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  • 1
    Electronic Resource
    Electronic Resource
    Metabolic reprogramming in plant innate immunity: the contributions of phenylpropanoid and oxylipin pathways (2004)
    Oxford, UK; Malden , USA : Munksgaard International Publishers
    Immunological reviews 198 (2004), S. 0 
    Details
    ISSN: 1600-065X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Summary:  In their environment, plants interact with a multitude of living organisms and have to cope with a large variety of aggressions of biotic or abiotic origin. To survive, plants have acquired, during evolution, complex mechanisms to detect their aggressors and defend themselves. Receptors and signaling pathways that are involved in such interactions with the environment are just beginning to be uncovered. What has been known for several decades is the extraordinary variety of chemical compounds the plants are capable to synthesize, and many of these products are implicated in defense responses. The number of natural products occurring in plants may be estimated in the range of hundreds of thousands, but only a fraction have been fully characterized. Despite the great importance of these metabolites for plant and also for human health, our knowledge about their biosynthetic pathways and functions is still fragmentary. Recent progress has been made particularly for phenylpropanoid and oxylipin metabolism, which are emphasized in this review. Both pathways are involved in plant resistance at several levels: by providing building units of physical barriers against pathogen invasion, by synthesizing an array of antibiotic compounds, and by producing signals implicated in the mounting of plant resistance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.0105-2896.2004.0129.x
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  • 2
    Electronic Resource
    Electronic Resource
    Scopoletin expression in elicitor-treated and tobacco mosaic virus-infected tobacco plants (2002)
    Oxford, UK : Blackwell Science, Ltd
    Physiologia plantarum 115 (2002), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Localized acquired resistance (LAR) characterizes a narrow zone of living cells expressing strong defense responses and surrounding cells undergoing a hypersensitive response (HR). In Samsun NN tobacco plants, tissues undergoing tobacco mosaic virus-induced or elicitor-induced LAR exhibit a strong blue fluorescence under UV light. We have shown that scopoletin and its glucoside, scopolin, accounted for the fluorescence: (1) both compounds were identified after extraction and purification by thin layer and high performance liquid chromatography; (2) there was a strict correlation between the occurrence of fluorescence and accumulation of high amounts of scopoletin; and (3) infiltration of commercial scopoletin caused a similar fluorescence to that occurring in LAR tissues. There was a 20-fold increase in scopoletin levels in LAR tissues compared to tissues treated with a non-HR dose of elicitor, while PR1 protein accumulated in similar amounts in both types of tissues. Scopoletin was able to suppress the elicitor-induced HR only when co-infiltrated with very low HR-dose of elicitor. These two observations suggested that, although scopoletin alone would not be able to control the development of the HR through its known antioxidant activity, it may nevertheless participate to such function of LAR tissues in combination with other antioxidant molecules.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.2002.1150208.x
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and characterization of six pathogenesis-related (PR) proteins of Samsun NN tobacco (1990)
    Springer
    Plant molecular biology 14 (1990), S. 381-390 
    Details
    ISSN: 1573-5028
    Keywords: Nicotiana tabacum cv. Samsun NN ; tobacco mosaic virus ; PR proteins ; purification ; serology ; thaumatin-like proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The purification to homogeneity of pathogenesis-related (PR) proteins R and S from Nicotiana tabacum cv. Samsun NN leaves has been achieved by using a combination of conventional and high-performance chromatographic supports. The same procedure allowed the purification and the characterization of four other proteins which displayed some properties characteristic of tobacco PR proteins and were shown to accumulate in tobacco leaves in response to virus infection. They can be, therefore, considered as new tobacco PR proteins which we designate as PR-s1,-s2,-r1 and-r2. The relative electrophoretic mobilities (Rf) under non-denaturing conditions were estimated to 0.30 for PR-r1 and-r2, 0.25 for Pr-R, 0.20 for PR-s1 and-s2 and 0.15 for PR-S. On SDS gels PR proteins R and S possessed the same apparent molecular weight (M r 24000) as did PR-proteins s1 and r1 (M r 14500) and PR-s2 and-r2 (M r 13000). However, proteins s1, s2, r1 and r2 had identical electrophoretic mobilities on SDS gels when the loading sample buffer contained no reducing agent. Polyclonal antisera were raised against PR proteins R and S and used in immunoblotting experiments. Proteins R and S were shown to be serologically closely related. No cross-reaction was detected with any of the four new tobacco PR proteins r1, r2, s1 and s2 or with the previously described PR proteins, i.e. PR-1a,-1b,-1c,-2,-N,-O,-P and-Q.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00028774
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  • 4
    Electronic Resource
    Electronic Resource
    Purification of tobacco O-methyltransferases by affinity chromatography and estimation of the rate of synthesis of the enzymes during hypersensitive reaction to virus infection (1988)
    Springer
    Planta 176 (1988), S. 36-41 
    Details
    ISSN: 1432-2048
    Keywords: Hypersensitivity ; Lignification ; O-methyltransferase ; Nicotiana (enzyme synthesis during TMV infection) ; Tobacco mosaic virus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The three tobacco (Nicotiana tabacum L.) S-adenosyl-L-methionine: o-diphenol-O-methyltransferases (OMTs; EC 2.1.1.6) were purified to homogeneity by affinity chromatography on adenosine-agarose. Amounts and catalytic actities of the enzymes were measured in tobacco leaves during the hypersensitive reaction to tobacco mosaic virus. The drastic increase in activity of each enzyme upon infection was shown to arise from the accumulation of enzymatic protein with constant specific enzymatic activity. Rates of OMT synthesis were determined from pulse-labeling experiments with L-[14C]leucine injected into the leaves. The specific radioactivities of the homogenous enzymes were compared in healthy and tobacco mosaic virus-infected tobacco. The results demonstrated that increase in OMT amounts is a consequence of de novo synthesis of the enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00392477
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  • 5
    Electronic Resource
    Electronic Resource
    Purification and characterization of 8 of the pathogenesis-related proteins in tobacco leaves reacting hypersensitively to tobacco mosaic virus (1986)
    Springer
    Plant molecular biology 6 (1986), S. 69-80 
    Details
    ISSN: 1573-5028
    Keywords: biochemical characterization ; high-performance liquid chromatography ; hypersensitive reaction ; Nicotiana tabacum ; pathogenesis-related proteins ; purification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Leaves of tobacco plants (Nicotiana tabacum cv. Samsun NN) which are reacting hypersensitively to infection with tobacco mosaic virus contain 10 major pathogenesis-related (PR) proteins which are absent, or present in small amounts in uninfected leaves. We describe here a preparative procedure of purification of the tobacco PR-proteins which involves a combination of conventional and high-performance liquid chromatography. The separation and isolation of the proteins were based on differences in net charge at different pH values, in isoelectric point and in apparent molecular weight. This procedure led to the purification to homogeneity of 8 PR-proteins, as shown by polyacrylamide slab gel electrophoresis (PAGE) of the purified proteins under denaturing and non-denaturing conditions. These were the 3 well-known proteins PR-1a,-1b and-1c, and 5 other major PR-proteins, called PR-2,-N,-O,-P and-Q, according to the nomenclature of Van Loon (39). None of the purified PR-proteins gave a positive Schiff reaction for carbohydrate content. Molecular weight determinations from gel permeation chromatography and from sodium dodecyl sulphate (SDS)-PAGE indicated that all 8 PR-proteins were monomers and that three groups could be distinguished among them. The first group is the PR-1 group containing PR-1a,-1b and-1c (12000 MW), the second consists of PR-P and PR-Q (14000 MW) and the third of PR-2, PR-N and PR-O (25000 MW). In the PR-1 group, PR-1a can be distinguished clearly from the two other members on denaturing slab gels containing both SDS and urea.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00027300
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