In vitro antifungal activity and mechanism of action of chitinase against four plant pathogenic fungi

Journal of Basic Microbiology

Volumn 48, Issue 4, 2008, Pages 293-301

  Yan, RuiXiang ^a,b   Hou, JianHua ^a   Ding, DongFeng ^a   Guan, WenQqiang ^b   Wang, CuiYan ^a   Wu, ZhiQiang ^a   Li, MingGang ^a  

^a NANKAI UNIVERSITY   (China)

^b National Engineering and Technology Research Centre for Agricultural Product Freshness   (China)

Author keywords

Antifungal activity; Chitinase; Mechanism plant pathogens

Indexed keywords

ASPERGILLUS NIGER; BOTRYOTINIA SQUAMOSA; BOTRYTIS; FUNGI; PICHIA PASTORIS; PYTHIUM; PYTHIUM APHANIDERMATUM; RHIZOPUS; RHIZOPUS STOLONIFER;

ANTIFUNGAL AGENT; CHITINASE; RECOMBINANT PROTEIN;

ARTICLE; CHEMISTRY; DRUG EFFECT; ENZYMOLOGY; FUNGUS; GENETICS; INFRARED SPECTROSCOPY; ISOLATION AND PURIFICATION; MICROBIOLOGY; MOLECULAR CLONING; PICHIA; PLANT; RICE; SCANNING ELECTRON MICROSCOPY; ULTRASTRUCTURE;

ANTIFUNGAL AGENTS; CHITINASE; CLONING, MOLECULAR; FUNGI; MICROSCOPY, ELECTRON, SCANNING; ORYZA SATIVA; PICHIA; PLANTS; RECOMBINANT PROTEINS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 54049087813     PISSN: 0233111X     EISSN: 15214028     Source Type: Journal    
DOI: 10.1002/jobm.200700392     Document Type: Article

References (33)

1. Mitsuhiro, U., Miki, K. and Tomoye, Y., 2003. A novel type of family 19 chitinase from Aeromonas sp. No. 10S-24: Cloning, sequence, expression, and the enzymatic properties. Eur. J. Biochem., 270, 2513-2520.
2. Flach, J., Pilet, P.E. and Jolles, P., 1992. What's new in chitinase research? Experientia, 48, 701-716.
3. Ancillo, G., Witte, B., Schmelzer, E. and Kombrink, E., 1999. A distinct member of the basic (class I) chitinase gene family in potato is specifically expressed in epidermal cells. Plant Mol. Biol., 39, 1137-1151.
4. Lotan, T., Or, N. and Fluhr, R., 1989. Pathogenesis-related proteins are developmentally regulated in tobacco flowers. Plant Cell, 1, 881-887.
5. Samac, D.A. and Shah, D.M., 1991. Developmental and pathogen-induced activation of the Arabidopsis acidic chitinase promoter. Plant Cell, 3, 1063-1072.
6. Van Hengel, A.J., Guzzo, F., Van Kammen, A. and Vries, S.C., 1998. Expression pattern of the carrot EP3 endochitinase genes in suspension cultures and in developing seeds. Plant Physiol., 117, 43-53.
7. Graham, L.S. and Sticklen, M.B., 1994. Plant chitinases. Can. J. Bot., 72, 1057-1083.
8. Kombrink, E. and Somssich, I.E., 1997. Pathogenesis-related proteins and plant defense. In: The Mycota, Vol. V Part A: Plant Relationships (Carroll G. and Tudzynski P. eds.), The Mycota., 5, 107-128.
9. Collinge, D.B., Kragh, K.M., Mikkelsen, J.D., Nielsen, K.K., Rasmussen, U. and Vad, K., 1993. Plant chitinases. Plant J., 3, 31-40.
10. Yanai, K., Tanaka, N., Kojima, N., Horiuchi, H., Ohta, A. and Takagi, M., 1992. Purification of two chitinases from Rhizopus obligosporus and isolation and sequencing of the encoding genes. J. Bacteriol., 174, 7398-7406.
11. Datta, K., Koukolíková-Nicola, Z., Baisakh, N., Oliva, N. and Datta, S.K., 2000. Agrobacterium-mediated engineering for sheath blight resistance of indica rice cultivars from different ecosystems. Theor. Appl. Genet., 100, 832-839.
12. Jones, J.D.G., Dean, C., Gidoni, D., Gilbert, D. and Lee, R., 1988. Expression of bacterial chitinase protein in tobacco leaves using two photosynthetic gene promoters. Mol. Genet. Genom., 212, 536-542.
13. Suslow, T.V., Matsubara, D., Jones, J. and Lee, R., Dunsmuir, P. 1988. Effect of expression of bacterial chitinase on tobacco susceptibility to leaf brown spot. Phytopathology, 78, 1556.
14. Broglie, K., Chet, I., Holliday, M., Cressman, R., Biddle, P. et al., 1991. Transgenic plants with enhanced resistance to the fungal pathogen Rhizoctonia solani. Science, 254, 1194-1197.
15. Terakawa, T., Takaya, N., Horiuchi, N. and Koike, M., 1997. A fungal chitinase gene from Rhizopus oligosporus confers antifungal activity to transgenic tobacco. Plant Cell Rep., 16, 439-443.
16. Vierheilig, H., Alt, M., Lange, J., Gut-Rella, M., Wiemken, A. and Boller, T., 1995. Colonization of transgenic tobacco constitutively expressing pathogenesis-related proteins by the vesiculararbuscular mycorrhizal fungus Glomus mosseae. Appl. Environ. Microbiol., 61, 3031-3034.
17. Arlorio, M., Ludwig, A., Boller, T., Mischiati, P. and Bonfante, P., 1991. Effects of chitinase and β-1,3-glucanase from pea on the growth of saprophytic and mycorrhizal fungi. Giornale Botanico Italiano, 125, 956-958.
18. Huang, J.K., Wen, L. and Swegle, M., 1991. Nucleotide sequence of a rice genomic clone that encodes a class I endochitinase. Plant Mol. Biol., 16, 479-480.
19. Scorer, A., Clare, J., McCombie, R., Romanos, A. and Sreekrishma, K., 1994. Rapid selection using G418 of high copy number transformants of Pichia pastoris for high-level foreign gene expression. Biotechnology, 12, 181-184.
20. Boller, T. and Mauch, F., 1988. Colorimetric assay for chitinase. Method Enzymol., 161, 430-435.
21. Melent'ev, A.I., Aktuganov, G.E. and Galimzyanova, N.F., 2001. The role of chitinase in the antifungal activity of Bacillus sp. 739. Microbiology, 70, 548-552.
22. Lin, Z.L. and Huang, X.L., 2000. Modern Microbiology and Experimental Technique. Beijing: Science Press.
23. Perez-Mendoza, J., Throne, J.E., Dowell, F.E. and Baker, J.E., 2003. Detection of insect fragments in wheat flour by near-infrared spectroscopy. J. Stored Prod. Res., 39, 305-312.
24. Cárdenas, G., Cabrera, G., Taboada, E. and Miranda, S.P., 2004. Chitin characterization by SEM, FTIR, XRD, and 13C cross polarization/mass angle spinning NMR. J. Appl. Polymer Sci., 93, 1876-1885.
25. Jiang, T.D., 2003. Chitin. Beijing: Chemical Industry Press.
26. Schlumbaum, A., Mauch, F., Vögeli, U. and Boller, T., 1986. Plant chitinases are potent inhibitors of fungal growth. Nature, 324, 365-367.
27. Mauch, F., Mauch-Mani, B. and 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.
28. Ludwig, A. and Boller, T., 1990. A method for the study of fungal growth inhibition by plant proteins. FEMS Microbiol. Lett., 69, 61-66.
29. Sela-Buurlage, M.B., Ponstein, A.S. and Bres-Vloemans, S.A., 1993. Only specific tobacco (Nicotiana tabacum) chitinases and β-1,3-glucanase exhibit antifungal activity. Plant Physiol., 101, 857-863.
30. Sleigh, M.A., 1989. Protozoa and Other Protists, p. 342. New York, USA: Chapman and Hall.
31. Feofilova, E.P., 2001. The kingdom fungi: heterogeneity of physiological and biochemical properties and relationships with plants, animals, and prokaryotes. Appl. Biochem. Microbiol., 37, 124-137.
32. Neuhaus, J.M., Sticher, L., Meins, F. and Boller, T., 1991. A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole. Proc. Natl. Acad. Sci., 88, 10362-10366.
33. Boller, T., 1993. Antimicrobial functions of the plant hydrolases, chitinase and β-1,3-glucanase. In: B. Fritig, M. Legrand (eds.), Mechanisms of Plant Defense Responses, pp. 391-400. Dordrecht, The Netherlands: Kluywer Academic Publishers.