Participation of Chitin-Binding Peroxidase Isoforms in the Wilt Pathogenesis of Cotton

Abstract

Specific chitin-binding isozymes of peroxidase (POX) play an important role in pathogenesis of plant diseases caused by fungi. We studied the dynamics of peroxidase activity in two varieties of cotton (Gossypium hirsutum L.); one was susceptible and the other resistant to the plant pathogen Verticillium dahliae. After infection with strongly and weakly virulent isolate of V. dahliae, we observed a correlation between the level of seedling tissue lesion and peroxidase activity. Thus, the first POX activity was observed in all infected plants 2 hours after inoculation, but POX activity of the resistant variety rapidly increased and maximized 3 days after infection, while POX activity in the susceptible variety showed a slow increase that continued to increase during the remaining 8 days of experimental observation. The increase of POX activity in the susceptible variety after infection may be explained by progressive fungal colonization of cotton tissues leading to irreversible senescence. Microscopic examination of plant tissues supports this hypothesis. The more virulent isolate caused more necrosis and significantly more POX activity than the mildly virulent in both susceptible and resistant plants. Control plants showed no changes in POX activity; however, the POX activity in the control resistant varieties was higher than the control susceptible varieties. These findings indicate the potential utilization of chitin binding POX as a biochemical tool to guide breeding programs to increase resistance to V. dahliae.

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E. Pshenichnov, N. Khashimova, A. Akhunov, Z. Golubenko and R. Stipanovic, "Participation of Chitin-Binding Peroxidase Isoforms in the Wilt Pathogenesis of Cotton," American Journal of Plant Sciences, Vol. 2 No. 1, 2011, pp. 43-49. doi: 10.4236/ajps.2011.21005.

Conflicts of Interest

The authors declare no conflicts of interest.

References

[1] N. Benhamou, “Elicitor-Induced Plant Defense Pathways,” Trends in Plant Science, Vol. 1, No. 7, July 1996, pp. 233-240.
[2] C. C. Lin and C. H. Kao, “Abscisic Acid Induced Changes in Cell Wall Peroxidase Activity and Hydrogen Peroxide Level in Roots of Rice Seedlings,” Plant Science, Vol. 160, No. 2, 2001, pp. 323-329. doi:10.1016/S0168-9452(00)00396-4
[3] L. C. Van Loon, “Induced Resistance in Plants and Role of Pathogenesis-Related Proteins,” European Journal of Plant Pathology, Vol. 103, 1997, pp. 735-765. doi:10.1023/A:1008638109140
[4] R. Hammerschmidt and J. Kuc, “Lignification as a Mechanism for Induced Systemic Resistance of Cucumber,” Physiological and Molecular Plant Pathology, Vol. 20, 1982, pp. 61-71. doi:10.1016/0048-4059(82)90024-8
[5] A. A. Aver’yanov, V. P. Lapikova, O. N. Nikolaev and A. I. Stepanov, “Active Oxygen-Associated Control of Rice Blast Disease by Riboflavin and Roseoflavin,” Biochemistry (Moscow), Vol. 65, No. 11, November 2000, pp. 1292-1298.
[6] G. P. Bolwell, K. A. Blee, V. S. Butt, P. R. Davies, S. L. Gardner, C. Gerrich, F. Minilaeva, E. G. Rowntree and P. Woitaszek, “Recent Advances in Understanding the Origin of the Apoplastic Oxidative Burst in Plant Cells,” Free Radical Research, Vol. 31, December 1999, pp. 137-145. doi:10.1080/10715769900301431
[7] C. S. Bestwick, I. R. Brown, M. H. R. Bennett and J. M. Mansfield, “Localization of Hydrogen Peroxidase Accumulation during the Hypersensitive Reaction of Lettuce Cells to Pseudomonas syringae pv. phaseolicola,” The Plant Cell, Vol. 9, No. 2, February 1997, pp. 209-221.
[8] K. E. Hammond-Kosak and J. D. Jones, “Resistant Gene- Dependent Plant Defense Responses,” The Plant Cell, Vol. 8, No. 10, October 1996, pp. 1773-1791.
[9] I. V. Maksimov, E. A. Cherepanova, I. E. Akhmetova and R. M. Khairullin, “Contribution of Chitin and Its Oligomers to the Induced Resistance of Plants against Phytopathogens,” Agricultural Chemistry, Vol. 8, 2004, pp. 77-89.
[10] C. Schweikert, A. Liszkay and P. Schopher, “Polysaccharide Degradation by Fenton Reaction- or Peroxidase- Gene-Rated Hydroxyl Radicals in Isolated Plant Cell Walls,” Phytochemistry, Vol. 61, No. 1, September 2002, pp. 31-35. doi:10.1016/S0031-9422(02)00183-8
[11] C. Dunand, M. Tognolli, M. Meyer, P. Simon and C. Penel, “Identification and Characterization of Ca2+ — Pectate Binding Peroxidase in Arabidopsis thailiana,” Journal of Plant Physiology, Vol. 159, No. 11, November 2002, pp. 1165-1171. doi:10.1078/0176-1617-00768
[12] P. Bonatti, P. Medeghini, G. Lorenzini, R. Formasiero, R. Boroni, C. Nali and E. Sgarbi, “Cytochemical Detection of Cell Wall Bound Peroxidase in Rust Infected Broad Bean Leaves,” Journal of Phytopathology, Vol. 140, No. 4, April 1994, pp. 319-325. doi:10.1007/BF02980704
[13] Sh. I. Ibragimov, “Catalogue of Cotton Varieties. Vol. 2,” Tashkent, Uzbekistan, 1993.
[14] Z. Golubenko, A. Akhunov, N. Khashimova, Yu. Beresneva, E. Mustakimova, F. Ibragimov, N. Abdurashidova and R. Stipanovic, “Induction of Peroxidase as a Disease Resistance Response in Resistant (Hibiscus trionum) and Susceptible (Althea armeniaca) in the Family Malvaceae,” Phytoparasitica, Vol. 35, No. 4, August 2007, pp. 401-413. doi:10.1007/BF02980704
[15] O. N. Lowry, N. Rosebrouhg and R. I. Randall, “Protein Measurement with the Folin Phenol Reagent,” Biolgical Chemistry, Vol. 193, November 1951, pp. 265-275.
[16] H. Z. Zheng, C. L. Cui, Yu. Zhang, D. Wang, Yu. Jing and K. Y. Kim, “Active Changes of Lignification-Related Enzymes in Pepper Response to Glomus Introduces and/or Phytophthoracapsici,” Journal of Zhejiang University Science, Vol. 6B, No. 8, July 2005, pp. 778-786. doi:10.1631/jzus.2005.B0778
[17] F. Passardi, C. Penel and C. Dunand, “Performing the Paradoxical: How Plant Peroxidase Modify the Cell Wall,” Trends in Plant Science, Vol. 9, No. 11, November 2004, pp. 534-540.
[18] P. Kawalleck, E. Schmelzer, K. Hahlbrock and I. E. Somssich, “Two Pathogen-Responsive Genes in Parsley Encode a Tyrosine-Rich Hydroxyproline Glycoprotein (HRGP) and Anionic Peroxidase,” Molecular and General Genetics, Vol. 247, No. 4, 1995, pp. 444-452. doi:10.1007/BF00293146

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