The symptom difference induced by Tobacco mosaic virus and Tomato mosaic virus in tobacco plants containing the N gene is determined by movement protein gene
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Tobamovirus
Movement protein
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Tobamovirus
Movement protein
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In a previous study, we isolated a new harpin protein, PopW, from the bacterium Ralstonia solanacearum ZJ3721 that can induce a hypersensitive response in tobacco, Nicotiana tabacum, leaves. In the current study, we demonstrate that, in a greenhouse experiment, PopW induced tobacco-acquired resistance against the Tobacco mosaic virus (TMV) with a biocontrol efficacy of 80.9 to 97.4% at a concentration as low as 25 μg/ml in both PopW-treated and neighboring leaves. The resistance induced by PopW is systemic acquired resistance mediated by salicylic acid, which was certified by the development of resistance being accompanied by the expression of the pathogenesis-related-1 gene (PR1) 8 h after PopW was sprayed onto the tobacco leaves. In addition, hydrogen peroxide began to accumulate 10 h after PopW spraying, peaking at 24 h with a maximum concentration of 1.97 μM/g fresh weight. The activities of phenylalanine ammonia lyase (EC4.3.1.5), polyphenoloxidase (EC1.14.18.1), and peroxidase (EC1.11.1.7) also increased, peaking at different times in the PopW-treated tobacco leaves. PopW also reduced the level of TMV disease in field trials with a biocontrol efficacy of 45.2%. Furthermore, PopW both increased tobacco yield (by 30.4 more than in control plants) and improved tobacco foliar quality, with an increase of 50.2% in the number of first-class tobacco leaves from treated compared with untreated plants. All of these results indicate that the new harpin protein PopW has the potential to be an effective biocontrol agent against TMV in tobacco.
Tobamovirus
Ralstonia solanacearum
Phenylalanine ammonia-lyase
Systemic Acquired Resistance
Bacterial wilt
Pathogenesis-related protein
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Transgenic tobacco plants expressing a gene encoding the tobacco mosaic virus (TMV) movement protein (30K) were studied using immunocytochemical techniques. The movement protein was shown to be localized within or on most of the plasmodesmata observed in the transformed plant. These results are consistent with the idea that the movement protein interacts with the plasmodesmata to facilitate the cell-to-cell spread of TMV.
Plasmodesma
Movement protein
Tobamovirus
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Movement protein
Tobamovirus
Tobacco etch virus
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Abstract The tomato Tm‐2 2 gene was considered to be one of the most durable resistance genes in agriculture, protecting against viruses of the Tobamovirus genus, such as tomato mosaic virus (ToMV) and tobacco mosaic virus (TMV). However, an emerging tobamovirus, tomato brown rugose fruit virus (ToBRFV), has overcome Tm‐2 2 , damaging tomato production worldwide. Tm‐2 2 encodes a nucleotide‐binding leucine‐rich repeat (NLR) class immune receptor that recognizes its effector, the tobamovirus movement protein (MP). Previously, we found that ToBRFV MP (MP ToBRFV ) enabled the virus to overcome Tm‐2 2 ‐mediated resistance. Yet, it was unknown how Tm‐2 2 remained durable against other tobamoviruses, such as TMV and ToMV, for over 60 years. Here, we show that a conserved cysteine (C68) in the MP of TMV (MP TMV ) plays a dual role in Tm‐2 2 activation and viral movement. Substitution of MP ToBRFV amino acid H67 with the corresponding amino acid in MP TMV (C68) activated Tm‐2 2 ‐mediated resistance. However, replacement of C68 in TMV and ToMV disabled the infectivity of both viruses. Phylogenetic and structural prediction analysis revealed that C68 is conserved among all Solanaceae‐infecting tobamoviruses except ToBRFV and localizes to a predicted jelly‐roll fold common to various MPs. Cell‐to‐cell and subcellular movement analysis showed that C68 is required for the movement of TMV by regulating the MP interaction with the endoplasmic reticulum and targeting it to plasmodesmata. The dual role of C68 in viral movement and Tm‐2 2 immune activation could explain how TMV was unable to overcome this resistance for such a long period.
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Movement protein
Plasmodesma
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Tobamovirus
Pathogenesis-related protein
Tobacco etch virus
Pathogenesis
Cauliflower mosaic virus
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ABSTRACT The tomato Tm-2 2 gene was considered one of the most durable resistance genes in agriculture, protecting against viruses of the Tobamovirus genus, such as Tomato mosaic virus (ToMV) and Tobacco mosaic virus (TMV). However, an emerging tobamovirus, Tomato brown rugose fruit virus (ToBRFV), has overcome Tm-2 2 , damaging tomato production worldwide. Tm-2 2 encodes a nucleotide-binding leucine-rich repeat (NLR) class immune receptor that recognizes its effector, the tobamovirus movement protein (MP). Previously, we found that ToBRFV MP (MP ToBRFV ) enabled the virus to overcome Tm-2 2 - mediated resistance. Yet, it was unknown how Tm-2 2 remained durable against other tobamoviruses, such as TMV and ToMV, for over 60 years. Here, we show that the presence of a conserved cysteine (C68) in the MP of TMV (MP TMV ) is both sufficient to trigger Tm-2 2 resistance and essential for viral movement. Substitution of MP ToBRFV amino acid H67 with the corresponding amino acid in MP TMV (C68) activated Tm-2 2 -medited resistance. However, replacement of C68 in TMV and ToMV disabled the infectivity of both viruses. Phylogenetic and structural prediction analysis revealed that C68 is conserved among all Solanaceae -infecting tobamoviruses except ToBRFV, and localizes to a predicted jelly-roll fold common to various MPs. Cell-to-cell, and subcellular movement analysis showed that C68 is required for the movement of TMV, by regulating the MP interaction with the endoplasmic reticulum and targeting it to plasmodesmata. The dual role of C68 in viral movement and Tm-2 2 immune activation could explain how TMV was unable to overcome this resistance for such a long period.
Tobamovirus
Movement protein
Plasmodesma
Mosaic virus
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Movement protein
Plasmodesma
Tobamovirus
Mosaic virus
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To fully understand vascular transport of plant viruses, the viral and host proteins, their structures and functions, and the specific vascular cells in which these factors function must be determined. We report here on the ability of various cDNA-derived coat protein (CP) mutants of tobacco mosaic virus (TMV) to invade vascular cells in minor veins of Nicotiana tabacum L. cv. Xanthi nn. The mutant viruses we studied, TMV CP-O, U1mCP15-17, and SNC015, respectively, encode a CP from a different tobamovirus (i.e., from odontoglossum ringspot virus) resulting in the formation of non-native capsids, a mutant CP that accumulates in aggregates but does not encapsidate the viral RNA, or no CP. TMV CP-O is impaired in phloem-dependent movement, whereas U1mCP15-17 and SNC015 do not accumulate by phloem-dependent movement. In developmentally-defined studies using immunocytochemical analyses we determined that all of these mutants invaded vascular parenchyma cells within minor veins in inoculated leaves. In addition, we determined that the CPs of TMV CP-O and U1mCP15-17 were present in companion (C) cells of minor veins in inoculated leaves, although more rarely than CP of wild-type virus. These results indicate that the movement of TMV into minor veins does not require the CP, and an encapsidation-competent CP is not required for, but may increase the efficiency of, movement into the conducting complex of the phloem (i.e., the C cell/sieve element complex). Also, a host factor(s) functions at or beyond the C cell/sieve element interface with other cells to allow efficient phloem-dependent accumulation of TMV CP-O.
Tobamovirus
Movement protein
Plasmodesma
Tobacco etch virus
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Plasmodesmata are cytoplasmic bridges be- tween plant cells thought to generally allow only the passage of small molecules and metabolites. However, large structures such as plant viruses also move from cell to cell via plasmodes- mata. In tobacco mosaic virus (TMV) infection a viral move- ment protein (TMV-MP) mediates viral spread. Here, a mi- croinjection assay is used to monitor the dynamics of TMV-MP function directly in wild-type plants. The results indicate that TMV-MP interacts with an endogenous plant pathway increas- ing plasmodesmal size exclusion limit to permit passage of 20-kDa dextrans. Furthermore, TMV-MP influences plas- modesmal size exclusion limit several cells distant from the inuection site, indicating either that TMV-MP itself crosses plasmodesmata or that TMV-MP induces a diffusable signal capable of dilating microchannels of plasmodesmata. The region of TMV-MP responsible for increasing plasmodesmal size exclusion limit was mapped to the carboxyl-terminal part of the 268-amino acid residue protein between amino acid residues 126 and 224.
Plasmodesma
Movement protein
Tobamovirus
Cowpea mosaic virus
Plant cell
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