Abstract
The effects of Bipolaris sorokiniana inoculation on accumulation of hydrogen peroxide and changes in the activities of superoxide dismutase (SOD), catalase (CAT), non-specific peroxidase (PX) and β-1,3-glucanase enzymes in leaves of differentially resistant spring barley and meadow fescue were investigated in this study. Hydrogen peroxide accumulated slightly in inoculated barley leaves 24 hours after inoculation, and its accumulation after 48 hours of pathogenesis remained week around sites of infection. In leaves of fescue, which is more resistant to B. sorokiniana, accumulation of H2O2 was faster and stronger in comparison to barley. A slight increase in SOD activity was observed only in infected fescue. Catalase activity in infected barely leaves decreased significantly 48 hours after inoculation, while in fescue-infected plants CAT activity, following a slight decrease, remained similar to the control values. PX activity was considerable lower in inoculated barley leaves after 6 hours, but at 24 and 48 hours after inoculation its activity increased significantly compared to the control. In inoculated fescue leaves activity of PX was higher at 6 and 24 hours compared to the control, while at 48 hours PX activity was strongly inhibited. β-1,3-Glucanase activity in inoculated barley plants did not differ from that of the control, while in infected fescue leaves it increased significantly 48 hours after inoculation. Based on the results, we suggest that the strong accumulation of H2O2, changes in antioxidant levels, together with the significant increase of β-1,3-Glucanase activity in infected fescue leaves, plays an important role in fescue’s greater resistance to B. sorokiniana.
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Abbreviations
- CAT:
-
catalase
- DAB:
-
3,3-Diaminobenzidine
- HR:
-
hypersensitive response
- NBT:
-
nitroblue tetrazolium
- PDA:
-
potato dextrose agar
- PX:
-
non-specific peroxidase
- SOD:
-
superoxide dismutase
- ROS:
-
reactive oxygen species
- TEMED:
-
N,N,N′,N′-tetramethyl-ethylenediamine
- Tris:
-
Tris(hydroxymethyl)amino-methane
References
Aebi, H. 1984. Catalase in vitro. Meth. Enzymol. 105:121–126.
Anuratha, C.S., Zen, K.C., Cole, K.C., Mew, T., Muthukrishnan, S. 1996. Induction of chitinase and β -1,3-glucanases in Rhizoctonia solani — infected rice plants: Isolation of an infection-related chitinase cDNA clone. Physiol. Plant. 97:39–46.
Apel, K., Hirt, H. 2004. Reactive oxygen species: Metabolism, oxidative stress and signal transduction. Annu. Rev. Plant Biol. 55:373–399.
Barna, B., Fodor, J., Pogány, M., Király, Z. 2003. Role of reactive oxygen species and antioxidants in plant disease resistance. Pest Manag. Sci. 59:459–464.
Beauchamp, C., Fridovich, I. 1971. Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 44:276–287.
Benhamu, N., Broglie, K., Broglie, R., Chet, I. 1993. Antifungal effect of bean endochitinase on Rhizoctonia solani: Ultrastructure changes and cytochemical aspects of chitin breakdown. Can. J. Microbiol. 39:318–328.
Bestwick, C.S., Brown, I.R., Mansfield, J.W. 1998. Localized changes in peroxidase activity accompany hydrogen peroxide generation during the development of a nonhost hypersensitive reaction in lettuce. Plant Physiol. 118:1067–1078.
Bolwell, G.P., Bindschedler, L.V., Blee, K., Butt, V.S., Davies, D.R., Gardner, S.L., Gerrish, C., Minibayeva, F. 2002. The apoplastic oxidative burst in response to biotic stress in plants: A three-component system. J. Exp. Bot. 53:1367–1376.
Bradford, M. 1976. A rapid and sensitive method for the quantification of microgram quantitaties of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248–254.
Fodor, J., Gullner, G., Ádám, A.L., Barna, B., Kőmíves, T., Király, Z. 1997. Local and systemic responses of antioxidants to tobacco mosaic virus infection and to salicylic acid in tobacco: Role in systemic acquired resistance. Plant Physiol. 114:1443–1451.
Gönner, M., Schlösser, E. 1993. Oxidative stress in interaction between Avena sativa L. and Drechslera spp. Physiol. Molec. Plant Pathol. 42:221–234.
Hammond-Kosack, K.E., Jones, J. 1996. Resistance gene-dependent plant defense response. Plant Cell 8:1773–1791.
Jongedijk, E., Tigelaar, H., Roekel van, J.S.C., Bres-Vloemans, S.A., Dekker, I., Elzen van der, P.J.M. Cornelissen, B.J.C., Melchers, L.S. 1995. Synergistic activity of chitinases and β -1,3-glucanases enhances fungal resistance in transgenic tomato plants. Euphytica 85:173–180.
Király, Z., El-Zahaby, H., Galal, A., Abdou, S., Ádám, A., Barna, B., Klement, Z. 1993. Effect of oxy free radicals on plant pathogenic bacteria and fungi and on some plant diseases. In: Mózsik, Gy. Emerit, I., Fehér, J., Matkovics, B., Vincze, Á. (eds), Oxygen Free Radicals and Scavengers in the Natural Sciences. Akadémiai Kiadó, Budapest, pp. 9–19.
Kumar, J., Schäfer, P., Hückelhoven, R., Langen, G., Baltruschat, H., Stein, E., Nagarajan, S., Kogel, K.-H. 2002. Bipolaris sorokiniana, a cereal pathogen of global concern: Cytological and molecular approaches towards better control. Mol. Plant Pathol. 3:185–195.
Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685.
Lamb, C., Dixon, R.A. 1997. The oxidative burst in plant disease resistance. Ann. Rev. Plant Physiol. Plant Molec. Biol. 48:251–275.
Lintle, M., van der Westhuizen, A.J. 2002. Glycoproteins from Russian wheat aphid infested wheat induce defence responses. Z. Naturforsch. 57:867–873.
van Loon, L.C., Rep, M., Pieterse, C.M. 2006. Significance of inducible defense-related proteins in infected plants. Annu. Rev. Phytopathol. 44:135–162.
Mauch, F., Mauch-Mani, B., Boller, T. 1988. Antifungal hydrolases in pea tissue II. Inhibition of fungal growth by combinations of chitinase and β -1,3-glucanase. Plant Physiol. 88:936–942.
Mehdy, M.C. 1994. Active oxygen species in plant defense against pathogens. Plant Physiol. 105:467–472.
Mittler, R. 2002. Oxidative stress, antioxidants and stress tolerance. Trends Plant Sci. 7:405–410.
Nelson, N. 1944. A photometric adaptation of the Somogyi method for the determination of glucose. J. Biol. Chem. 153:375–380.
Płażek, A., Dubas, E. 2005. Activation of phenylpropanoid pathway and catalase in leaves of barley and meadow fescue infected by Bipolaris sorokiniana (Sacc.) Shoem. In: Zwierzykowski, Z., Kosmala, A. (eds), Recent Advances in Genetic and Breeding of the Grasses. Institute of Plant Genetics, Polish Academy of Sciences, Poznañ, Poland; Centre of Excellence in Plant Agrobiology and Molecular Genetics, pp. 197–202.
Pıażek, A., Rapacz, M. 2000. The intensity of respiration and heat emission from seedlings of Festuca pratensis (Hud.) and Hordeum vulgare L. during pathogenesis caused by Bipolaris sorokiniana (Sacc.) Shoem. Acta Physiol. Plant. 22:25–30.
Pıażek, A., Żur, I. 2003. Cold-induced plant resistance to necrotrophic pathogens and antioxidant enzyme activities and cell membrane permeability. Plant Sci. 164:1019–1028.
Profotová, B., Burketová, L., Valentová, O. 2007. Chitinase isozymes induced by TYMV and Leptosphaeria maculans during compatible and incompatible interaction with Brassica napus. Biol. Plant. 51:507–513.
Ryan, C.A. 1988. Oligosaccharides as recognition signals for the expression of defensive genes in plants. Biochem. 27:8879–8883.
Somogyi, M. 1952. Notes of sugar determination. J. Biol. Chem. 195:19–23.
Stintzi, A., Heitz, T., Prasad, V., Wiedemann-Merdinoglu, S., Kauffmann, S., Geoffroy, P., Legrand, M., Fritig, B. 1993. Plant “pathogenesis-related” proteins and their role in defense against pathogens. Biochimie 75:687–706.
Thordal-Christensen, H., Zhang, Z., Wei, Y., Collinge, D.B. 1997. Subcellular localization of H 2 O 2 in plants. H 2 O 2 accumulation in papillae and hypersensitive response during the barley — powdery mildew interaction. Plant J. 11:1187–1194.
Vranová, E., Inzé, D., Van Breusegem, F. 2002. Signal transduction during oxidative stress. J. Exp. Bot. 53:1227–1236.
Wang, Y., Kausch, A.P., Chandlee, J.M., Luo, H., Ruemmele, B.A., Browning, M., Jacksen, N., Goldsmith, M.R. 2003. Co-transfer and expression of chitinase, glucanase, and bar genes in creeping bentgrass for conferring fungal disease resistance. Plant Sci. 165:497–506.
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Płażek, A., Skoczowski, A., Hura, K. et al. Accumulation of H2O2 and changes in activities of antioxidative enzymes and β-1,3-glucanase in barley and meadow fescue leaves attacked by Bipolaris sorokiniana. CEREAL RESEARCH COMMUNICATIONS 37, 399–408 (2009). https://doi.org/10.1556/CRC.37.2009.3.9
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DOI: https://doi.org/10.1556/CRC.37.2009.3.9