Complementation of a potato virus X mutant mediated by bombardment of plant tissues with cloned viral movement protein genes.

SYu, Morozov; On, Fedorkin; Jüttner, G.; Schiemann, Joachim; Baulcombe, David C.; Jg, Atabekov

doi:10.1099/0022-1317-78-8-2077

Cited by 110 publications

(98 citation statements)

References 45 publications

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“…On rare occasions, GFP was detected in two or more adjacent cells in tobacco or wheat leaves (Table 1). Occasions of GFP fluorescence in adjacent cells were reported in previous studies and might be due to simultaneous delivery of plasmids to neighbouring cells during bombardment (Itaya et al, 1997;Krishnamurthy et al, 2002;Mitra et al, 2003;Morozov et al, 1997;Yang et al, 2000).…”

Section: Cell-to-cell Movement Of Sbwmv Proteinsmentioning

confidence: 92%

Evidence that the 37 kDa protein of Soil-borne wheat mosaic virus is a virus movement protein

Melcher

Doss

et al. 2003

Journal of General Virology

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Experiments were conducted to determine if the 37 kDa protein (37K) of Soil-borne wheat mosaic virus (SBWMV) is a virus movement protein. First, evidence was obtained that indicated that 37K has the ability to move from cell to cell, similar to other virus movement proteins (MPs). Plasmids containing the GFP gene fused to the SBWMV 37K, the coat protein (CP) or the CP readthrough domain (RT) ORFs were delivered by biolistic bombardment to wheat and tobacco leaves. In wheat leaves, cell-to-cell movement of GFP-37K was observed, while GFP, GFP-CP and GFP-RT accumulated primarily in single cells. All fusion proteins accumulated in single cells in tobacco leaves. Thus, cell-to-cell movement is a specific property of 37K that occurs in SBWMV host plants. Subcellular accumulation of 37K was studied using SBWMV-infected and 37K-expressing transgenic wheat. In infected and transgenic wheat leaves, 37K accumulated in the cell wall, similar to other virus MPs, and in aggregates in the cytoplasm. Phylogenetic studies were conducted to compare the furovirus 37K proteins with members of the 30K superfamily of virus MPs. Amino acid sequences of the furovirus 37K proteins were aligned with the MPs from 43 representative viruses. The furovirus 37K proteins were found to reside in a clade that also contained the dianthovirus MPs. Combined, these data suggest that SBWMV 37K is probably a virus MP.

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Section: Cell-to-cell Movement Of Sbwmv Proteinsmentioning

confidence: 92%

Evidence that the 37 kDa protein of Soil-borne wheat mosaic virus is a virus movement protein

Melcher

Doss

et al. 2003

Journal of General Virology

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“…After incubation at -208C for 1 h, the samples were centrifuged at 2000g for 30 s and washed carefully three times with absolute ethanol. Fullgrown leaves were detached from 6-to 8-week-old N. benthamiana plants, placed on moist Whatman paper in a Petri dish, and inoculated by particle bombardment using the PDS-100 system (Bio-Rad) as described (Morozov et al, 1997).…”

Section: Transient Protein Expression In Leaf Cells From Vectors Intrmentioning

confidence: 99%

Control of Nuclear and Nucleolar Localization of Nuclear Inclusion Protein a of Picorna-LikePotato virus AinNicotianaSpecies

2009

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The multifunctional nuclear inclusion protein a (NIa) of potyviruses (genus Potyvirus; Potyviridae) accumulates in the nucleus of virus-infected cells for unknown reasons. In this study, two regions in the viral genome-linked protein (VPg) domain of NIa in Potato virus A (PVA) were found to constitute nuclear and nucleolar localization signals (NLS) in plant cells (Nicotiana spp). Amino acid substitutions in both NLS I (residues 4 to 9) and NLS II (residues 41 to 50) prevented nuclear localization, whereas mutations in either single NLS did not. Mutations in either NLS, however, prevented nucleolar localization and prevented or diminished virus replication in protoplasts, accumulation in infected plant tissues, and/or systemic movement in plants. One NLS mutant was partially complemented by the wild-type VPg expressed in transgenic plants. Furthermore, NLS I controlled NIa accumulation in Cajal bodies. The VPg domain interacted with fibrillarin, a nucleolar protein, and depletion of fibrillarin reduced PVA accumulation. Overexpression of VPg in leaf tissues interfered with cosuppression of gene expression (i.e., RNA silencing), whereas NLS I and NLS II mutants, which exhibited reduced nuclear and nucleolar localization, showed no such activity. These results demonstrate that some of the most essential viral functions required for completion of the infection cycle are tightly linked to regulation of the NIa nuclear and nucleolar localization.

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“…However, underlying shared aspects of the movement process have been revealed by the finding that movement of TGB1-deficient PVX can be rescued by the 30K MP (Morozov et al, 1997) and that TGB1 can rescue movement of 30K MP-deficient Odontoglossum ringspot virus, a tobamovirus related to TMV (Ajjikuttira et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Experimental and bioinformatic evidence that raspberry leaf blotch emaravirus P4 is a movement protein of the 30K superfamily

Chen

Karlin

et al. 2013

Journal of General Virology

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Emaravirus is a recently described genus of negative-strand RNA plant viruses. Emaravirus P4 protein localizes to plasmodesmata, suggesting that it could be a viral movement protein (MP). In the current study, we showed that the P4 protein of raspberry leaf blotch emaravirus (RLBV) rescued the cell-to-cell movement of a defective potato virus X (PVX) that had a deletion mutation in the triple gene block 1 movement-associated protein. This demonstrated that RLBV P4 is a functional MP. Sequence analyses revealed that P4 is a distant member of the 30K superfamily of MPs. All MPs of this family contain two highly conserved regions predicted to form b-strands, namely b1 and b2. We explored by alanine mutagenesis the role of two residues of P4 (Ile106 and Asp127) located in each of these strands. We also made the equivalent substitutions in the 29K MP of tobacco rattle virus, another member of the 30K superfamily. All substitutions abolished the ability to complement PVX movement, except for the I106A substitution in the b1 region of P4. This region has been shown to mediate membrane association of 30K MPs; our results show that it is possible to make non-conservative substitutions of a well-conserved aliphatic residue within b1 without preventing the membrane association or movement function of P4.

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Complementation of a potato virus X mutant mediated by bombardment of plant tissues with cloned viral movement protein genes.

Cited by 110 publications

References 45 publications

Evidence that the 37 kDa protein of Soil-borne wheat mosaic virus is a virus movement protein

Evidence that the 37 kDa protein of Soil-borne wheat mosaic virus is a virus movement protein

Control of Nuclear and Nucleolar Localization of Nuclear Inclusion Protein a of Picorna-LikePotato virus AinNicotianaSpecies

Experimental and bioinformatic evidence that raspberry leaf blotch emaravirus P4 is a movement protein of the 30K superfamily

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