Antifungal activity of a plant cystatin

Molecular Plant-Microbe Interactions

Volumn 12, Issue 7, 1999, Pages 624-627

  Pernas, Mónica ^a   López Solanilla, Emilia ^a   Sánchez Monge, Rosa ^a   Salcedo, Gabriel ^a   Rodríguez Palenzuela, Pablo ^a  

^a UNIVERSIDAD POLITÉCNICA DE MADRID   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTATIN; ENZYME ACTIVITY; FUNGICIDAL ACTIVITY; PLANT METABOLISM; PLANT PATHOGEN INTERACTION; PROTEINASE; SECONDARY METABOLITE;

BOTRYTIS CINEREA; COLLETOTRICHUM GRAMINICOLA; SEPTORIA NODORUM; TRICHODERMA VIRIDE;

EID: 0345086457     PISSN: 08940282     EISSN: None     Source Type: Journal    
DOI: 10.1094/MPMI.1999.12.7.624     Document Type: Article

References (27)

1. Abe, K., Emory, Y., Kondo, H., Suzuki, K., and Arai, S. 1987. Molecular cloning of a cysteine proteinase inhibitor of rice (Oryzacystatin). J. Biol. Chem. 26:16793-16797.
2. Abe, M., Abe, K., Kuroda, M., and Arai, S. 1992. Corn kernel cysteine proteinase inhibitor as a novel cystatin superfamily member of plant origin. Eur. J. Biochem. 209:933-937.
3. Anastasi, A., Brown, M. A., Kembhavi, A. A., Nicklin, M., Sayers, C., Sunter, D., and Barret, A. J. 1983. Cystatin, a protein inhibitor of cysteine proteinases. Biochem. J. 211:129-138.
4. Barret, A. 1987. The cystatins: A new class of peptidase inhibitors. Trends Biochem. Sci. 12:193-196.
5. Barret, A. J., Khembhavi, A. A., Brown, M. A., Kirschke, H., Knight, C. G., Tamai, M, and Hanada, K. 1982. L-trans-epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem. J. 20:189-198.
6. Broekaert, W. F., Terras, F. R. G., Cammue, B. P. A., and Vanderleyden, J. 1990. An automated quantitative assay for fungal growth. FEMS Microbiol. Lett. 69:55-60.
7. García-Olmedo, F., Molina, A., Alamillo, J. M., and Rodriguez-Palenzuela, P. Plant defense peptides. Byopolymers-Peptide Sci. (In press.)
8. Georgopapadakou, N., and Smith, S. 1985. Chitin synthase in Candida albicans: Comparison of digitonin-permeabilized cells and spheroplast membranes. J. Bacteriol. 162:826-829.
9. Harrach, T., Eckert, K., Maurer, H. R, Machleidt, I., Machleidt, W., and Nuck, R. 1998. Isolation and characterization of two forms of an acidic bromelain stem proteinase. J. Protein Chem. 17:351-361.
10. Hines, M. E., Osuala, C. I., and Nielsen, S. S. 1991. Isolation and partial characterization of a soybean cystatin cysteine proteinase inhibitor of coleopteran digestive proteolytic activity. J. Agric. Food Chem. 39: 1515-1520.
11. Impoolsup, A., Bhumiratana, A., and Flegel, T. W. 1981. Isolation of alkaline and neutral proteases from Aspergillus flavus var. columnaris, a soy sauce Koji mold. Appl. Environ. Microbiol. 42:619-628.
12. Kamens, J., Paskind, M., Hugumin, M., Talanian, R. V., Allen, H., Banach, D., Bump, N., Johnston, C. G., Li, P., Mankovich, J. A., Terranova, M., and Ghayur, T. 1996. Identification and characterization of ICH-2, a novel member of the interleukin-1β-converting enzyme family of cysteine proteases. J. Biol. Chem. 270:15250-15266.
13. Kondo, H., Abe, K., Nishimura, I., Watanabe, H., Emory, Y., and Arai, S. 1990. Two distinct cystatin species in rice seeds with different specificities against cysteine proteinases. J. Biol. Chem. 265:15832-15837.
14. Kondo, H., Ijiri, S., Abe, K., Maeda, H., and Arai, S. 1992. Inhibitory effect of oryzacystatins and a truncation mutant on the replication of poliovirus in infected Vero cells. FEBS Lett. 299:48-50.
15. Leplé, J. C., Bonad-Bottino, M., Augustin, S., Pilate, G., Dumanois, V., Delplanque, A., Cornu, D., and Jouanin, L. 1995. Toxicity to Chrysomela tremulae (Coleoptera: Chrysomelidae) of transgenic poplars expressing a cysteine proteinase inhibitor. Mol. Breeding 1:319-328.
16. Liang, C., Brookhart, G., Feng, G. H., Reeck, G. R., and Kramer, K. J. 1991. Inhibition of digestive proteinases of stored grain coleoptera by oryzacystatin, a cysteine proteinase inhibitor from rice seed. FEBS Lett. 2:139-142.
17. Lorito, M., Broadway, R. M., Hayes, C. K., Woo, S. L., Noviello, C., Williams, D. L., and Harman, G. E. 1994. Proteinase inhibitors from plants as a novel class of fungicides. Mol. Plant-Microbe Interact. 7: 525-527.
18. Machida, S., and Saito, M. 1993. Purification and characterization of membrane-bound chitin synthase. J. Biol. Chem. 268:1702-1707.
19. Margis, R., Reis, E. M., and Villeret, V. 1998. Structural and phylogenetic relationships among plant and animal cystatins. Arch. Biochem. Biophys. 359:24-30.
20. Misaka, T., Kuroda, M., Iwabuchi, K., Abe, K., and Arai, S. 1996. Soyacystatin, a novel cysteine proteinase inhibitor in soybean, is distinct in protein structure and gene organization from other cystatins of animal and plant origin. Eur. J. Biochem. 240:609-614.
21. Molina, M., Ahl Goy, P., Fraile, A., Sánchez-Monge, R., and García-Olmedo, F. 1993. Inhibition of bacterial and fungal plant pathogens by thionins of types I and II. Plant Sci. 92:169-177.
22. Pernas, M., Sánchez-Monge, R., Gómez, L., and Salcedo, G. 1998. A chestnut seed cystatin differentially effective against cysteine proteinases from closely related pests. Plant Mol. Biol. 38:1235-1242.
23. Salmia, M. 1980. Inhibitors of endogenous proteinases in Scots pine seed: Fractionation and activity changes during germination. Physiol. Plant. 48:266-270.
24. Twining, S. S. 1984. Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes. Anal. Biochem. 143:30-34.
25. Urwin, P. E., Atkinson, H. J., Waller, D. A., McPherson, M. J. 1995. Engineered oryzacystatin-I expressed in transgenic hairy roots confers resistance to Globodera pallida. Plant J. 8:121-131.
26. Urwin, P. E., Lilley, C. J., McPherson, J., and Atkinson, J. 1997. Resistance to both cyst and root-knot nematodes conferred by transgenic Arabidopsis expressing a modified plant cystatin. Plant J. 12:455-461.
27. Zhao, Y., Botella, M. A., Subramanian, L., Niu, X., Nielsen, S. S., Bressan, R. A., and Hasegawa, P. M. 1996. Two wound inducible soybean cysteine proteinase inhibitors have greater insect digestive proteinase inhibitory activities than a constitutive homolog. Plant Physiol. 111: 1299-1306.