Selected reactive oxygen species and antioxidant enzymes in common bean after Pseudomonas syringae pv. phaseolicola and Botrytis cinerea infection

• Autorzy: Nowogorska A. , Patykowski J.
• Języki publikacji: EN

Abstrakty

EN

Phaseolus vulgaris cv. Korona plants were inoculated with the bacteria Pseudomonas syringae pv. phaseolicola (Psp), necrotrophic fungus Botrytis cinerea (Bc) or with both pathogens sequentially. The aim of the experiment was to determine how plants cope with multiple infection with pathogens having different attack strategy. Possible suppression of the non-specific infection with the necrotrophic fungus Bc by earlier Psp inoculation was examined. Concentration of reactive oxygen species (ROS), such as superoxide anion (O₂⁻) and H₂O₂ and activities of antioxidant enzymes such as superoxide dismutase SOD), catalase (CAT) and peroxidase (POD) were determined 6, 12, 24 and 48 h after inoculation. The measurements were done for ROS cytosolic fraction and enzymatic cytosolic or apoplastic fraction. Infection with Psp caused significant increase in ROS levels since thebeginning of experiment. Activity of the apoplastic enzymes also increased remarkably at the beginning of experiment in contrast to the cytosolic ones. Cytosolic SOD and guaiacol peroxidase (GPOD) activities achieved the maximum values 48 h after treatment. Additional forms of the examined enzymes after specific Psp infection were identified; however, they were not present after single Bc inoculation. Subsequent Bc infection resulted only in changes of H₂O₂ and SOD that occurred to be especially important during plant–pathogen interaction. Cultivar Korona of common bean is considered to be resistant to Psp and mobilises its system upon infection with these bacteria. We put forward a hypothesis that the extent of defence reaction was so great that subsequent infection did not trigger significant additional response.

• Wydawca: -
• Czasopismo: Acta Physiologiae Plantarum
• Rocznik: 2015
• Tom: 37
• Numer: 01
• Opis fizyczny: Article: 1725 [10 p.], fig.,ref.

Twórcy

autor

Nowogorska A.

• Department of Plant Physiology and Biochemistry, Faculty of Biology and Environmental Protection, University of Lodz, Banacha 12/16, 90-237 Lodz, Poland

autor

Patykowski J.

• Department of Plant Physiology and Biochemistry, Faculty of Biology and Environmental Protection, University of Lodz, Banacha 12/16, 90-237 Lodz, Poland

Bibliografia

• AbuQamar S, Luo H, Laluk K, Mickelbart MV, Mengiste T (2009) Crosstalk between biotic and abiotic stress responses in tomato is mediated by the AIM1 transcription factor. Plant J 58:347–360
• AbuQamar S, Ajeb S, Sham A, Enan MR, Iratni R (2013) A mutation in the expansin-like A2 gene enhances resistance to necrotrophic fungi and hypersensitivity to abiotic stress in Arabidopsis thaliana. Mol Plant Pathol 14(8):813–827
• Adie BA, Pérez-Pérez J, Mm Pérez-Pérez, Godoy M, Sánchez-Serrano JJ, Schmelz EA, Solano R (2007) ABA is essentialsignal for plant resistance to pathogens affecting JA biosynthesis and the activation of defences in Arabidopsis. Plant Cell 19:1665–1681
• Alfano JR, Collmer A (1996) Bacterial pathogens in plants: life up against the wall. Plant Cell 8:1683–1698
• Baptista P, Martins A, Pais MS, Tavares RM, Lino-Neto T (2007) Involvement of reactive oxygen species during early stages of ectomycorrhiza establishment between Castanea sativa and Pisolithus tinctorius. Mycorrhiza 17:185–193
• Beauchamp C, Fridovich I (1971) Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem 44:276–287
• Beckers GJM, Spoel SH (2005) Fine-tuning plant defence signalling: salicylate versus jasmonate. Plant Biol 8:1–10
• Bolwell PP, Page A, Piślewska M, Wojtaszek P (2001) Pathogenic infection and the oxidative defences in plant apoplast. Protoplasma 217:20–32
• Bowler C, Flur R (2000) The role of calcium and activated oxygens as signals for controlling cross-tolerance. Trends Plant Sci 5:241–246
• Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254
• Burr SJ, Fry SF (2009) Extracellular cross-linking of maize arabinoxylans by oxidation of feruloyl esters to form oligoferuloyl esters and ether-like bonds. Plant J 58:554–567
• Capaldi DJ, Taylor KE (1983) A new peroxidase colour reaction: oxidative coupling of 3-methyl-2-benzothiazolinone hydrazone (MBTH) with its formaldehyde azine application to glucose and choline oxidases. Anal Biochem 129:329–336
• Creissen G, Firmin J, Freyer M, Kular B, Leyland N, Reynold H, Pastori G, Wellburn F, Baker N, Wellburn A, Mullineaux P (1999) Elevated glutathione biosynthetic capacity in the chloroplasts of transgenic tobacco paradoxically caused increased oxidative stress. Plant Cell 11:1277–1291
• Derksen H, Rampitsch C, Daayf F (2013) Signaling cross-talk in plant disease resistance. Plant Sci 207:79–87
• Dhindsa RS, Plumb-Dhindsa P, Thorpe TA (1981) Leaf senescence correlated with increased levels of membrane permeability and lipid peroxidation, and decreased levels of superoxide dismutase and catalase. J Exp Bot 32:93–101
• Doke N (1983) Involvement of superoxide anion generation in the hypersensitive response of potato tuber tissues to infection with an incompatible race of Phytophthora infestans and to the hyphal wall components. Physiol Plant Pathol 23:345–357
• Dorey S, Bailleul F, Saindrenan P, Fritig B, Kauffmann S (1998) Tobacco class I and II catalases are differentially expressed during elicitor induced hypersensitive cell death and localized acquired resistance. Mol Plant Microb Int 11:1102–1109
• Encina A, Fry SC (2005) Oxidative coupling of a feruloylarabinoxylan trisaccharide (FAXX) in the walls of living maize cells requires endogenous hydrogen peroxide and is controlled by a low-Mr apoplastic inhibitor. Planta 223:77–89
• Finiti I, Leyva MO, López-Cruz J, Calderan Rodrigues B, Vicedo B, Angulo C, Bennett AB, Grant M, Garcıa-Agustın P, González-Bosch C (2013) Functional analysis of endo-1,4-b-glucanases in response to Botrytis cinerea and Pseudomonas syringae reveals their involvement in plant–pathogen interactions. Plant Biol 15:819–831
• Flor HH (1971) Current status of the gene-for-gene concept. Annu Rev Phytopathol 9:275–296
• Garcia-Arenal F, Sagasta EM (1980) Scanning electron microscopy of Botrytis cinerea penetration of bean (Phaseolus vulgaris) hypocotyls. Phytopathol Z 99:37–42
• Glazebrook J (2005) Contrasting mechanisms of defense against biotrophic and necrotrophic pathogens. Annu Rev Phytopathol 43:205–227
• Goldberg R, Catesson AM, Czaninski Y (1983) Some properties of syringaldazine oxidase, a peroxidase specifically involved In the lignification processes. Z Pflanzenphysiol 110:267–279
• Huckelhoven R (2007) Cell wall-associated mechanisms of disease resistance and susceptibility. Annual Rev Phytopathol 45:101–127
• Imberty A, Goldberg R, Catesson AM (1985) Isolation and characterization of Populus isoperoxidases involved in the last step of lignification. Planta 164:221–226
• Koornneef A, Pieterse CMJ (2008) Cross talk in defense signalling. Plant Physiol 146:839–844
• Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685
• Laluk K, AbuQamar S, Mengiste T (2011) The Arabidopsis mitochondrial localized pentatricopeptide repeat protein PGN functions in defense against necrotrophic fungi and abiotic stress tolerance. Plant Physiol 156:2053–2068
• Lamb C, Dixon RA (1997) The oxidative burst in plant disease resistance. Annu Rev Plant Physiol Plant Mol Biol 48:251–275
• Lebeda A, Sedlarova M (2003) Cellular mechanisms involved in the expression of specificity in Lactuca spp–Bremia lactucae interactions. In: Hintum ThJL. Van-Lebeda A, Pink DAC, Schut JW (eds) Eucarpia leafy vegetables conference 2003. CGN, Wageningen, The Netherlands, pp 55–60
• Maehly AC, Chance B (1954) The assay of catalases and peroxidases. In: Glick D (ed) Methods of biochemical analysis. Willey, New York, pp 357–425
• Mayer AM, Staples RC, Gilad NL (2001) Mechanisms of survival of necrotrophic fungal plant pathogens in hosts expressing the hypersensitive response. Phytochemistry 58(1):33–41
• Mehdy MC (1994) Active oxygen species in plant defense against pathogens. Plant Physiol 105(2):467–472
• Mellersh DG, Foulds IV, Higgins VJ, Heath MC (2002) H2O2 plays different roles in determining penetration failure in three diverse plant–fungal interactions. Plant J 29:257–268
• Mengiste T, Chen X, Salmeron J, Dietrich R (2003) The BOTRYTIS SUSCEPTIBLE1 gene encodes an R2R3MYB transcription factor protein that is required for biotic and abiotic stress responses in Arabidopsis. Plant Cell 15:2551–2565
• Mika A, Boenisch MJ, Hopff D, Lu¨thje S (2010) Membrane-bound guaiacol peroxidases from maize (Zea mays L.) roots are regulated by methyl jasmonate, salicylic acid, and pathogen elicitors. J Exp Bot 61(3):831–841
• Oudgenoeg G, Dirksen E, Ingemann S, Hilhorst R, Gruppen H, Boeriu CG, Piersma SR, van Berkel WJH, Laane C, Voragen AGJ (2002) Horseradish peroxidase-catalyzed oligomerization of ferulic acid on a template of a tyrosine-containing tripeptide. J Biol Chem 24(277):21332–21340
• Passardi F, Cosio C, Penel C, Dunand C (2005) Peroxidases have more functions than a Swiss army knife. Plant Cell Rep 24:255–265
• Patykowski J (2008) Rola apoplastu w interakcji ros´lina—patogen po infekcji pomidora przez Botrytis cinerea. Wydawnictwo Uniwersytetu Łódzkiego, Łódź
• Polle A, Otter T, Seifert F (1994) Apoplastic peroxidases and lignification in needles of Norway Spruce (Picea abies). Plant Physiol 106:53–60
• Romero-Puertas MC, Rodríguez-Serrano M, Corpas FJ, Gómez M, Del Río LA, Sandalio LM (2004) Cadmium-induced subcellular accumulation of O₂⁻ and H2O2 in pea leaves. Plant Cell Environ 27:1122–1134
• Sakamoto A, Okumura T, Kaminaka H, Sumi K, Tanaka K (1995) Structure and differential response to abscisic acid of two promoters for the cytosolic copper/zinc-superoxide dismutase genes, SodCc1 and SodCc2, in rice protoplasts. FEBS Lett 358:62–66
• Schouten A, van Baarlen P, van Ka JA (2007) Phytotoxic Nep1-like proteins from the necrotrophic fungus Botrytis cinerea associate with membranes and the nucleus of plant cell. New Phytol 177:493–505
• Schwacke R, Hager A (1992) Fungal elicitors induce a transient release of active oxygen species from cultured spruce cells that is dependent on Ca₂⁺ and protein-kinase activity. Planta 187:136–141
• Sedlářová M, Lebeda A, Luhová L (2004) The role of active oxygen species in resistance of Lactuca spp. to Bremia lactucae. Acta Fytotech Zootech 7:272–274
• Shi J, Fu XZ, Peng T, Huang XS, Fan QJ, Liu JH (2010) Spermine pretreatment confers dehydration tolerance of citrus in vitro plants via modulation of antioxidative capacity and stomatal response. Tree Physiol 30:914–922
• Shlezinger N, Minz A, Gur Y, Hatam I, Dagdas YF, Talbot NJ, Sharo A (2011) Anti-apoptotic machinery protects the necrotrophic fungus Botrytis cinerea from host-induced apoptotic like cell death during plant infection. PLoS Pathog 7(8):e100218
• Takahama U (1995) Oxidation of hydroxycinnamic acid and hydroxycinnamyl alcohol derivatives by laccase and peroxidase. Interactions among p-hydroxyphenyl, guaiacyl and syringyl groups during the oxidation reactions. Physiol Plant 93:61–68
• Takahashi S, Seki M, Ishida J, Satou M, Sakurai T, Narusaka M, Kamiya A, Nakajima M, Enju A, Akimaya K, Yamaguchi-Shinozaki K, Shinozaki K (2004) Monitoring the expression profiles of genes induced by hyperosmotic, high salinity, and oxidative stress and abscisic acid treatment in Arabidopsis cell culture using a full length cDNA microarray. Plant Mol Biol 56:29–55
• Thaler JS, Owen B, Hoggins VJ (2004) The role of the jasmonate response in plant susceptibility to diverse pathogens with a range of lifestyles. Plant Physiol 135:1–9
• Thomma BPHJ, Eggermont K, Penninckx IAMA, Mauch-Mani B, Vogelsang R, Cammue BPA, Broekaert WF (1998) Separate jasmonate-dependent and salicylate-dependent defense-response pathways in Arabidopsis are essential for resistance to distinct microbial pathogens. Proc Natl Acad Sci USA 95:15107–15111
• Thordal-Christensen H, Zhang Z, Wei Y, Collinge DB (1997) Subcellular localization of H2O2 in plants. H2O2 accumulation in papillae and hypersensitive response during the barley–powdery mildew interaction. Plant J 11:1187–1194
• Van Baarlen P, Woltering EJ, Staats M, van Kan JAL (2007) Histochemical and genetic analysis of host and non-host interactions of Arabidopsis with three Botrytis species: an important role for cell death control. Mol Plant Pathol 8(1):41–54
• Welinder KG, Justesen AF, Kjaersgard IV, Jensen RB, Rasmussen SK, Jespersen HM, Duroux L (2002) Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana. Eur J Biochem 269:6063–6081
• Williamson B, Tudzynski B, Tudzynski P, van Kan JAL (2007) Botrytis cinerea: the cause of grey mould disease. Mol Plant Pathol 8:561–580
• Wojtaszek P (1997) Oxidative burst: an early plant response to pathogen infection. Biochem J 322:681–692

Identyfikatory

DOI

10.1007/s11738-014-1725-3