Studies on the Formation of Diffusion Barriers in Hypersensitive Hosts of Tobacco Mosaic Virus and the Role of Necrotization in the Formation of Diffusion Barriers as well as in the Localization of Virus Infections)

1976 ◽  
Vol 87 (4) ◽  
pp. 345-352 ◽  
Author(s):  
G. Schuster ◽  
M. Flemming
2005 ◽  
Vol 79 (4) ◽  
pp. 2549-2558 ◽  
Author(s):  
Meenu S. Padmanabhan ◽  
Sameer P. Goregaoker ◽  
Sheetal Golem ◽  
Haiymanot Shiferaw ◽  
James N. Culver

ABSTRACT Virus-infected plants often display developmental abnormalities that include stunting, leaf curling, and the loss of apical dominance. In this study, the helicase domain of the Tobacco mosaic virus (TMV) 126- and/or 183-kDa replicase protein(s) was found to interact with the Arabidopsis Aux/IAA protein PAP1 (also named IAA26), a putative regulator of auxin response genes involved in plant development. To investigate the role of this interaction in the display of symptoms, a TMV mutant defective in the PAP1 interaction was identified. This mutant replicated and moved normally in Arabidopsis but induced attenuated developmental symptoms. Additionally, transgenic plants in which the accumulation of PAP1 mRNA was silenced exhibit symptoms like those of virus-infected plants. In uninfected tissues, ectopically expressed PAP1 accumulated and localized to the nucleus. However, in TMV-infected tissues, PAP1 failed to accumulate to significant levels and did not localize to the nucleus, suggesting that interaction with the TMV replicase protein disrupts PAP1 localization. The consequences of this interaction would affect PAP1's putative function as a transcriptional regulator of auxin response genes. This is supported by gene expression data indicating that ∼30% of the Arabidopsis genes displaying transcriptional alterations in response to TMV contain multiple auxin response promoter elements. Combined, these data indicate that the TMV replicase protein interferes with the plant's auxin response system to induce specific disease symptoms.


2006 ◽  
Vol 80 (13) ◽  
pp. 6712-6715 ◽  
Author(s):  
Mark Seemanpillai ◽  
Rabab Elamawi ◽  
Christophe Ritzenthaler ◽  
Manfred Heinlein

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.


1999 ◽  
Vol 354 (1383) ◽  
pp. 603-611 ◽  
Author(s):  
John G. Shaw

In order to establish infections, viruses must be delivered to the cells of potential hosts and must then engage in activities that enable their genomes to be expressed and replicated. With most viruses, the events that precede the onset of production of progeny virus particles are referred to as the early events and, in the case of positive–strand RNA viruses, they include the initial interaction with, and the entry of, host cells and the release (uncoating) of the genome from the virus particles. Though the early events remain one of the more poorly understood areas of plant virology, the virus with which most of the relevant research has been performed is tobacco mosaic virus (TMV). In spite of this effort, there remains much uncertainty about the form or constituent of the virus that actually enters the initially invaded cell in a plant and about the mechanism(s) that trigger the subsequent uncoating (virion disassembly) reactions. A variety of approaches have been used in attempts to determine the fate of TMV particles that are involved in the establishment of an infection and these are briefly described in this review. In some recent work, it has been proposed that the uncoating process involves the bidirectional release of coat protein subunits from the viral RNA and that these activities may be mediated by cotranslational and coreplicational disassembly mechanisms.


Biochemistry ◽  
1965 ◽  
Vol 4 (1) ◽  
pp. 31-37 ◽  
Author(s):  
Charles L. Stevens ◽  
Max A. Lauffer

ACS Nano ◽  
2011 ◽  
Vol 5 (3) ◽  
pp. 1606-1616 ◽  
Author(s):  
Michael A. Bruckman ◽  
Carissa M. Soto ◽  
Heather McDowell ◽  
Jinny L. Liu ◽  
Banahalli R. Ratna ◽  
...  

2003 ◽  
Vol 84 (3) ◽  
pp. 727-732 ◽  
Author(s):  
E. M. Karger ◽  
O. Yu. Frolova ◽  
N. V. Fedorova ◽  
L. A. Baratova ◽  
T. V. Ovchinnikova ◽  
...  

Replication of tobacco mosaic virus (TMV) is connected with endoplasmic reticulum (ER)-associated membranes at early stages of infection. This study reports that TMV movement protein (MP)-specific protein kinases (PKs) associated with the ER of tobacco were capable of phosphorylating Thr104 in TMV MP. The MP-specific PKs with apparent molecular masses of about 45–50 kDa and 38 kDa were revealed by gel PK assays. Two types of mutations were introduced in TMV MP gene of wild-type TMV U1 genome to substitute Thr104 by neutral Ala or by negatively charged Asp. Mutation of Thr104 to Ala did not affect the size of necrotic lesions induced by the mutant virus in Nicotiana tabacum Xanthi nc. plants. Conversely, mutation of Thr to Asp mimicking Thr104 phosphorylation strongly inhibited cell-to-cell movement. The possible role of Thr104 phosphorylation in TMV MP function is discussed.


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