  
Specific Cell ◽  
Viral Movement Protein ◽  
Rna Molecules ◽  
Rna Complexes

Cell–to–cell movement of tobacco mosaic virus (TMV) is used to illustrate macromolecular traffic through plant intercellular connections, the plasmodesmata. This transport process is mediated by a specialized viral movement protein, P30. In the initially infected cell, P30 is produced by transcription of a subgenomic RNA derived from the invading virus. Presumably, P30 then associates with a certain proportion of the viral RNA molecules, sequestering them from replication and mediating their transport into neighbouring uninfected host cells. This nucleoprotein complex is targeted to plasmodesmata, possibly via interaction with the host cell cytoskeleton. Prior to passage through a plasmodesma, the plasmodesmal channel is dilated by the movement protein. It is proposed that targeting of P30–TMV RNA complexes to plasmodesmata involves binding to a specific cell wall–associated receptor molecule. In addition, a cell wall–associated protein kinase, phosphorylates P30 at its carboxy–terminus and minimizes P30–induced interference with plasmodesmatal permeability during viral infection.

scholarly journals Replication of Tobacco Mosaic Virus on Endoplasmic Reticulum and Role of the Cytoskeleton and Virus Movement Protein in Intracellular Distribution of Viral RNA

1999 ◽  
Vol 147 (5) ◽  
pp. 945-958 ◽  
Author(s):  
Paloma Más ◽  
Roger N. Beachy
Keyword(s):  
In Situ Hybridization ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Viral Rna ◽  
Pharmacological Agents ◽  
Intracellular Targeting ◽  
Cytoplasmic Filaments ◽  
Infected Cells

Little is known about the mechanisms of intracellular targeting of viral nucleic acids within infected cells. We used in situ hybridization to visualize the distribution of tobacco mosaic virus (TMV) viral RNA (vRNA) in infected tobacco protoplasts. Immunostaining of the ER lumenal binding protein (BiP) concurrent with in situ hybridization revealed that vRNA colocalized with the ER, including perinuclear ER. At midstages of infection, vRNA accumulated in large irregular bodies associated with cytoplasmic filaments while at late stages, vRNA was dispersed throughout the cytoplasm and was associated with hair-like protrusions from the plasma membrane containing ER. TMV movement protein (MP) and replicase colocalized with vRNA, suggesting that viral replication and translation occur in the same subcellular sites. Immunostaining with tubulin provided evidence of colocalization of vRNA with microtubules, while disruption of the cytoskeleton with pharmacological agents produced severe changes in vRNA localization. Mutants of TMV lacking functional MP accumulated vRNA, but the distribution of vRNA was different from that observed in wild-type infection. MP was not required for association of vRNA with perinuclear ER, but was required for the formation of the large irregular bodies and association of vRNA with the hair-like protrusions.

scholarly journals Intramolecular Complementing Mutations in Tobacco Mosaic Virus Movement Protein Confirm a Role for Microtubule Association in Viral RNA Transport

2002 ◽  
Vol 76 (8) ◽  
pp. 3974-3980 ◽  
Author(s):  
Vitaly Boyko ◽  
Jamie Alan Ashby ◽  
Elena Suslova ◽  
Jacqueline Ferralli ◽  
Oliver Sterthaus ◽  
...  
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Inclusion Bodies ◽  
Fluorescent Protein ◽  
Movement Protein ◽  
Microscopic Analysis ◽  
Viral Rna ◽  
Cell Transport ◽  
Substitution Mutations ◽  
Green Fluorescent

ABSTRACT The movement protein (MP) of Tobacco mosaic virus (TMV) facilitates the cell-to-cell transport of the viral RNA genome through plasmodesmata (Pd). A previous report described the functional reversion of a dysfunctional mutation in MP (Pro81Ser) by two additional amino acid substitution mutations (Thr104Ile and Arg167Lys). To further explore the mechanism underlying this intramolecular complementation event, the mutations were introduced into a virus derivative expressing the MP as a fusion to green fluorescent protein (GFP). Microscopic analysis of infected protoplasts and of infection sites in leaves of MP-transgenic Nicotiana benthamiana indicates that MPP81S-GFP and MPP81S;T104I;R167K-GFP differ in subcellular distribution. MPP81S-GFP lacks specific sites of accumulation in protoplasts and, in epidermal cells, exclusively localizes to Pd. MPP81S;T104I;R167K-GFP, in contrast, in addition localizes to inclusion bodies and microtubules and thus exhibits a subcellular localization pattern that is similar, if not identical, to the pattern reported for wild-type MP-GFP. Since accumulation of MP to inclusion bodies is not required for function, these observations confirm a role for microtubules in TMV RNA cell-to-cell transport.

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