Skip to main content
Log in

Identification and characterization of maize pathogenesis-related proteins. Four maize PR proteins are chitinases

  • Published:
Plant Molecular Biology Aims and scope Submit manuscript

Abstract

Eight pathogenesis-related proteins extractable at pH 2.8 were found to accumulate in maize leaves after mercuric chloride treatment or brome mosaic virus infection. These proteins were called PRm (pathogenesis-related maize) proteins. Seven PRm proteins were purified to homogeneity by preparative polyacrylamide gel electrophoresis and their amino acid compositions determined. Estimated molecular weights in SDS-containing gels were: PRm 1 14.2 kDa; Prm 2 16.5 kDa; PRm 3 and PRm 4 25 kDa; PRm 6b 30.5 kDa; PRm 6a 32 kDa; PRm 7 34.5 kDa. Antisera raised against either PRm 3 or PRm 4 reacted specifically each with PRm 3 or PRm 4. Antisera raised against PRm 6b reacted with PRm 6b as well as with PRm 6a and antisera against PRm 7 reacted with PRm 7 and PRm 5. Tobacco anti-PR 1b antisera reacted with maize PRm 2.

Chitinase (poly[1,4-(N-acetyl-β-D-glucosamide)]glycanhydrolase, EC 3.2.1.14) activity was found for PRm 3, PRm 4, PRm 5, and PRm 7.

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

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Abu Jawdah Y: Changes in the soluble proteins of bean leaves upon fungal or viral infections or after chemical injury. Phytopathol Z 103: 272–279 (1982).

    Google Scholar 

  2. Ahl P, Benjama A, Sanson R, Gianinazzi S: Induction chez le tabac par Pseudomonass syringae de nouvelles proteines (protéines b) associées au développement d'une résistance non spécfique à une dexième infection. Phytopathol Z 102: 201–212 (1981).

    Google Scholar 

  3. Antoniw JF, Ritter CE, Pierpoint WS, van Loon LC: Comparison of three pathogenesis-related proteins from plants of two cultivars of tobacco infected with TMV. J Gen Virol 47: 79–87 (1980).

    Google Scholar 

  4. Antoniw JF, White RF: The effects of aspirin and polyacrylic acid on soluble leaf proteins and resistance to virus infection in five cultivars of tobacco. Phytopathol Z 98: 331–341 (1980).

    Google Scholar 

  5. Blake MS, Johnson KH, Russel-Jones GJ, Gotschlich EC: A rapid sensitive method for detection of alkaline phosphatase-conjugated anti-antibodies on Western blots. Anal. Biochem 136: 175–179 (1984).

    Google Scholar 

  6. Boller T, Gehri A, Mauch F, Vögeli U: Chitinase in bean leaves: induction by ethylene, purification, properties, and possible function. Planta 157: 22–31 (1983).

    Google Scholar 

  7. Boller T, Vögeli U: Vacuolar localization of ethylene-induced chitinase in bean leaves. Plant Physiol 74: 442–444 (1984).

    Google Scholar 

  8. Bradford MM: A rapid and sensitive method for the quantification of microgram quantities of protein utilising the principle of protein-dye binding. Anal Biochem 72: 248–254 (1976).

    Google Scholar 

  9. Brooks KP, Sanders EG: Preparative polyacrylamide gel electrophoresis: removal of polyacrylate from proteins. Anal Biochem 107: 182–186 (1980).

    Google Scholar 

  10. Camacho-Henriquez A, Sänger HL: Analysis of acid-extractable tomato leaf proteins after infection with a viroid, two viruses and a fungus and partial purification of the pathogenesis-related protein P14. Arch Virol 74: 181–196 (1982).

    Google Scholar 

  11. Carr JP, Dixon DC, Klessig DF: Synthesis of pathogenesis-related proteins in tobacco is regulated at the level of mRNA accumulation and occurs on membrane bound polysomes. Proc Natl Acad Sci USA 82: 7999–8003 (1985).

    Google Scholar 

  12. Cornelissen BJC, Hooft van Huijsduijnen RAM, van Loon LC, Bol JF: Molecular characterization of messenger RNAs for pathogenesis-related proteins 1a, 1b and 1c, induced by TMV infection in tobacco. EMBO J 3: 37–40 (1986).

    Google Scholar 

  13. Cornellissen BJC, Horowitz J, van Kan JAL, Goldberg RB, Bol JF: Structure of tabacco genes encoding pathogenesis-related proteins from the PR-1 group. Nucl Acid Acid Res 15: 6799–6812 (1987).

    Google Scholar 

  14. Coutts RHA: Alterations in the soluble protein pattern of tobacco and cowpea leaves following inoculation with tobacco necrosis virus. PI Sci Lett 12: 189–197 (1978).

    Google Scholar 

  15. Fraser RSS: Evidence for the occurrence of the “pathogenesis-related” proteins in leaves of healthy tobacco plants during flowering. Physiol Plant Pathol 19: 69–76 (1981).

    Google Scholar 

  16. Gianinazzi S, Ahl P, Cornu A, Scalla R, Cassini R: First report of host b-protein appearance in response to a fungal infection in tobacco. Physiol Plant Pathol 16: 337–342 (1980).

    Google Scholar 

  17. Gianinazzi S, Kassanis B: Virus resistance induced in plants by polyacrylic acid. J Gen Virol 23: 1–9 (1974).

    Google Scholar 

  18. Gianinazzi S, Martin C, Vallée JC: Hypersensibilité aux virus, température et protéines solubles chez le Nicotiana Xanthi-nc. Apparition de nouvelles macromolécules lors de la répression de la synthèse virale. CR Acad Sciences Paris 270: 2283–2386 (1970).

    Google Scholar 

  19. Gianinazzi S, Pratt A, Shewry PR, Miflin BJ: Partial purification and preliminary characterization of soluble leaf proteins specific to virus-infected tobacco plants. J Gen Virol 34: 345–351 (1977).

    Google Scholar 

  20. Hooft van Huijsduijnen RAM, Cornelissen BJC, van Loon LC, van Boom JH, Tromp M, Bol JF: Virus-induced synthesis of messenger RNAs for precursors of pathogenesis-related proteins in tobacco. EMBO J 4: 2167–2171 (1985).

    Google Scholar 

  21. Jamet E, Fritig B: Purification and characterization of 8 of the pathogenesis-related proteins in tobacco leaves reacting hypersenstively to tobacco mosaic virus. Plant Mol Biol 6: 69–80 (1986).

    Google Scholar 

  22. Kassanis B, Gianinazzi S, White RF: A possible explication of the resistance of virus-infected plants to second infection. J Gen Virol 23: 11–16 (1974).

    Google Scholar 

  23. Kauffmann S, Legrand M, Geoffroy P, Fritig B: Biological function of pathogenesis-related proteins: four PR proteins of tobacco have 1,3-β-glucanase activity. EMBO J 11: 3209–3212 (1987).

    Google Scholar 

  24. Kombrink E, Schröder M, Hahlbrock K: Several “pathogenesis-related” proteins in potato are 1,3-β-glucanases and chitinases. Proc Natl Acad Sci USA 85: 782–786 (1988).

    Google Scholar 

  25. Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277: 680–685 (1970).

    Google Scholar 

  26. Legrand M, Kauffmann S, Geoffroy P, Fritig B: Biological function of pathogenesis-related proteins: Four tobacco pathogenesis-related proteins are chitinases. Proc Natl Acad Sci USA 84: 6750–6754 (1987).

    Google Scholar 

  27. Lucas J, Camacho-Henriquez A, Lottspeich F, Henschen A, Sänger HL: Amino acid sequence of the ‘pathogenesis-related’ leaf protein P14 from viroid-infected tomato reveals a new type of structuraly unfamiliar proteins. EMBO J 4: 2745–2749 (1985).

    Google Scholar 

  28. Matsuoka M, Ohashi Y: Induction of pathogenesis-related proteins in tobacco leaves. Plant Physiol 80: 505–510 (1986).

    Google Scholar 

  29. Moore S: On the determination of cysteic acid. J Biol Chem 250: 4007–4021 (1963).

    Google Scholar 

  30. Parent JC, Asselin A: Detection of pathogenesis-related proteins (PR or b) and other proteins in the intercellular fluid of hypersensitive plants infected with tobacco mosaic virus. Can J Bot 62: 564–569 (1984).

    Google Scholar 

  31. Pennazio S: Changes in soluble protein constitution of Gomphrena globosa leaves showing spontaneous local lesions. Riv Patrol Veg IV 17: 127–135 (1981).

    Google Scholar 

  32. Pfeiffer P, Hirth L: Formation of artificial top component from bromegrass mosaic virus at high salt concentration. Virology 58: 362–368 (1974).

    Google Scholar 

  33. Pierpoint WS: The pathogenesis-related proteins of tobacco leaves. Phytochemistry 25: 1595–1601 (1986).

    Google Scholar 

  34. Redolfi P, Cantisani A: Preliminary characterisation of new soluble proteins in Phaseolus vulgaris cv. Saxa reacting hypersensitively to viral infection. Physiol Plant Pathol 25: 9–19 (1984).

    Google Scholar 

  35. Somssich IE, Schmelzer E, Bollmann J, Hahlbrock K: Rapid activation by fungal elicitor of genes encoding “pathogenesis-related” proteins in cultured parsley cells. Proc Natl Acad Sci USA 83: 2427–2430 (1987).

    Google Scholar 

  36. de Tapia M, Bergman P, Awade A, Burkard G: Analysis of acid extractable bean leaf proteins induced by mercuric chloride treament and alfalfa mosaic virus infection. Partial purification and characterization. Plant Sci 45: 167–177 (1986).

    Google Scholar 

  37. de Tapia M, Dietrich A, Burkard G: In vitro synthesis and processing of a bean pathogenesis-related (PR4) protein. Eur J Biochem 166: 554–563 (1987).

    Google Scholar 

  38. Towbin H, Staehelin T, Gordon J: Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76: 4350–4354 (1979).

    Google Scholar 

  39. van Loon LC: Specific soluble leaf proteins in virus-infected tobacco plants are not normal constituents. J Gen Virol 30: 375–379 (1976).

    Google Scholar 

  40. van Loon LC: Regulation of changes in proteins and enzymes associated with active defense against virus infection. In: Wood RKS (ed) Active defense mechanism in plants, pp. 247–273, NATO (1982).

  41. van Loon LC: “Pathogenesis-related” proteins Pl Mol Biol 4: 111–116 (1985).

    Google Scholar 

  42. van Loon LC, van Kammen A: Polyacrylamide disc electrophoresis of the soluble leaf proteins from Nicotiana tabacum Var. “Samsun NN”. Changes in proteins constitution after infection with tobacco. Virology 40: 199–201 (1970).

    Google Scholar 

  43. van Loon LC, Gerritsen YAM, Ritter CE: Identification, purification and characterization of pathogenesis-related proteins from virus-infected Samsun NN tobacco leaves. Pl Mol Biol 9: 593–609 (1987).

    Google Scholar 

  44. Wagih EE, Coutts RHA: Similarities in the soluble protein profiles of leaf tissue following either a hypersensitive reaction to virus infection or plasmolysis Pl Sci Lett 21: 61–69 (1981).

    Google Scholar 

  45. White RF: Acetyl salicylic acid (aspirin) induces resistance to tobacco mosaic virus in tobacco. Virology 99: 410–412 (1979).

    Google Scholar 

  46. White RF, Rybicki EP, von Wechmar MB, Dekker JL, Antoniw JF: Detection of PR 1-type proteins in Amaranthaceae, Chenopodiaceae, Gramineae and Solanaceae by immunoelectroblotting. J Gen Virol 68: 2043–2048 (1987).

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Nasser, W., de Tapia, M., Kauffmann, S. et al. Identification and characterization of maize pathogenesis-related proteins. Four maize PR proteins are chitinases. Plant Mol Biol 11, 529–538 (1988). https://doi.org/10.1007/BF00039033

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00039033

Key words

Navigation