GRAPEVINE FANLEAF VIRUS PDF

GRAPEVINE FANLEAF VIRUS PDF

Infection by Grapevine fanleaf nepovirus (GFLV), a bipartite RNA virus of positive polarity belonging to the Comoviridae family, causes extensive cytopathic. The specific transmission of Grapevine fanleaf virus by its nematode vector Xiphinema index is solely determined by the viral coat protein. There are plenty of plant viruses that no one has heard of, but few are as widely known as grapevine fanleaf virus. Learn how to identify a sick.

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Fanleaf DegenerationPurdue University. Such parallelism is not unexpected since CPMV and GFLV belong to the same family and share many common features, among them a similar genome organization 2. The arrowheads in panels B, C, E, and F indicate the perinuclear viral compartment.

N, nucleus; Nu, nucleolus.

For Cowpea mosaic virus CPMVvirus-induced accumulation of vesicles derived from the endomembrane system was described as early as by de Zoeten et al. Although some fanlewf centers were found in the ER-rich perinuclear region, many of them remained peripheral.

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Tubular structures involved in movement of cowpea mosaic virus are also formed in infected cowpea protoplasts. The VPg-containing perinuclear aggregates and punctate dsRNA labeling are indicated in panel N by full arrowheads and in panel O by arrows. Try asking one of our Experts. Crystal structure of Grapevine Fanleaf Virus capsid.

In the first syndrome, infectious malformations, the vines may be stunted or show reduced vigor. BFA and cerulenin treatment. Grapevine fanleaf degeneration disease is caused by the grapevine fanleaf virus GFLVa member of the nepovirus group. In the case of poliovirus, it was shown that specific viral proteins were responsible for vesicle formation 6762 and that formation of the poliovirus replication complex is a process that requires coupled grzpevine translation, vesicle production, and viral RNA synthesis The coat protein derives from RNA2 [5] and forms the icosahedral capsid of 60 identical protein subunits.

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The fluorescent conjugates Alexa-fluor or coupled to goat anti-rabbit, goat anti-guinea pig, or goat anti-mouse immunoglobulin G IgG; referred to as A or A, respectively were from Molecular Probes Eugene, Oreg.

At 48 h postelectroporation, protoplasts were fixed with glutaraldehyde as follows. ISEM of sucrose gradient fractions. Yellow mottling may sometimes accompany foliar deformations.

Genome organization of grapevine fanleaf nepovirus RNA2 deduced from the K polyprotein P2 in vitro cleavage products. At the mid stage of infection, large cortical aggregates formed, leading to a completely disrupted cortical ER 49 as for GFLV. Several plant viruses belonging to different groups, such as tobamoviruses 30bromoviruses 50potyviruses 59and comoviruses 11similarly appear to strongly modify the endomembrane compartments.

Ultrathin sections 90 nm were stained with uranyl acetate and lead citrate.

Intracellular distribution fajleaf poliovirus proteins and the induction of virus specific cytoplasmic structures. Polyclonal anti-VPg antibodies named anti-VPg were raised in rabbits against a synthetic peptide corresponding to the VPg sequence and purified by immunoaffinity chromatography against the VPg peptide Observations were done under an epifluorescence microscope Nikon Eclipse E with adequate filters. The ER aggregates and anti-VPg labeling colocalized perfectly as shown by the yellow signal obtained upon merging the two pictures Fig.

These contained VPg either as polyprotein precursors involved in RNA replication or as a final maturation product associated with viral RNA and also double-stranded viral replicative forms and neosynthesized viral RNA, which confirmed their direct involvement in GFLV replication. Author information Article notes Copyright and License information Disclaimer. Three tobacco T-BY2 cell grapevime were used throughout this study: To compare the distribution of the viral proteins involved in replication with that of proteins involved in movement and encapsidation, we analyzed the intracellular distribution of the movement protein 2B MP and the coat protein 2C CPboth of which are dispensable for replication The 2C protein was predominantly found in the perinuclear viral compartment Fig.

Consistent with its function in cell-to-cell movement, the movement protein was generally detected at the cell periphery at 48 hpi, fnaleaf after its release from the precursor polyprotein. To further refine the analysis of GFLV replication sites, the ultrastructural organization of the perinuclear aggregates containing the viral products was studied by electron microscopy on infected protoplasts Fig. These typical foliar symptoms resemble a fan, hence, the name of the virus and the disease Figure 1.

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In addition, by using transgenic T-BY2 protoplasts expressing green fluorescent protein in the endoplasmic reticulum ER or in the Golgi apparatus GAwe could directly show that GFLV replication induced a depletion of the cortical ER, together with a condensation and redistribution of ER-derived membranes, to generate the viral compartment.

Grapevine Fanleaf Degeneration Disease – eXtension

Since no CP labeling was observed along the intact part of the tubules, virions were probably inaccessible to antibodies there, as already observed with CPMV It infects grapeviecausing chlorosis of the leaves and lowering the fruit quality.

The membranes were then incubated with goat anti-rabbit IgG A or goat gapevine IgG B and C coupled to horseradish peroxidase and revealed by chemiluminescence. The sedimentation of Golgi Fig. Structural organization of poliovirus RNA replication is mediated by viral proteins of the P2 genomic region.

Finally, coat protein was also sometimes observed within the nucleoplasm Fig. For FDA, the parameters were as follows: Sucrose ggapevine fractionation and analysis. Three-dimensional reconstruction from CLSM image stack was obtained by using the surface rendering software Bitplane, Zurich, Switzerland.

PDB entry 2y26 [1] Virus classification Group: By using this site, you agree to the Terms of Use vvirus Privacy Policy. Panel J is a 2. Changing patterns of localization of the tobacco mosaic virus movement protein and replicase to the endoplasmic reticulum and microtubules during infection.