scholarly journals Evidence for interaction between the 2a polymerase protein and the 3a movement protein of Cucumber mosaic virus

2005 ◽  
Vol 86 (11) ◽  
pp. 3171-3177 ◽  
Author(s):  
Min Sook Hwang ◽  
Sang Hyon Kim ◽  
Jeong Hyun Lee ◽  
Jung Myung Bae ◽  
Kyung Hee Paek ◽  
...  

The genome of Cucumber mosaic virus consists of three single-stranded RNA molecules, RNAs 1, 2 and 3. RNAs 1 and 2 encode the 1a and 2a proteins, respectively, which are necessary for replication of the viral genome and have been implicated in movement of the viral RNAs in plants. The 3a movement protein (MP), encoded by RNA 3, is essential for transferring the RNA genomes from infected cells to adjacent cells across the plasmodesmata. Far-Western analysis demonstrated that bacterially expressed 2a polymerase protein directly interacted with the MP. Interaction was confirmed in a yeast two-hybrid assay, and co-immunoprecipitation analysis showed that the MP interacted only with the 2a polymerase protein. A yeast three-hybrid assay showed that the 1a–2a protein interaction relevant for replicase complex formation was not affected by the MP. Although the MP has no affinity for the 1a protein, it interacted indirectly with the 1a protein via the 2a polymerase protein. These results suggest that the replicase complex may be involved in movement through its interaction with the MP.

PLoS ONE ◽  
2016 ◽  
Vol 11 (9) ◽  
pp. e0163320 ◽  
Author(s):  
Reenu Kumari ◽  
Surender Kumar ◽  
Lakhmir Singh ◽  
Vipin Hallan

1999 ◽  
Vol 354 (1383) ◽  
pp. 637-643 ◽  
Author(s):  
Vitaly Citovsky

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.


2007 ◽  
Vol 23 (4) ◽  
pp. 281-286 ◽  
Author(s):  
Jang-Kyun Seo ◽  
Sung-Hyun Hwang ◽  
Sung-Hwan Kang ◽  
Hong-Soo Choi ◽  
Su-Heon Lee ◽  
...  

2019 ◽  
Vol 29 (2) ◽  
pp. 219-230
Author(s):  
M. Siddiqur Rahman ◽  
K. Jahan ◽  
Ashfak Ahmed Sabuz ◽  
A.M. Akanda

Alteration of cellular components and host physiology due to five biotypes of Cucumber mosaic virus (CMV) were investigated to know the effects on ultimate growth and yield of chilli. Severe reduction of cellular components like chlorophyll-a (59.31%), chlorophyll-b (68.40%), total chlorophyll (63.20%) and β-carotene (51.14%) were observed in plant infected by mosaic and stunting (MoS) as compared to healthy plant. The ratio of RNA to DNA was increased in the infected leaves. The reduction of photosynthesis rate was found 6.32 to 17.10% in CMV infected plants as compared to healthy plants. Stomatal conductance and inter cellular CO2 was found lower in CMV infected plats. Considerable yield reduction (28.80 to 78.11%.) was found infected with five symptomatic isolate of CMV. The present findings indicate that multiplication of virus particles in the infected cells alter the biochemical compounds of cells that disrupt the physiological process which affect the growth and yield of chilli.


2002 ◽  
Vol 76 (7) ◽  
pp. 3554-3557 ◽  
Author(s):  
Emese Huppert ◽  
Dénes Szilassy ◽  
Katalin Salánki ◽  
Zoltán Divéki ◽  
Ervin Balázs

ABSTRACT A hybrid virus (CMVcymMP) constructed by replacing the movement protein (MP) of cucumber mosaic cucumovirus (CMV) with that of cymbidium ringspot tombusvirus (CymRSV) was viable and could efficiently spread both cell to cell and long distance in host plants. The hybrid virus was able to move cell to cell in the absence of functional CP, whereas CP-deficient CMV was restricted to single inoculated cells. In several Chenopodium and Nicotiana species, the symptom phenotype of the hybrid virus infection was clearly determined by the foreign MP gene. In Nicotiana debneyi and Nicotiana tabacum cv. Xanthi, the hybrid virus could move systemically, contrary to CymRSV.


2001 ◽  
Vol 75 (8) ◽  
pp. 3859-3872 ◽  
Author(s):  
Jin-Hyun Ahn ◽  
Yixun Xu ◽  
Won-Jong Jang ◽  
Michael J. Matunis ◽  
Gary S. Hayward

ABSTRACT The human cytomegalovirus (HCMV) major immediate-early protein IE2 is a nuclear phosphoprotein that is believed to be a key regulator in both lytic and latent infections. Using yeast two-hybrid screening, small ubiquitin-like modifiers (SUMO-1, SUMO-2, and SUMO-3) and a SUMO-conjugating enzyme (Ubc9) were isolated as IE2-interacting proteins. In vitro binding assays with glutathioneS-transferase (GST) fusion proteins provided evidence for direct protein-protein interaction. Mapping data showed that the C-terminal end of SUMO-1 is critical for interaction with IE2 in both yeast and in vitro binding assays. IE2 was efficiently modified by SUMO-1 or SUMO-2 in cotransfected cells and in cells infected with a recombinant adenovirus expressing HCMV IE2, although the level of modification was much lower in HCMV-infected cells. Two lysine residues at positions 175 and 180 were mapped as major alternative SUMO-1 conjugation sites in both cotransfected cells and an in vitro sumoylation assay and could be conjugated by SUMO-1 simultaneously. Although mutations of these lysine residues did not interfere with the POD (or ND10) targeting of IE2, overexpression of SUMO-1 enhanced IE2-mediated transactivation in a promoter-dependent manner in reporter assays. Interestingly, many other cellular proteins identified as IE2 interaction partners in yeast two-hybrid assays also interact with SUMO-1, suggesting that either directly bound or covalently conjugated SUMO moieties may act as a bridge for interactions between IE2 and other SUMO-1-modified or SUMO-1-interacting proteins. When we investigated the intracellular localization of SUMO-1 in HCMV-infected cells, the pattern changed from nuclear punctate to predominantly nuclear diffuse in an IE1-dependent manner at very early times after infection, but with some SUMO-1 protein now associated with IE2 punctate domains. However, at late times after infection, SUMO-1 was predominantly detected within viral DNA replication compartments containing IE2. Taken together, these results show that HCMV infection causes the redistribution of SUMO-1 and that IE2 both physically binds to and is covalently modified by SUMO moieties, suggesting possible modulation of both the function of SUMO-1 and protein-protein interactions of IE2 during HCMV infection.


1998 ◽  
Vol 10 (4) ◽  
pp. 525-537 ◽  
Author(s):  
Leila M. Blackman ◽  
Petra Boevink ◽  
Simon Santa Cruz ◽  
Peter Palukaitis ◽  
Karl J. Oparka

2001 ◽  
Vol 75 (17) ◽  
pp. 8045-8053 ◽  
Author(s):  
Hideaki Nagano ◽  
Kazuyuki Mise ◽  
Iwao Furusawa ◽  
Tetsuro Okuno

ABSTRACT Plant viruses have movement protein (MP) gene(s) essential for cell-to-cell movement in hosts. Cucumber mosaic virus (CMV) requires its own coat protein (CP) in addition to the MP for intercellular movement. Our present results using variants of both CMV and a chimeric Brome mosaic virus with the CMV MP gene revealed that CMV MP truncated in its C-terminal 33 amino acids has the ability to mediate viral movement independently of CP. Coexpression of the intact and truncated CMV MPs extremely reduced movement of the chimeric viruses, suggesting that these heterogeneous CMV MPs function antagonistically. Sequential deletion analyses of the CMV MP revealed that the dispensability of CP occurred when the C-terminal deletion ranged between 31 and 36 amino acids and that shorter deletion impaired the ability of the MP to promote viral movement. This is the first report that a region of MP determines the requirement of CP in cell-to-cell movement of a plant virus.


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