Skip to main content

Part of the book series: Plant Gene Research ((GENE))

Abstract

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.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • 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.

    Article  CAS  Google Scholar 

  • 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 

  • 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.

    Article  CAS  Google Scholar 

  • Boller, T., 1982: Enzymatic equipment of plant vacuoles. Physical Vég. 20, 247–257.

    CAS  Google Scholar 

  • Brown, W., Ryan, C. A. (in review): Isolation and characterization of a wound-induced trypsin inhibitor from alfalfa leaves.

    Google Scholar 

  • 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.

    Article  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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 

  • 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 

  • Green, T., Ryan, C. A., 1972: Wound-induced proteinase inhibitor in plant leaves; a possible defense mechanism against insects. Science 175, 776–777.

    Article  PubMed  CAS  Google Scholar 

  • Hahlbrock, K., Grisebach, H., 1979: Enzymatic controls in the biosynthesis of lignin and flavonoids. Ann. Rev. Plant Physiol. 30, 105–130.

    Google Scholar 

  • 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 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  CAS  Google Scholar 

  • 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 

  • Kreuzaler, F., Ragg, H., Fauty, E., Kuhn, D., Hahlbrock, K., 1983: U.V. irradiation

    Google Scholar 

  • of chalcone synthase in cell suspension cultures of Petroselenum hortense. Proc. Natl. Acad. Sci. U. S. A. 80 2591–2593.

    Google Scholar 

  • Knc, J. 1980: Plant immunization-mechanisms and practical implication. In: Active defense mechanisms in plants, pp. 157–178. New York: Plenum Press.

    Google Scholar 

  • Knc, J., 1982: Induced immunity to plant disease. BioScience 32, 854–860.

    Article  Google Scholar 

  • 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 

  • 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 

  • 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 

  • Laskowski, M., Jr., Kato, I., 1980: Protein inhibitors of proteinases. Ann. Rev. Biochem. 49, 593–626.

    Article  PubMed  CAS  Google Scholar 

  • Müller, K. O., Börger, H., 1940: Experimentelle Untersuchungen über die Phytophthora-Resistenz der Kartoffel. Arb. Biol. Reichsanst. 23, 189–231.

    Google Scholar 

  • 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 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • 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 

  • 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 

  • Ryan, C. A., 1979: Proteinase inhibitors. In: Herbivores, their interaction with secondary metabolites, pp. 599–618. New York: Academic Press.

    Google Scholar 

  • Ryan, C. A., 1973: Proteolytic enzymes and their inhibitors in plants. Ann. Rev. Plant Physiol. 24, 173–196.

    Article  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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 

  • 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.

    PubMed  Google Scholar 

  • 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 

  • 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.

    CAS  Google Scholar 

  • Stöessl, A., 1980: Phytoalexins — a biogenic perspective. Phytopath. Z. 99, 251–272.

    Article  Google Scholar 

  • 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 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • West, C. A., 1981: Fungal elicitors of the phytoalexin response in higher plants. Naturwissenschaften 68, 447–457.

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1984 Springer-Verlag/Wien

About this chapter

Cite this chapter

Ryan, C.A. (1984). Defense Responses of Plants. In: Verma, D.P.S., Hohn, T. (eds) Genes Involved in Microbe-Plant Interactions. Plant Gene Research. Springer, Vienna. https://doi.org/10.1007/978-3-7091-8739-5_14

Download citation

  • DOI: https://doi.org/10.1007/978-3-7091-8739-5_14

  • Publisher Name: Springer, Vienna

  • Print ISBN: 978-3-7091-8741-8

  • Online ISBN: 978-3-7091-8739-5

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics