Defense Responses of Plants

  • C. A. Ryan
Part of the Plant Gene Research book series (GENE)


One of the most promising areas of research concerned with plants and their reaction to their environments is that of natural plant defense systems. Within these defense systems lies a variety of both constitutive and active defenses in which a broad spectrum of chemicals are involved. These chemicals are either present all the time as toxins of deterrents or are induced in response to signals that are released from the sites of pest attacks. In this latter category are two types of responses; (i) those that are localized, in which signals travel to only a relatively few cells within the vicinity of the attack site and, (ii) those that are distal response. In the latter case, signals travel throughout the plant to mobilize defense systems in cells many cm away. Many of the active defense responses can produce resistances that are very broad, and can include a variety of pathogens, including viruses, bacteria and fungi (see Kúc, 1982; Rhodes, 1980; Schultz, 1982). The biochemistry of the regulation of the induced defense compounds and the molecular biology of the signals and the genes that are regulated are generally not known.


Tomato Leaf Cell Wall Fragment Proteinase Inhibitor Gene Pest Attack Biotic Elicitor 
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  1. Bishop, P. D., Makus, D., Pearce, G., Ryan, C. A., 1981: Proteinase inhibitor-inducing factor activity in tomato leaves resides in oligosaccharides enzymically released from cell walls. Proc. Natl. Acad. Sci. (U. S. A.) 78, 3536–3540.CrossRefGoogle Scholar
  2. Bishop, P. D., Pearce, G., Bryant, J., Ryan, C. A., 1984: Isolation and characterization of the proteinase inhibitor induction factor and a PIIF-active oligosaccharide fragments, in review.Google Scholar
  3. Boller, T., Gehri, A., Mauch, F., Vögeli, V., 1983: Chitinase in bean leaves: induction by ethylene, purification, properties and possible function. Planta 157, 22–31.CrossRefGoogle Scholar
  4. Boller, T., 1982: Enzymatic equipment of plant vacuoles. Physical Vég. 20, 247–257.Google Scholar
  5. Brown, W., Ryan, C. A. (in review): Isolation and characterization of a wound-induced trypsin inhibitor from alfalfa leaves.Google Scholar
  6. Bruce, R. J., West, C. A., 1981: The role of pectic fragments of the plant cell wall in elicitation by a fungal endopolygalacturonase. Plant Physiol. 69, 1181–1188.CrossRefGoogle Scholar
  7. Ebel, J., Ayers, A. R., Albersheim, P., 1976: Host-pathogen interaction. XII. Response of suspension cultured soybean cells to elicitor isolated from Phytophthora megasperma var. sojae, a fungal pathogen of soybeans. Plant Physiol. 57, 775–779.PubMedCrossRefGoogle Scholar
  8. Graham, J., Okita, T., Pearce, G., Merryweather, J., Titani, K., Walsh, K., Ryan, C. A., 1983: Molecular cloning and characterization of tomato leaf Inhibitors I and II. Fed. Proc. 42, 1143.Google Scholar
  9. Gardiner, S. E., Schröeder, J., Matern, I., Hammer, D., Hahlbrock, K., 1980: mRNA-dependent regulation of UDP-aprose synthase activity in irradiated plant cells. J. Biol. Chem. 225, 10 752–10 757.Google Scholar
  10. Green, T., Ryan, C. A., 1972: Wound-induced proteinase inhibitor in plant leaves; a possible defense mechanism against insects. Science 175, 776–777.PubMedCrossRefGoogle Scholar
  11. Hahlbrock, K., Grisebach, H., 1979: Enzymatic controls in the biosynthesis of lignin and flavonoids. Ann. Rev. Plant Physiol. 30, 105–130.Google Scholar
  12. Hahlbrock, K., 1981: Flavonoids. In: Stumpf, P. K., Conn, E. E. (eds.), The biochemistry of plants, pp. 425–456. New York: Academic Press.Google Scholar
  13. Hahlbrock, K., Lamb, C., Purwin, C., Ebel, J., Fauty, E., Schäfer, E., 1981: Rapid response of suspension-cultured parsley cells to the elicitor from Phytophthora megasperma var. sojae. Plant Physiol. 67, 768–771.PubMedCrossRefGoogle Scholar
  14. Hahlbrock, K., Boudet, A. M., Chappell, J., Kreuzaler, F., Kuhn, D. N., Ragg, H., 1983: Differential induction of mRNAs by light and elicitor in cultured plant cells. In: Proc. NATO Conference on Structure and Function of the Plant Genome, Ciferri, O., and Dure, L., eds., pp. 15–24.Google Scholar
  15. Hahn, G. M., Darvill, A., Albersheim, P., 1981: Host pathogen intraction, XIX. The endogenous elicitor and fragment of a plant cell wall polysaccharide that elicits phytoalexin accumulation in soybeans. Plant Physiol. 68, 1161–1169.PubMedCrossRefGoogle Scholar
  16. Hargreaves, I. A., Bailey, J. A., 1978: Phytoalexin production by hypocotyls of Phaseolus vulgares in response to constitutive metabolites released by damaged bean cells. Physiol. Plant Pathol. 13, 89–100.CrossRefGoogle Scholar
  17. Janzen, D., 1979: New horizons in the biology of plant defenses, In: Herbivores: their interaction with secondary plant metabolites, pp. 331–351. New York: Academic Press.Google Scholar
  18. Kreuzaler, F., Ragg, H., Fauty, E., Kuhn, D., Hahlbrock, K., 1983: U.V. irradiationGoogle Scholar
  19. of chalcone synthase in cell suspension cultures of Petroselenum hortense. Proc. Natl. Acad. Sci. U. S. A. 80 2591–2593.Google Scholar
  20. Knc, J. 1980: Plant immunization-mechanisms and practical implication. In: Active defense mechanisms in plants, pp. 157–178. New York: Plenum Press.Google Scholar
  21. Knc, J., 1982: Induced immunity to plant disease. BioScience 32, 854–860.CrossRefGoogle Scholar
  22. Kuhn, D. N., Chappell, J., Hahlbrock, K., 1983: Identification and use of cDNAs of phenylalanine ammonia-lyase and 4-coumorate-CoA lyase mRNAs in studies of the induction of phytoalexin biosynthetic enzymes in cultured parsley cells. In: Proc. NATO Conference on “Structure and Function of the Plant Genome”, Ciferri, O., and Dure, L., eds., pp. 329–336.Google Scholar
  23. Lawton, M. A., Dixon, R. A., Hahlbrock, K., Lamb, C., 1983 a: Elicitor induction of mRNA activity: Rapid effects of elicitor on phenylalanine ammonia-lyase and chalcone synthase mRNA in bean cells. Eur. J. Biochem. 130, 131–139.Google Scholar
  24. Lawton, M. A., Dixon, R. A., Hahlbrock, K., Lamb, C., 1983 b: Rapid induction of the synthesis of phenylalanine ammonia-lyase and of chalcone synthase in elicitor-treated plant cells. Eur. J. Biochem. 129, 593–601.Google Scholar
  25. Laskowski, M., Jr., Kato, I., 1980: Protein inhibitors of proteinases. Ann. Rev. Biochem. 49, 593–626.PubMedCrossRefGoogle Scholar
  26. Müller, K. O., Börger, H., 1940: Experimentelle Untersuchungen über die Phytophthora-Resistenz der Kartoffel. Arb. Biol. Reichsanst. 23, 189–231.Google Scholar
  27. Nelson, C., Ryan, C. A., 1980a: In vitro synthesis of pre-proteins or vacuolar compartmented proteinase inhibitors that accumulate in leaves of wounded tomato plants. Proc. Natl. Acad. Sci. U. S. A., 77 1975–1979.Google Scholar
  28. Nelson, C., Ryan, C. A., 1980b: Temporal shifts in the apparent in vivo transcriptional efficiencies of tomato leaf proteinase Inhibitors I and II mRNAs following wounding. Biochem. Biophys. Res. Commun. 94, 355–359.PubMedCrossRefGoogle Scholar
  29. Nothnagel, E. A., McNeil, M., Albersheim, P., Dell, A., 1983: Host-Pathogen interactions. XXII. A galacturonic acid oligosaccharide from plant cell walls elicits phytoalexins. Plant Physiol. 71, 916–926.PubMedCrossRefGoogle Scholar
  30. Plunkett, G., Senear, D. F., Zuroske, G., Ryan, C. A., 1982: Proteinase Inhibitors I and II from leaves of wounded tomato plants: purification and properties. Arch. Biochem. Biophys. 213, 463–472.PubMedCrossRefGoogle Scholar
  31. Ragg, H., Kuhn, D. N., Hahlbrock, H., 1981: Coordinated regulation of 4-coumorate-CoA ligase and phenylalanine ammonia-lyase mRNAs in cultured plant cells. J. Biol. Chem. 256, 10061–10065.PubMedGoogle Scholar
  32. Rhodes, D., 1979: Evolution of plant chemical defenses against herbivores. In: Herbivores, their interaction with secondary plant metabolites, pp. 3–54. New York: Academic Press.Google Scholar
  33. Ryan, C. A., 1981: Proteinase inhibitors. In: Stumpf, P. K., Conn, E. E. (eds.), The biochemistry of plants, Vol. 6, pp. 351–370. New York: Academic Press.Google Scholar
  34. Ryan, C. A., 1979: Proteinase inhibitors. In: Herbivores, their interaction with secondary metabolites, pp. 599–618. New York: Academic Press.Google Scholar
  35. Ryan, C. A., 1973: Proteolytic enzymes and their inhibitors in plants. Ann. Rev. Plant Physiol. 24, 173–196.CrossRefGoogle Scholar
  36. Ryan, C. A., Bishop, P., Pearce, G., Darvill, A. G., McNeil, M., Albersheim, P., 1981: A sycamore cell wall polysaccharide and a chemically related tomato leaf polysaccharide possess similar proteinase inhibitor-inducing activities. Plant Physiol., 68, 616–618.PubMedCrossRefGoogle Scholar
  37. Ryan, C. A., Kuo, T., Pearce, G., Kunkel, R., 1977: Variability in the concentration of three heat-stable proteinase inhibitor proteins in potato tubers. Am. Potato J. 53, 433–440.Google Scholar
  38. Schröder, J., Kreuzaler, F., Schäfer, E., Hahlbrock, K., 1979: Concomitant induction of phenylalanine ammonia-lyase and flavone synthase mRNAs in irradiated plant cells. J. Biol. Chem. 254, 57–65.PubMedGoogle Scholar
  39. Schultz, J. C., 1983: Impact of variable plant defense chemistry on susceptibility of insects to natural enemies. In: Plant resistance to insects, Am. Chem. Soc., pp. 39–45.Google Scholar
  40. Sengupta, C., Deluca, V., Bailey, D. C., Verma, D. P. S., 1981: Post-translational processing of 7 S and 15 S components of soybean storage proteins. Plant Mol. Biol. 1, 19–34.Google Scholar
  41. Stöessl, A., 1980: Phytoalexins — a biogenic perspective. Phytopath. Z. 99, 251–272.CrossRefGoogle Scholar
  42. Verma, D. P. S., Kumar, V., Maclachlan, G., 1982: ß-glucanases in higher plants: localization and potential functions. In: Cellulose and other natural polymer systems. Biogenesis, structure and degradation. Brown, M., Jr. (ed.), pp. 459–488. New York: Plenum Press.Google Scholar
  43. Walker-Simmons, M., Ryan, C. A., 1983: Chitosans and pectic polysaccharides both induce the accumulation of the antifungal phytoalexin pisatin in pea pods and anti-nutrient proteinase inhibitors in tomato leaves. Biochem. Biophys. Res. Comm. 110, 194–199.PubMedCrossRefGoogle Scholar
  44. West, C. A., 1981: Fungal elicitors of the phytoalexin response in higher plants. Naturwissenschaften 68, 447–457.CrossRefGoogle Scholar

Copyright information

© Springer-Verlag/Wien 1984

Authors and Affiliations

  • C. A. Ryan
    • 1
  1. 1.Institute of Biological Chemistry and Biochemistry/Biophysics ProgramWashington State UniversityPullmanUSA

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