Role of Pathogenesis-Related (PR) Proteins in Plant Defense Mechanism

  • Deepti Jain
  • Jitendra Paul Khurana


Plant growth and development is often challenged by several abiotic and biotic stresses, such as drought, cold, salinity, wounding, heavy metals, and pathogen attacks, respectively. A plant responds to these threats by activating a cascade of genes, encoding different effectors, receptors, and signaling and protective molecules. Among all, the induction and accumulation of pathogenesis-related (PR) proteins in plants in response to these adverse conditions is very important as PR proteins are an indispensible component of innate immune responses in plants under biotic or abiotic stress conditions. The PR proteins protect the plants from further infection by not only accumulating locally in the infected and surrounding tissues but also in remote uninfected tissues. Induction of PRs has been reported from many plant species belonging to different families suggesting a general role for these proteins in adaptation to biotic or abiotic stress conditions. PR proteins are also involved in hypersensitive response (HR) or systemic acquired resistance (SAR) against infection. Thus, PR proteins have been defined as “proteins encoded by the host plant but induced only in pathological or related situations,” the latter inferring situations of nonpathogenic origin. In this chapter, structure, biochemistry, source, regulation of gene expression, and role in defense mechanism of various pathogenesis-related proteins will be discussed.


Abiotic stress PR proteins Stress response Biotic stress Pathogenesis 


  1. Abad LR et al (1996) Antifungal activity of tobacco osmotin has specificity and involves plasma membrane permeabilization. Plant Sci 118(1):11–23CrossRefGoogle Scholar
  2. Abeles FB et al (1971) Preparation and purification of glucanase and chitinase from bean leaves. Plant Physiol 47(1):129–134PubMedPubMedCentralCrossRefGoogle Scholar
  3. Adams DJ (2004) Fungal cell wall chitinases and glucanases. Microbiology 150(7):2029–2035PubMedCrossRefGoogle Scholar
  4. Akiyama T et al (2004) Cloning, characterization and expression of OsGLN2, a rice endo-1, 3-β-glucanase gene regulated developmentally in flowers and hormonally in germinating seeds. Planta 220(1):129–139PubMedCrossRefGoogle Scholar
  5. Alexander D et al (1993) Increased tolerance to two oomycete pathogens in transgenic tobacco expressing pathogenesis-related protein 1a. Proc Natl Acad Sci 90(15):7327–7331PubMedPubMedCentralCrossRefGoogle Scholar
  6. Alonso E et al (1995) Differential in vitro DNA binding activity to a promoter element of the gn1β-1, 3-glucanase gene in hypersensitively reacting tobacco plants. Plant J 7(2):309–320PubMedCrossRefGoogle Scholar
  7. Anand A et al (2004) Apoplastic extracts from a transgenic wheat line exhibiting lesion-mimic phenotype have multiple pathogenesis-related proteins that are antifungal. Mol Plant-Microbe Interact 17(12):1306–1317PubMedCrossRefGoogle Scholar
  8. Anguelova-Merhar VS et al (2001) β-1, 3-Glucanase and Chitinase activities and the resistance response of wheat to leaf rust. J Phytopathol 149(7–8):381–384CrossRefGoogle Scholar
  9. Antoniw JF, Pierpoint WS (1978) Purification of a tobacco leaf protein associated with resistance to virus infection [proceedings]. Biochem Soc Trans 6(1):248–250PubMedCrossRefGoogle Scholar
  10. Ashfield T et al (1994) Cf gene-dependent induction of a b-1, 3-glucanase promoter in tomato plants infected with Cladosporium fulvum. MPMI-Mol Plant Microbe Interact 7(5):645–656CrossRefGoogle Scholar
  11. Bachmann D et al (1998) Improvement of potato resistance to Phytophthora infestans by overexpressing antifungal hydrolases. 5th international workshop on pathogenesis-related proteins. Signaling pathways and biological activities. AussoisGoogle Scholar
  12. Bartnicki-Garcia S (1968) Cell wall chemistry, morphogenesis, and taxonomy of fungi. Annu Rev Microbiol 22(1):87–108PubMedCrossRefGoogle Scholar
  13. Beerhues L, Kombrink E (1994) Primary structure and expression of mRNAs encoding basic chitinase and 1, 3-β-glucanase in potato. Plant Mol Biol 24(2):353–367PubMedCrossRefGoogle Scholar
  14. Bernier F, Berna A (2001) Germins and germin-like proteins: plant do-all proteins. But what do they do exactly? Plant Physiol Biochem 39(7):545–554CrossRefGoogle Scholar
  15. Bohlmann H et al (1998) Wounding and chemicals induce expression of the Arabidopsis thaliana gene Thi2. 1, encoding a fungal defense thionin, via the octadecanoid pathway. FEBS Lett 437(3):281–286PubMedCrossRefGoogle Scholar
  16. Boller T, Felix G (1996) Olfaction in plants: specific perception of common microbial molecules. In: Stacey G, Mullin B, Gresshoff PM (éds) Biology of plant-microbe interactions. International Society for Molecular Plant-Microbe Interactions, Knoxville, É.-U:1-8Google Scholar
  17. Brederode FT et al (1991) Differential induction of acquired resistance and PR gene expression in tobacco by virus infection, ethephon treatment, UV light and wounding. Plant Mol Biol 17(6):1117–1125PubMedCrossRefGoogle Scholar
  18. Broekaert WF et al (1988) Comparison of some molecular, enzymatic and antifungal properties of chitinases from thorn-apple, tobacco and wheat. Physiol Mol Plant Pathol 33(3):319–331CrossRefGoogle Scholar
  19. Brogue K et al (1991) Transgenic plants with enhanced resistance to the fungal pathogen Rhizoctonia solani. Science 254(5035):1194–1197PubMedCrossRefGoogle Scholar
  20. Bucciaglia PA, Smith AG (1994) Cloning and characterization of tag 1, a tobacco anther β-1, 3-glucanase expressed during tetrad dissolution. Plant Mol Biol 24(6):903–914PubMedCrossRefGoogle Scholar
  21. Buchner P et al (2002) Characterization of a tissue-specific and developmentally regulated β-1, 3-glucanase gene in pea (Pisum sativum). Plant Mol Biol 49(2):171–186PubMedCrossRefGoogle Scholar
  22. Caruso C et al (1996) Structural and antifungal properties of a pathogenesis-related protein from wheat kernel. J Protein Chem 15(1):35–44PubMedCrossRefGoogle Scholar
  23. Castresana C et al (1990) Tissue-specific and pathogen-induced regulation of a Nicotiana plumbaginifolia beta-1, 3-glucanase gene. Plant Cell 2(12):1131–1143PubMedPubMedCentralGoogle Scholar
  24. Chamnongpol S et al (1998) Defense activation and enhanced pathogen tolerance induced by H2O2 in transgenic tobacco. Proc Natl Acad Sci 95(10):5818–5823PubMedPubMedCentralCrossRefGoogle Scholar
  25. Chang M-M et al (1992) Molecular characterization of a pea β-1, 3-glucanase induced by Fusarium solani and chitosan challenge. Plant Mol Biol 20(4):609–618PubMedCrossRefGoogle Scholar
  26. Cordero MJ et al (1994) Differential expression and induction of chitinases and β1- 3-glucanases in response to fungal infection during germination of maize seeds. Mol Plant Microbe Interact 7:23–31CrossRefGoogle Scholar
  27. Darvill AG, Albersheim P (1984) Phytoalexins and their elicitors-a defense against microbial infection in plants. Annu Rev Plant Physiol 35(1):243–275CrossRefGoogle Scholar
  28. Datta K et al (1999) Over-expression of the cloned rice thaumatin-like protein (PR-5) gene in transgenic rice plants enhances environmental friendly resistance to Rhizoctonia solani causing sheath blight disease. Theor Appl Genet 98(6–7):1138–1145CrossRefGoogle Scholar
  29. Datta K et al (2001) Enhanced resistance to sheath blight by constitutive expression of infection-related rice chitinase in transgenic elite indica rice cultivars. Plant Sci 160(3):405–414PubMedCrossRefGoogle Scholar
  30. Delaney TP (1997) Genetic dissection of acquired resistance to disease. Plant Physiol 113(1):5PubMedPubMedCentralCrossRefGoogle Scholar
  31. Donnell PJO et al (1996) Ethylene as a signal mediating the wound response of tomato plants. Science 274(5294):1914CrossRefGoogle Scholar
  32. Edreva A (2005) Pathogenesis-related proteins: research progress in the last 15 years. Gen Appl Plant Physiol 31(1–2):105–124Google Scholar
  33. Epple P et al (1995) An Arabidopsis thaliana thionin gene is inducible via a signal transduction pathway different from that for pathogenesis-related proteins. Plant Physiol 109(3):813–820PubMedPubMedCentralCrossRefGoogle Scholar
  34. Fagoaga C et al (2001) Increased tolerance to Phytophthora citrophthora in transgenic orange plants constitutively expressing a tomato pathogenesis related protein PR-5. Mol Breed 7(2):175–185CrossRefGoogle Scholar
  35. Fecht-Christoffers MM et al (2003) Effect of manganese toxicity on the proteome of the leaf apoplast in cowpea. Plant Physiol 133(4):1935–1946PubMedPubMedCentralCrossRefGoogle Scholar
  36. Fulcher RG et al (1976) β-1, 3-glucans may be associated with cell plate formation during cytokinesis. Can J Bot 54(5–6):539–542CrossRefGoogle Scholar
  37. Gau AE et al (2004) Accumulation of pathogenesis-related proteins in the apoplast of a susceptible cultivar of apple (Malus domestica cv. Elstar) after infection by Venturia inaequalis and constitutive expression of PR genes in the resistant cultivar Remo. Eur J Plant Pathol 110(7):703–711CrossRefGoogle Scholar
  38. Goodman RN, Novacky AJ (1994) The hypersensitive reaction in plants to pathogens: a resistance phenomenon. Am Phytopathol Soc (APS)Google Scholar
  39. Hammond-Kosack KE, Jones JD (1996) Resistance gene-dependent plant defense responses. Plant Cell 8(10):1773PubMedPubMedCentralCrossRefGoogle Scholar
  40. Hanselle T, Barz W (2001) Purification and characterisation of the extracellular PR-2b β-1, 3-glucanase accumulating in different Ascochyta rabiei-infected chickpea (Cicer arietinum L.) cultivars. Plant Sci 161(4):773–781CrossRefGoogle Scholar
  41. Hart CM et al (1993) A 61 bp enhancer element of the tobacco β-1, 3-glucanase B gene interacts with one or more regulated nuclear proteins. Plant Mol Biol 21(1):121–131PubMedCrossRefGoogle Scholar
  42. Helleboid S et al (2000) Cloning of β-1, 3-glucanases expressed during Cichorium somatic embryogenesis. Plant Mol Biol 42(2):377–386PubMedCrossRefGoogle Scholar
  43. Horvath DM et al (1998) Four classes of salicylate-induced tobacco genes. Mol Plant-Microbe Interact 11(9):895–905PubMedCrossRefGoogle Scholar
  44. Ignatius SMJ et al (1994) Effects of fungal infection and wounding on the expression of chitinases and β-1, 3 glucanases in near-isogenic lines of barley. Physiol Plant 90(3):584–592CrossRefGoogle Scholar
  45. Jach G et al (1995) Enhanced quantitative resistance against fungal disease by combinatorial expression of different barley antifungal proteins in transgenic tobacco. Plant J 8(1):97–109PubMedCrossRefGoogle Scholar
  46. Jeun YC (2000) Immunolocalization of PR-protein P14 in leaves of tomato plants exhibiting systemic acquired resistance against Phytophthora infestans induced by pretreatment with 3-aminobutryic acid and preinoculation with tobacco necrosis virus. J Plant Dis Prot:352–367Google Scholar
  47. Jeun YCH, Buchenauer H (2001) Infection structures and localization of the pathogenesis-related protein AP 24 in leaves of tomato plants exhibiting systemic acquired resistance against Phytophthora infestans after pre-treatment with 3-aminobutyric acid or tobacco necrosis virus. J Phytopathol 149(3–4):141–154CrossRefGoogle Scholar
  48. Jongedijk E et al (1995) Synergistic activity of chitinases and β-1, 3-glucanases enhances fungal resistance in transgenic tomato plants. Euphytica 85(1–3):173–180CrossRefGoogle Scholar
  49. Jung HW, Hwang BK (2000) Pepper gene encoding a basic β-1, 3-glucanase is differentially expressed in pepper tissues upon pathogen infection and ethephon or methyl jasmonate treatment. Plant Sci 159(1):97–106PubMedCrossRefGoogle Scholar
  50. Kaku H et al (1997) N-acetylchitooligosaccharides elicit expression of a single (1→ 3)-β-glucanase gene in suspension-cultured cells from barley (Hordeum vulgare). Physiol Plant 100(1):111–118CrossRefGoogle Scholar
  51. Kauffmann S et al (1987) Biological function of pathogenesis-related’ proteins: four PR proteins of tobacco have 1, 3-β-glucanase activity. EMBO J 6(11):3209PubMedPubMedCentralGoogle Scholar
  52. Klarzynski O et al (2000) Linear β-1, 3 glucans are elicitors of defense responses in tobacco. Plant Physiol 124(3):1027–1038PubMedPubMedCentralCrossRefGoogle Scholar
  53. Lawrence CB et al (2000) Constitutive hydrolytic enzymes are associated with polygenic resistance of tomato to Alternaria solani and may function as an elicitor release mechanism. Physiol Mol Plant Pathol 57(5):211–220CrossRefGoogle Scholar
  54. Legrand M et al (1987) Biological function of pathogenesis-related proteins: four tobacco pathogenesis-related proteins are chitinases. Proc Natl Acad Sci U S A 84(19):6750–6754PubMedPubMedCentralCrossRefGoogle Scholar
  55. Leubner-Metzger G, Meins Jr F (1999) 3 functions and regulation of plant β-(PR-2). Pathogenesis-related proteins in plantsGoogle Scholar
  56. Li WL et al (2001) Isolation and characterization of novel cDNA clones of acidic chitinases and β-1, 3-glucanases from wheat spikes infected by Fusarium graminearum. Theor Appl Genet 102(2–3):353–362CrossRefGoogle Scholar
  57. Livne B et al (1997) TMV-induced expression of tobacco β-glucanase promoter activity is mediated by a single, inverted, GCC motif. Plant Sci 130(2):159–169CrossRefGoogle Scholar
  58. Lozovaya VV et al (1998) β-l, 3-glucanase and resistance to Aspergillus flavus infection in maize. Crop Sci 38(5):1255–1260CrossRefGoogle Scholar
  59. Lusso M, Kuc J (1995) Evidence for transcriptional regulation of β-1, 3-glucanase as it relates to induced systemic resistance of tobacco to blue mold. Mol Plant-Microbe Interact 8(3):473–475Google Scholar
  60. Martin GB et al (1993) Map-based cloning of a protein kinase gene conferring disease resistance in tomato. Sci-New York Wash 262:1432–1432CrossRefGoogle Scholar
  61. Mauch F et al (1988a) Antifungal hydrolases in pea tissue I. Purification and characterization of two chitinases and two β-1, 3-glucanases differentially regulated during development and in response to fungal infection. Plant Physiol 87(2):325–333PubMedPubMedCentralCrossRefGoogle Scholar
  62. Mauch F et al (1988b) Antifungal hydrolases in pea tissue II. Inhibition of fungal growth by combinations of chitinase and β-1, 3-glucanase. Plant Physiol 88(3):936–942PubMedPubMedCentralCrossRefGoogle Scholar
  63. Meikle PJ et al (1991) The location of (1→ 3)-β-glucans in the walls of pollen tubes of Nicotiana alata using a (1→ 3)-β-glucan-specific monoclonal antibody. Planta 185(1):1–8PubMedCrossRefGoogle Scholar
  64. Meins F Jr et al (1992) The primary structure of plant pathogenesis-related glucanohydrolases and their genes. Springer, BerlinCrossRefGoogle Scholar
  65. Meins F et al (1994) Plant chitinase genes. Plant Mol Biol Report 12(2):S22–S28CrossRefGoogle Scholar
  66. Melchers LS et al (1998) The utility of PR genes to develop disease resistance in transgenic crops. 5th international workshop on pathogenesis-related proteins. Signalling pathways and biological activitiesGoogle Scholar
  67. Neuhaus JM (1999) Plant chitinases (pr-3, pr-4, pr-8, pr-11). Pathogenesis-related proteins in plants: 77–105Google Scholar
  68. Neuhaus JM et al (1996) A revised nomenclature for chitinase genes. Plant Mol Biol Report 14(2):102–104CrossRefGoogle Scholar
  69. Nielsen KK et al (1992) An acidic class III chitinase in sugar beet: induction by Cercospora beticola, characterization, and expression in transgenic tobacco plants. Mol Plant-Microbe Interact: MPMI 6(4):495–506CrossRefGoogle Scholar
  70. Niki T et al (1998) Antagonistic effect of salicylic acid and jasmonic acid on the expression of pathogenesis-related (PR) protein genes in wounded mature tobacco leaves. Plant Cell Physiol 39(5):500–507CrossRefGoogle Scholar
  71. Ohme-Takagi M, Shinshi H (1995) Ethylene-inducible DNA binding proteins that interact with an ethylene-responsive element. Plant Cell 7(2):173–182PubMedPubMedCentralCrossRefGoogle Scholar
  72. Ori N et al (1990) A major stylar matrix polypeptide (sp41) is a member of the pathogenesis-related proteins superclass. EMBO J 9(11):3429PubMedPubMedCentralGoogle Scholar
  73. Pan S-Q et al (1989) Direct detection of β-1, 3-glucanase isozymes on polyacrylamide electrophoresis and isoelectrofocusing gels. Anal Biochem 182(1):136–140PubMedCrossRefGoogle Scholar
  74. Park C-J et al (2004a) Molecular characterization of pepper germin-like protein as the novel PR-16 family of pathogenesis-related proteins isolated during the resistance response to viral and bacterial infection. Planta 219(5):797–806PubMedCrossRefGoogle Scholar
  75. Park CJ et al (2004b) Pathogenesis-related protein 10 isolated from hot pepper functions as a ribonuclease in an antiviral pathway. Plant J 37(2):186–198PubMedCrossRefGoogle Scholar
  76. Penninckx IA et al (1996) Pathogen-induced systemic activation of a plant defensin gene in Arabidopsis follows a salicylic acid-independent pathway. Plant Cell 8(12):2309–2323PubMedPubMedCentralCrossRefGoogle Scholar
  77. Pieterse CMJ, van Loon LC (1999) Salicylic acid-independent plant defence pathways. Trends Plant Sci 4(2):52–58PubMedCrossRefGoogle Scholar
  78. Pieterse CM et al (1996) Systemic resistance in Arabidopsis induced by biocontrol bacteria is independent of salicylic acid accumulation and pathogenesis-related gene expression. Plant Cell 8(8):1225–1237PubMedPubMedCentralCrossRefGoogle Scholar
  79. Poupard P et al (2003) A wound-and ethephon-inducible PR-10 gene subclass from apple is differentially expressed during infection with a compatible and an incompatible race of Venturia inaequalis. Physiol Mol Plant Pathol 62(1):3–12CrossRefGoogle Scholar
  80. Rauscher M et al (1999) PR-1 protein inhibits the differentiation of rust infection hyphae in leaves of acquired resistant broad bean. Plant J 19(6):625–633PubMedCrossRefGoogle Scholar
  81. Raz V, Fluhr R (1993) Ethylene signal is transduced via protein phosphorylation events in plants. Plant Cell 5(5):523–530PubMedPubMedCentralCrossRefGoogle Scholar
  82. Rezzonico E et al (1998) Transcriptional down-regulation by abscisic acid of pathogenesis-related β-1, 3-glucanase genes in tobacco cell cultures. Plant Physiol 117(2):585–592PubMedPubMedCentralCrossRefGoogle Scholar
  83. Robert N et al (2001) Molecular characterization of the incompatible interaction of Vitis vinifera leaves with Pseudomonas syringae pv. pisi: expression of genes coding for stilbene synthase and class 10 PR protein. Eur J Plant Pathol 107(2):249–261CrossRefGoogle Scholar
  84. Rohe M et al (1995) The race-specific elicitor, NIP1, from the barley pathogen, Rhynchosporium secalis, determines avirulence on host plants of the Rrs1 resistance genotype. EMBO J 14(17):4168PubMedPubMedCentralGoogle Scholar
  85. Rohini VK, Rao KS (2001) Transformation of peanut (Arachis hypogaea L.) with tobacco chitinase gene: variable response of transformants to leaf spot disease. Plant Sci 160(5):889–898PubMedCrossRefGoogle Scholar
  86. Roulin S et al (1997) Expression of specific (1→ 3)-β-glucanase genes in leaves of near-isogenic resistant and susceptible barley lines infected with the leaf scald fungus (Rhynchosporium secalis). Physiol Mol Plant Pathol 50(4):245–261CrossRefGoogle Scholar
  87. Rushton PJ, Somssich IE (1998) Transcriptional control of plant genes responsive to pathogens. Curr Opin Plant Biol 1(4):311–315PubMedCrossRefGoogle Scholar
  88. Rushton PJ et al (1996) Interaction of elicitor-induced DNA-binding proteins with elicitor response elements in the promoters of parsley PR1 genes. EMBO J 15(20):5690PubMedPubMedCentralGoogle Scholar
  89. Ryals JA et al (1996) Systemic acquired resistance. Plant Cell 8(10):1809PubMedPubMedCentralCrossRefGoogle Scholar
  90. Schlumbaum A et al (1986) Plant chitinases are potent inhibitors of fungal growthGoogle Scholar
  91. Scofield SR et al (1996) Molecular basis of gene-for-gene specificity in bacterial speck disease of tomato. Science 274(5295):2063PubMedCrossRefGoogle Scholar
  92. Sela-Buurlage MB et al (1993) Only specific tobacco (Nicotiana tabacum) chitinases and β-1, 3-glucanases exhibit antifungal activity. Plant Physiol 101(3):857–863PubMedPubMedCentralCrossRefGoogle Scholar
  93. Selitrennikoff CP (2001) Antifungal proteins. Appl Environ Microbiol 67(7):2883–2894PubMedPubMedCentralCrossRefGoogle Scholar
  94. Sharma V (2013) Pathogenesis related defence functions of plant Chitinases and β-1, 3-Glucanases. Vegetos-An Int J Plant Res 26(2s):205–218CrossRefGoogle Scholar
  95. Simmons CR (1994) The physiology and molecular biology of plant 1, 3-β-D-glucanases and 1, 3; 1, 4-β-D-glucanases. Crit Rev Plant Sci 13(4):325–387Google Scholar
  96. Sinha M et al (2014) Current overview of allergens of plant pathogenesis related protein families. Sci World J 2014:543195Google Scholar
  97. Suarez V et al (2001) Substrate specificity and antifungal activity of recombinant tobacco class I chitinases. Plant Mol Biol 45(5):609–618PubMedCrossRefGoogle Scholar
  98. Tang X et al (1996) Initiation of plant disease resistance by physical interaction of AvrPto and Pto kinase. Science 274:5295–2060CrossRefGoogle Scholar
  99. Thalmair M et al (1996) Ozone and ultraviolet B effects on the defense-related proteins ß-1, 3-glucanase and chitinase in tobacco. J Plant Physiol 148(1):222–228CrossRefGoogle Scholar
  100. Thomma BPHJ et al (1998) Separate jasmonate-dependent and salicylate-dependent defense-response pathways in Arabidopsis are essential for resistance to distinct microbial pathogens. Proc Natl Acad Sci 95(25):15107–15111PubMedPubMedCentralCrossRefGoogle Scholar
  101. Tonón C et al (2002) Isolation of a potato acidic 39 kDa β-1, 3-glucanase with antifungal activity against Phytophthora infestans and analysis of its expression in potato cultivars differing in their degrees of field resistance. J Phytopathol 150(4–5):189–195CrossRefGoogle Scholar
  102. Van Loon LC (1997) Induced resistance in plants and the role of pathogenesis-related proteins. Eur J Plant Pathol 103(9):753–765CrossRefGoogle Scholar
  103. Van Loon LC (1999) Occurrence and properties of plant pathogenesis-related proteins. In: Datta SK, Muthukrishnan S (eds) Pathogenesis-related proteins in plants, CRC press, Boca Raton, p 1–19Google Scholar
  104. Van Loon LC, van Kammen A (1970) Polyacrylamide disc electrophoresis of the soluble leaf proteins from Nicotiana tabacum var. “Samsun” and “Samsun NN”. II. Changes in protein constitution after infection with tobacco mosaic virus. Virology 40(2):190–211PubMedGoogle Scholar
  105. Van Loon LC, Van Strien EA (1999) The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins. Physiol Mol Plant Pathol 55(2):85–97CrossRefGoogle Scholar
  106. Van Loon LC et al (1994) Recommendations for naming plant pathogenesis-related proteins. Plant Mol Biol Report 12(3):245–264CrossRefGoogle Scholar
  107. Van Loon LC et al (1998) Systemic resistance induced by rhizosphere bacteria. Annu Rev Phytopathol 36(1):453–483PubMedCrossRefGoogle Scholar
  108. Vigers AJ et al (1992) Thaumatin-like pathogenesis-related proteins are antifungal. Plant Sci 83(2):155–161CrossRefGoogle Scholar
  109. Vleeshouwers VGAA et al (2000) Does basal PR gene expression in Solanum species contribute to non-specific resistance to Phytophthora infestans? Physiol Mol Plant Pathol 57(1):35–42CrossRefGoogle Scholar
  110. Vögeli-Lange R et al (1994) Developmental, hormonal, and pathogenesis-related regulation of the tobacco class I β-1, 3-glucanase B promoter. Plant Mol Biol 25(2):299–311PubMedCrossRefGoogle Scholar
  111. Ward ER et al (1991) Coordinate gene activity in response to agents that induce systemic acquired resistance. Plant Cell 3(10):1085–1094PubMedPubMedCentralCrossRefGoogle Scholar
  112. Wu C-T, Bradford KJ (2003) Class I chitinase and β-1, 3-glucanase are differentially regulated by wounding, methyl jasmonate, ethylene, and gibberellin in tomato seeds and leaves. Plant Physiol 133(1):263–273PubMedPubMedCentralCrossRefGoogle Scholar
  113. Wubben JP et al (1996) Differential induction of chitinase and 1, 3-β-glucanase gene expression in tomato by Cladosporium fulvum and its race-specific elicitors. Physiol Mol Plant Pathol 48(2):105–116CrossRefGoogle Scholar
  114. Wyatt SE et al (1991) β-1, 3-glucanase, chitinase, and peroxidase activities in tobacco tissues resistant and susceptible to blue mould as related to flowering, age and sucker development. Physiol Mol Plant Pathol 39(6):433–440CrossRefGoogle Scholar
  115. Xu YI et al (1994) Plant defense genes are synergistically induced by ethylene and methyl jasmonate. Plant Cell 6(8):1077–1085PubMedPubMedCentralCrossRefGoogle Scholar
  116. Yalpani N et al (1991) Salicylic acid is a systemic signal and an inducer of pathogenesis-related proteins in virus-infected tobacco. Plant Cell 3(8):809–818PubMedPubMedCentralCrossRefGoogle Scholar
  117. Yamamoto T et al (2000) Transgenic grapevine plants expressing a rice chitinase with enhanced resistance to fungal pathogens. Plant Cell Rep 19(7):639–646CrossRefGoogle Scholar
  118. Yang Y et al (1997) Signal perception and transduction in plant defense responses. Genes Dev 11(13):1621–1639PubMedCrossRefGoogle Scholar
  119. Yeh S et al (2000) Chitinase genes responsive to cold encode antifreeze proteins in winter cereals. Plant Physiol 124(3):1251–1264PubMedPubMedCentralCrossRefGoogle Scholar
  120. Zemanek AB et al (2002) Changes in β-1, 3-glucanase mRNA levels in peach in response to treatment with pathogen culture filtrates, wounding, and other elicitors. J Plant Physiol 159(8):877–889CrossRefGoogle Scholar
  121. Zhou J et al (1997) The Pto kinase conferring resistance to tomato bacterial speck disease interacts with proteins that bind a cis-element of pathogenesis-related genes. EMBO J 16(11):3207–3218PubMedPubMedCentralCrossRefGoogle Scholar
  122. Zhu Q et al (1994) Enhanced protection against fungal attack by constitutive Co-expression of Chitinase and glucanase genes in transgenic tobacco. Bio/Technology 12:807–812Google Scholar

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© Springer Nature Singapore Pte Ltd. 2018

Authors and Affiliations

  1. 1.Interdisciplinary Centre for Plant Genomics, Department of Plant Molecular BiologyDelhi University-South CampusNew DelhiIndia

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