Defence Proteins, Glycanhydrolases and Oligosaccharide Signals in Plant-Virus Interactions

  • B. Fritig
  • S. Kauffmann
  • J. Rouster
  • B. Dumas
  • P. Geoffroy
  • M. Kopp
  • M. Legrand
Conference paper
Part of the NATO ASI Series book series (volume 41)

Abstract

Most defence proteins and enzymes that are typical of incompatible plant-fungi interactions are also induced or stimulated in hypersensitive plant-virus interactions. Examples include “pathogenesis-related” (PR) proteins, proteases, inhibitors of proteases, hydrolases (chitinases and 1,3-ß-glucanases), enzymes of ethylene biosynthesis, of aromatic metabolism, of phytoalexin biosynthesis and oxidative enzymes. At least 10 PR proteins are glycanhydrolases (4 chitinases and 6 glucanases) with differential specific activity. They are direct anti-microbial defence enzymes and are supposed to cause other defence responses through the release of oligosaccharidic elicitors of pathogen and/or plant origin. Oligosaccharides are shown to protect plants from infection by viruses by a host-mediated process that may not be a classical defence mechanism.

Keywords

Tobacco Mosaic Virus Active Defence Alfalfa Mosaic Virus Hypersensitive Resistance Physiol Plant Pathol 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
This is a preview of subscription content, log in to check access.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Albersheim P, Darvill AG (1985) Oligosaccharins. Sci Am 253:44–50CrossRefGoogle Scholar
  2. Antoniw JF, White RF (1983) Biochemical properties of the PR proteins from tobacco. Neth J Plant Pathol 89:255–264CrossRefGoogle Scholar
  3. Antoniw JF, Ritter CE, Pierpoint WS, van Loon LC (1980) Comparison of three pathogenesis-related proteins from plants of two cultivars of tobacco infected with TMV. J Gen Virol 47:79–87CrossRefGoogle Scholar
  4. Bailey JA, Mansfield JW (eds) (1982) Phytoalexins. Blackie, Glasgow LondonGoogle Scholar
  5. Bailey JA, Deverall BJ (eds) (1983) The dynamics of host defence. Academic Press, Sydney New York LondonGoogle Scholar
  6. Bartnicki-Garcia S (1968) Cell wall chemistry, morphogenesis and taxonomy of fungi. Annu Rev Microbiol 22:87–108PubMedCrossRefGoogle Scholar
  7. Boiler T, Gehri A, Mauch F, Vogeli U (1983) Chitinase in bean leaves: induction by ethylene, purification, properties, and possible function. Planta 157:22–31CrossRefGoogle Scholar
  8. Bruening G, Ponz F, Glascock C, Russel ML, Rowhani A, Chay C (1987) Resistance of cowpeas to cowpea mosaic virus and to tobacco ringspot virus. In: Evered D, Harnett S (eds) Ciba Foundation Symposium 133: Plant resistance to viruses. John Wiley & Sons, Chichester, p 23Google Scholar
  9. Cabib E (1987) The synthesis and degradation of chitin. Adv Enzymol 59:59–101PubMedGoogle Scholar
  10. Collinge DB, Slusarenko AK (1987) Plant gene expression in response to pathogens. Plant Mol Biol 9:389–410CrossRefGoogle Scholar
  11. Cornelissen BJC, Hooft van Huijsduijnen RAM, Bol JF (1986) A tobacco mosaic virus-induced tobacco protein is homologous to the sweet-tasting protein thaumatin. Nature 321:531–532PubMedCrossRefGoogle Scholar
  12. Darvill AG, Albersheim P (1984) Phytoalexins and their elicitors - a defense against microbial infection in plants. Annu Rev Plant Physiol 35:243–275CrossRefGoogle Scholar
  13. Dumas B, Legrand M, Geoffroy P, Fritig B (1988) Purification of tobacco O-methyltransferases by affinity chromatography and estimation of rate of synthesis of the enzymes during the hypersensitive reaction to virus infection. Planta 176:36–41CrossRefGoogle Scholar
  14. Felix G, Meins J (1985) Purification, immunoassay and characterization of an abundant, cytokinin-regulated polypeptide in cultured tobacco tissues. Evidence that the protein is a ß-1,3-glucanase. Planta 164:423–428CrossRefGoogle Scholar
  15. Fortin MG, Parent JG, Asselin A (1985) Comparative study of two groups of b proteins (pathogenesis-related) from the intercellular fluid of Nicotiana leaf tissue infected by TMV. Can J Bot 63:932–93Google Scholar
  16. Fraser RSS (1985) Mechanisms of genetically controlled resistance and virulence: virus diseases. In: Fraser RSS (ed) Mechanisms of resistance to plant diseases. Nijhoff, Dordrecht, p 143CrossRefGoogle Scholar
  17. Fraser RSS (1988) Virus recognition and pathogenicity: implications for resistance mechanisms and breeding. Pestic Sci 23:267–275CrossRefGoogle Scholar
  18. Fritig B, Kauffmann S, Dumas B, Geoffroy P, Kopp M, Legrand M (1987) Mechanism of the hypersensitivity reaction of plants. In : Evered D, Harnett S (eds) Ciba Foundation Symposium 133: Plant resistance to viruses. John Wiley & Sons, Chichester, p 92Google Scholar
  19. Gianinazzi S, Martin C, Vallee JC (1970) Hypersensibilite aux virus, temperature et protéines solubles chez le Nicotiana Xanthi nc. Apparition de nouvelles macromolécules lors de la repression de la synthèse virale. C R Acad Sci (Paris) D270:2383–2386Google Scholar
  20. Goodman RN, Kiraly Z, Wood KR (1986) The biochemistry and physiology of plant disease. University of Missouri Press, Columbia, MissouriGoogle Scholar
  21. Granell A, Bellés JM, Conejero V (1987) Induction of pathogenesis-related proteins in tomato by citrus exocortis viroid, silver ion and ethephon. Physiol Mol Plant Pathol 31:83–90CrossRefGoogle Scholar
  22. Hahn MG, Bucheli P, Cervone F, Doares SH, O’Neil RA, Darvill A, Albersheim P (1989) The roles of cell wall constituents in plant pathogen interactions. In: Nester E, Kosuge T (eds) Plant-Microbe Interactions, Vol. 3. Macmillan, London New York, in press.Google Scholar
  23. Hooft van Huijsduijnen RAM, Kauffmann S, Brederode FT, Cornelissen BJC, Legrand M, Fritig B, Bol J (1987) Homology between chitinases that are induced by TMV infection of tobacco. Plant Mol Biol 9:411–420CrossRefGoogle Scholar
  24. Jamet E, Fritig B (1986) Purification and characterization of 8 of the pathogenesis-related proteins in tobacco leaves reacting hypersensitively to tobacco mosaic virus. Plant Mol Biol 6:69–80CrossRefGoogle Scholar
  25. Kauffmann S (1988) Les protéines PR (Pathogenesis-Related) du Tabac: Des protéines impliquées dans les réactions de défense aux agents phytopathogènes. Isolement, propriétés sérologiques et activités biologiques. Thèse de l’Université Louis Pasteur, StrasbourgGoogle Scholar
  26. Kauffmann S, Legrand M, Geoffroy P, Fritig B (1987) Biological function of ’pathogenesis-related’ proteins: four PR proteins of tobacco have 1,3-ß-glucanase activity. EMBO J 6:3209–3212PubMedGoogle Scholar
  27. Keen NT, Staskawicz B (1988) Host range determinants in plant pathogens and symbionts. Annu Rev Microbiol 42:421–440CrossRefGoogle Scholar
  28. Knorr DA, Dawson WO (1988) A point mutation in the tobacco mosaic virus capsid protein gene induces hypersensitivity in Nicotiana sylvestris. Proc Natl Acad Sci USA 85:170–174PubMedCrossRefGoogle Scholar
  29. Kombrink E, Schröder M, Hahlbrock K (1988) Several “pathogenesis-related” proteins in potato are 1,3-ß-glucanases and chitinases. Proc Natl Acad Sci USA 85:782–786PubMedCrossRefGoogle Scholar
  30. Konate G, Fritig B (1983) Extension of the ELISA method to the measurement of the specific radioactivity of viruses in crude cellular extracts. J Virol Meth 6:347–356CrossRefGoogle Scholar
  31. Konate G, Fritig B (1984) An efficient microinoculation procedure to study plant virus multiplication at pre-determined individual infection sites on the leaves. Phytopathol Z 109:131–138CrossRefGoogle Scholar
  32. Konate G, Kopp M, Fritig B (1982) Multiplication du virus de la mosaïque du tabac dans des hôtes à réponse systémique ou nécrotique: approche biochimique à l’étude de la résistance hypersensible aux virus. Phytopathol Z 105:214–225CrossRefGoogle Scholar
  33. Kopp M, Rouster J, Fritig B, Darvill A, Albersheim P (1989) Host-pathogen interactions XXXII. A fungal glucan preparation protects Nicotianae against infection by viruses. Plant Physiol 90:208–216PubMedCrossRefGoogle Scholar
  34. Lamb CJ, Lawton MA, Dron M, Dixon RA (1989) Signals and transduction mechanisms for activation of plant defenses against microbial attack. Cell 56:215–224PubMedCrossRefGoogle Scholar
  35. Legrand M, Fritig B, Hirth L (1976) Enzymes of the phenyl-propanoid pathway and the necrotic reaction of hypersensitive tobacco to tobacco mosaic virus. Phytochemistry 15:1353–1359CrossRefGoogle Scholar
  36. Legrand M, Fritig B, Hirth L (1978) o-diphenol O-methyltransferases of healthy and tobacco mosaic virus-infected hypersensitive tobacco. Planta 144:101–108CrossRefGoogle Scholar
  37. Legrand M, Kauffmann S, Geoffroy P, Fritig B (1987) Biological function of “pathogenesis-related” proteins: four tobacco PR-proteins are chitinases. Proc Natl Acad Sci USA 84:6750–6754PubMedCrossRefGoogle Scholar
  38. Linthorst HJM, Meuwissen RLJ, Kauffmann S, Bol J (1989) Constitutive expression of pathogenesis-related proteins PR-1, GRP, and PR-S in tobacco has no effect on virus infection. The Plant Cell 1:285–291PubMedCrossRefGoogle Scholar
  39. McNeil M, Darvill AG, Fry SC, Albersheim P (1984) Structure and function of the primary cell walls of plants. Annu Rev Biochem 53:625–663PubMedCrossRefGoogle Scholar
  40. Massala R, Legrand M, Fritig B (1980) Effect of α-aminooxyacetate, a competitive inhibitor of phenylalanine ammonia-lyase, on the hypersensitive resistance of tobacco to tobacco mosaic virus. Physiol Plant Pathol 16:213–226CrossRefGoogle Scholar
  41. Massala R, Legrand M, Fritig B (1987) Comparative effects of two competitive inhibitors of phenylalanine ammonia-lyase on the hypersensitive resistance of tobacco to tobacco mosaic virus. Plant Physiol Biochem 25:217–225Google Scholar
  42. Mauch F, Mauch-Mani B, Boiler T (1988) Antifungal hydrolase in pea tissue. II. Inhibition of fungal growth by combinations of chitinase and ß-l,3-glucanase. Plant Physiol 88:936–942PubMedCrossRefGoogle Scholar
  43. Mazau D, Esquerre-Tugaye M-T (1986) Hydroxyproline-rich glycoprotein accumulation in the cell walls of plants infected by various pathogens. Physiol Mol Plant Pathol 29:147–157CrossRefGoogle Scholar
  44. Métraux JP, Boiler T (1986) Local and systemic induction of chitinase in cucumber plants in response to viral, bacterial and fungal infections. Physiol Mol Plant Pathol. 28:161–169CrossRefGoogle Scholar
  45. Métraux JP, Burkhart W, Moyer M, Dincher S, Middlesteadt W, Williams S, Payne G, Carnes M, Ryals J (1989) Isolation of a complementary DNA encoding a chitinase with structural homology to a bifunctional lysozyme/chitinase. Proc Natl Acad Sci USA 86:896–900PubMedCrossRefGoogle Scholar
  46. Modderman PW, Schot CP, Klis FM, Wieringa-Brants DH (1985) Acquired resistance in hypersensitive tobacco against tobacco mosaic virus, induced by plant cell wall components. Phytopathol Z 113:165–170CrossRefGoogle Scholar
  47. Moore AE, Stone BA (1972) Effect of infection with TMV and other viruses on the level of a ß-1,3-glucan hydrolase in leaves of Nicotiana glutinosa. Virology 50:791–798PubMedCrossRefGoogle Scholar
  48. Pierpoint WS, Robinson NP, Leason MB (1981) The pathogenesis-related proteins of tobacco: their induction by viruses in intact plants and their induction by chemicals in detached leaves. Physiol Plant Pathol 19:85–97Google Scholar
  49. Pierpoint WS, Tatham AS, Pappin DJC (1987) Identification of the virus-induced protein of tobacco leaves that resembles the sweet-protein thaumatin. Physiol Mol Plant Pathol 31:291–298CrossRefGoogle Scholar
  50. Ponz F, Bruening G (1986) Mechanisms of resistance to plant viruses. Annu Rev Phytopathol 24:355–381CrossRefGoogle Scholar
  51. Ponz F, Glascock CB, Bruening G (1988) An inhibitor of polyprotein processing with the characteristics of a natural virus resistance factor. Mol Plant-Microbe Interact 1:25–31CrossRefGoogle Scholar
  52. Richardson M, Valdes-Rodriguez S, Blanco-Labra A (1987) A possible function for thaumatin and a TMV-induced protein suggested by homology to a maize inhibitor. Nature 327:432–434CrossRefGoogle Scholar
  53. Roby D, Toppan A, Esquerre-Tugaye MT (1987) Cell surfaces in plant-microorganism interactions. VIII Increased proteinase inhibitor activity in melon plants in response to infection by Colletotrichum lagenarium or to treatment with an elicitor fraction from this fungus. Physiol Mol Plant Pathol 30:453–460CrossRefGoogle Scholar
  54. Ryan CA (1981) Proteinase inhibitors. In: Stumpf PK, Conn EE (eds) Biochemistry of plants, Vol. 6. Academic Press, London, p 351Google Scholar
  55. Ryan CA (1987) Oligosaccharide signalling in plants. Annu Rev Cell Biol 3:295–317PubMedCrossRefGoogle Scholar
  56. Ryan CA (1988) Oligosaccharides as recognition signals for the expression of defensive genes in plants. Biochemistry 27:8879–8883CrossRefGoogle Scholar
  57. Saito T, Meshi T, Takamatsu N, Okada Y (1987) Coat protein gene sequence of tobacco mosaic virus encodes a host response determinant. Proc Natl Acad Sci USA 84:6074–6077PubMedCrossRefGoogle Scholar
  58. Schlumbaum A, Mauch F, Vogeli U, Boiler T (1986) Plant chitinases are potent inhibitors of fungal growth. Nature 324:365–367CrossRefGoogle Scholar
  59. Shimomura T, Dijkstra J (1975) The occurrence of callose during the progress of local lesion formation. Neth J Plant Pathol 81:107–121CrossRefGoogle Scholar
  60. Shinshi H, Mohnen D, Meins F (1987) Regulation of a plant pathogenesis-related enzyme: inhibition of chitinase and chitinase mRNA accumulation in cultured tobacco tissues by auxin and cytokinin. Proc Natl Acad Sci USA 84:89–93PubMedCrossRefGoogle Scholar
  61. Staskawicz B, Bonas U, Dahlbeck D, Huynh T, Kearny B, Ronald P, Whalen M (1988) Molecular determinants of specificity in plant-bacterial interactions. In: Keen NT, Kosuge T, Walling LL (eds) Physiology and biochemistry of plant-microbial interactions. American Society of Plant Physiologists, Rockville, p 124Google Scholar
  62. Van Loon LC (1982) Regulation of changes in proteins and enzymes associated with the active defence against virus infection. In: Wood RKS (ed) Active defence mechanisms in plants. Plenum Press, New York, p 247Google Scholar
  63. Van Loon LC (1985) Pathogenesis-related proteins. Plant Mol Biol 4:111–116CrossRefGoogle Scholar
  64. Van Loon LC, van Kammen A (1970) Polyacrylamide disc electrophoresis of the soluble leaf proteins from Nicotiana tabacum var. “Samsun” and “Samsun NN”. Changes in protein constitution after infection with TMV. Virology 40:199–201CrossRefGoogle Scholar
  65. Varner JE, Lin LL (1989) Plant cell wall structure. Cell 56:231–239PubMedCrossRefGoogle Scholar
  66. Vera P, Conejero V (1988) Pathogenesis-related proteins of tomato. P-69 as an alkaline endoproteinase. Plant Physiol 87:58–63PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1990

Authors and Affiliations

  • B. Fritig
    • 1
  • S. Kauffmann
    • 1
  • J. Rouster
    • 1
  • B. Dumas
    • 1
  • P. Geoffroy
    • 1
  • M. Kopp
    • 1
  • M. Legrand
    • 1
  1. 1.Institut de Biologie Moléculaire des Plantes du CNRSStrasbourgFrance

Personalised recommendations