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Volumn 6, Issue AUG, 2015, Pages

The battle in the apoplast: Further insights into the roles of proteases and their inhibitors in plant–pathogen interactions

Author keywords

Chitinase; Cysteine protease; Defence; Metalloprotease; Protease inhibitor; Serine protease

Indexed keywords


EID: 84938835638     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2015.00584     Document Type: Article
Times cited : (170)

References (62)
  • 1
    • 84862672227 scopus 로고    scopus 로고
    • Enhancing transgenic pea (Pisum sativum L.) resistance against fungal diseases through stacking of two antifungal genes (chitinase and glucanase)
    • Amian, A. A., Papenbrock, J., Jacobsen, H. J., and Hassan, F. (2011). Enhancing transgenic pea (Pisum sativum L.) resistance against fungal diseases through stacking of two antifungal genes (chitinase and glucanase). GM Crops 2, 104-109. doi: 10. 4161/gmcr. 2. 2. 16125.
    • (2011) GM Crops , vol.2 , pp. 104-109
    • Amian, A.A.1    Papenbrock, J.2    Jacobsen, H.J.3    Hassan, F.4
  • 2
    • 0842323769 scopus 로고    scopus 로고
    • Potato oxysterol binding protein and cathepsin B are rapidly up-regulated in independent defence pathways that distinguish R gene-mediated and field resistances to Phytophthora infestans
    • Avrova, A. O., Taleb, N., Rokka, V. M., Heilbronn, J., Campbell, E., Hein, I., et al. (2004). Potato oxysterol binding protein and cathepsin B are rapidly up-regulated in independent defence pathways that distinguish R gene-mediated and field resistances to Phytophthora infestans. Mol. Plant Pathol. 5, 45-56. doi: 10. 1111/j. 1364-3703. 2004. 00205. x.
    • (2004) Mol. Plant Pathol , vol.5 , pp. 45-56
    • Avrova, A.O.1    Taleb, N.2    Rokka, V.M.3    Heilbronn, J.4    Campbell, E.5    Hein, I.6
  • 3
    • 84867103592 scopus 로고    scopus 로고
    • Plant β-1, 3-glucanases: Their biological functions and transgenic expression against phytopathogenic fungi
    • Balasubramanian, V., Vashisht, D., Cletus, J., and Sakthivel, N. (2012). Plant β-1, 3-glucanases: their biological functions and transgenic expression against phytopathogenic fungi. Biotechnol. Lett. 34, 1983-1990. doi: 10. 1007/s10529-012-1012-6.
    • (2012) Biotechnol. Lett , vol.34 , pp. 1983-1990
    • Balasubramanian, V.1    Vashisht, D.2    Cletus, J.3    Sakthivel, N.4
  • 4
    • 84855489042 scopus 로고    scopus 로고
    • Phytophthora infestans effector Avrblb2 prevents secretion of a plant immune protease at the haustorial interface
    • Bozkurt, T. O., Schornack, S., Win, J., Shindo, T., Ilyas, M., Oliva, R., et al. (2011). Phytophthora infestans effector Avrblb2 prevents secretion of a plant immune protease at the haustorial interface. Proc. Natl. Acad. Sci. U. S. A. 108, 20832-20837. doi: 10. 1073/pnas. 1112708109.
    • (2011) Proc. Natl. Acad. Sci. U.S.A , vol.108 , pp. 20832-20837
    • Bozkurt, T.O.1    Schornack, S.2    Win, J.3    Shindo, T.4    Ilyas, M.5    Oliva, R.6
  • 5
    • 68149161684 scopus 로고    scopus 로고
    • Evolution of a subtilisin-like protease gene family in the grass endophytic fungus Epichloë festucae
    • Bryant, M. K., Schardl, C. L., Hesse, U., and Scott, B. (2009). Evolution of a subtilisin-like protease gene family in the grass endophytic fungus Epichloë festucae. BMC Evol. Biol. 9: 168. doi: 10. 1186/1471-2148-9-168.
    • (2009) BMC Evol. Biol , vol.9 , pp. 168
    • Bryant, M.K.1    Schardl, C.L.2    Hesse, U.3    Scott, B.4
  • 6
    • 84885637689 scopus 로고    scopus 로고
    • Transgenic expression of plant chitinases to enhance disease resistance
    • Cletus, J., Balasubramanian, V., Vashisht, D., and Sakthivel, N. (2013). Transgenic expression of plant chitinases to enhance disease resistance. Biotechnol. Lett. 35, 1719-1732. doi: 10. 1007/s10529-013-1269-4.
    • (2013) Biotechnol. Lett , vol.35 , pp. 1719-1732
    • Cletus, J.1    Balasubramanian, V.2    Vashisht, D.3    Sakthivel, N.4
  • 7
    • 33750036094 scopus 로고    scopus 로고
    • Transgenic tobacco plants overexpressing chitinases of fungal origin show enhanced resistance to biotic and abiotic stress agents
    • de las Mercedes Dana, M., Pintor-Toro, J. A., and Cubero, B. (2006). Transgenic tobacco plants overexpressing chitinases of fungal origin show enhanced resistance to biotic and abiotic stress agents. Plant Physiol. 142, 722-730. doi: 10. 1104/pp. 106. 086140.
    • (2006) Plant Physiol , vol.142 , pp. 722-730
    • de las Mercedes Dana, M.1    Pintor-Toro, J.A.2    Cubero, B.3
  • 8
    • 84870667343 scopus 로고    scopus 로고
    • The genomes of the fungal plant pathogens Cladosporium fulvum and Dothistroma septosporum reveal adaptation to different hosts and lifestyles but also signatures of common ancestry
    • de Wit, P. J. G. M, van der Burgt, A., Ökmen, B., Stergiopoulos, I., Abd-Elsalam, K. A., Aerts, A. L., et al. (2012). The genomes of the fungal plant pathogens Cladosporium fulvum and Dothistroma septosporum reveal adaptation to different hosts and lifestyles but also signatures of common ancestry. PLoS Genet. 8: e1003088. doi: 10. 1371/journal. pgen. 1003088.
    • (2012) PLoS Genet , vol.8
    • de Wit, P.J.G.M.1    van der Burgt, A.2    Ökmen, B.3    Stergiopoulos, I.4    Abd-Elsalam, K.A.5    Aerts, A.L.6
  • 9
    • 0034255023 scopus 로고    scopus 로고
    • Genetic complexity of pathogen perception by plants: The example of Rcr3, a tomato gene required specifically by Cf-2
    • Dixon, M. S., Golstein, C., Thomas, C. M., van der Biezen, E. A., and Jones, J. D. G. (2000). Genetic complexity of pathogen perception by plants: the example of Rcr3, a tomato gene required specifically by Cf-2. Proc. Natl. Acad. Sci. U. S. A. 97, 8807-8814. doi: 10. 1073/pnas. 97. 16. 8807.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 8807-8814
    • Dixon, M.S.1    Golstein, C.2    Thomas, C.M.3    van der Biezen, E.A.4    Jones, J.D.G.5
  • 10
    • 84893146052 scopus 로고    scopus 로고
    • Effector specialization in a lineage of the Irish potato famine pathogen
    • Dong, S., Stam, R., Cano, L. M., Song, J., Sklenar, J., Yoshida, K., et al. (2014). Effector specialization in a lineage of the Irish potato famine pathogen. Science 343, 552-555. doi: 10. 1126/science. 1246300.
    • (2014) Science , vol.343 , pp. 552-555
    • Dong, S.1    Stam, R.2    Cano, L.M.3    Song, J.4    Sklenar, J.5    Yoshida, K.6
  • 11
    • 84864588388 scopus 로고    scopus 로고
    • Balancing selection at the tomato Rcr3 guardee gene family maintains variation in strength of pathogen defense
    • Hörger, A. C., Ilyas, M., Stephan, W., Tellier, A., van der Hoorn, R. A. L., and Rose, L. E. (2012). Balancing selection at the tomato Rcr3 guardee gene family maintains variation in strength of pathogen defense. PLoS Genet. 8: e1002813. doi: 10. 1371/journal. pgen. 1002813.
    • (2012) PLoS Genet , vol.8
    • Hörger, A.C.1    Ilyas, M.2    Stephan, W.3    Tellier, A.4    van der Hoorn, R.A.L.5    Rose, L.E.6
  • 12
    • 84888434209 scopus 로고    scopus 로고
    • The structural basis of specific protease-inhibitor interactions at the plant-pathogen interface
    • Hörger, A. C., and van der Hoorn, R. A. L. (2013). The structural basis of specific protease-inhibitor interactions at the plant-pathogen interface. Curr. Opin. Struct. Biol. 23, 842-850. doi: 10. 1016/j. sbi. 2013. 07. 013.
    • (2013) Curr. Opin. Struct. Biol , vol.23 , pp. 842-850
    • Hörger, A.C.1    van der Hoorn, R.A.L.2
  • 13
    • 84856244145 scopus 로고    scopus 로고
    • Overexpression of rice chitinase gene in transgenic peanut (Arachis hypogaea L.) improves resistance against leaf spot
    • Iqbal, M., Nazir, F., Ali, S., Asif, M. A., Zafar, Y., Iqbal, J., et al. (2012). Overexpression of rice chitinase gene in transgenic peanut (Arachis hypogaea L.) improves resistance against leaf spot. Mol. Biotechnol. 50, 129-136. doi: 10. 1007/s12033-011-9426-2.
    • (2012) Mol. Biotechnol , vol.50 , pp. 129-136
    • Iqbal, M.1    Nazir, F.2    Ali, S.3    Asif, M.A.4    Zafar, Y.5    Iqbal, J.6
  • 14
    • 0027666351 scopus 로고
    • The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity
    • Iseli, B., Boller, T., and Neuhaus, J. M. (1993). The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity. Plant Physiol. 103, 221-226. doi: 10. 1104/pp. 103. 1. 221.
    • (1993) Plant Physiol , vol.103 , pp. 221-226
    • Iseli, B.1    Boller, T.2    Neuhaus, J.M.3
  • 15
    • 33751100626 scopus 로고    scopus 로고
    • The plant immune system
    • Jones, J. D. G., and Dangl, J. L. (2006). The plant immune system. Nature 444, 323-329. doi: 10. 1038/nature05286.
    • (2006) Nature , vol.444 , pp. 323-329
    • Jones, J.D.G.1    Dangl, J.L.2
  • 16
    • 84942543899 scopus 로고    scopus 로고
    • Synergistic action of a metalloprotease and a serine protease from Fusarium oxysporum f. sp. lycopersici cleaves chitin-binding tomato chitinases, reduces their antifungal activity and enhances fungal virulence
    • Karimi Jashni, M., Dols, H. M. I., Iida, Y., Boeren, S., Beenen, H. G., Mehrabi, R., et al. (2015). Synergistic action of a metalloprotease and a serine protease from Fusarium oxysporum f. sp. lycopersici cleaves chitin-binding tomato chitinases, reduces their antifungal activity and enhances fungal virulence. Mol. Plant Microbe Interact. doi: 10. 1094/MPMI-04-15-0074-R [Epub ahead of print].
    • (2015) Mol. Plant Microbe Interact
    • Karimi Jashni, M.1    Dols, H.M.I.2    Iida, Y.3    Boeren, S.4    Beenen, H.G.5    Mehrabi, R.6
  • 17
    • 78649768763 scopus 로고    scopus 로고
    • An effector-targeted protease contributes to defense against Phytophthora infestans and is under diversifying selection in natural hosts
    • Kaschani, F., Shabab, M., Bozkurt, T., Shindo, T., Schornack, S., Gu, C., et al. (2010). An effector-targeted protease contributes to defense against Phytophthora infestans and is under diversifying selection in natural hosts. Plant Physiol. 154, 1794-1804. doi: 10. 1104/pp. 110. 158030.
    • (2010) Plant Physiol , vol.154 , pp. 1794-1804
    • Kaschani, F.1    Shabab, M.2    Bozkurt, T.3    Shindo, T.4    Schornack, S.5    Gu, C.6
  • 18
    • 67649671753 scopus 로고    scopus 로고
    • Protease inhibitors from plants with antimicrobial activity
    • Kim, J. Y., Park, S. C., Hwang, I., Cheong, H., Nah, J. W., Hahm, K. S., et al. (2009). Protease inhibitors from plants with antimicrobial activity. Int. J. Mol. Sci. 10, 2860-2872. doi: 10. 3390/ijms10062860.
    • (2009) Int. J. Mol. Sci , vol.10 , pp. 2860-2872
    • Kim, J.Y.1    Park, S.C.2    Hwang, I.3    Cheong, H.4    Nah, J.W.5    Hahm, K.S.6
  • 19
    • 0037177596 scopus 로고    scopus 로고
    • A tomato cysteine protease required for Cf-2-dependent disease resistance and suppression of autonecrosis
    • Krüger, J., Thomas, C. M., Golstein, C., Dixon, M. S., Smoker, M., Tang, S., et al. (2002). A tomato cysteine protease required for Cf-2-dependent disease resistance and suppression of autonecrosis. Science 296, 744-747. doi: 10. 1126/science. 1069288.
    • (2002) Science , vol.296 , pp. 744-747
    • Krüger, J.1    Thomas, C.M.2    Golstein, C.3    Dixon, M.S.4    Smoker, M.5    Tang, S.6
  • 20
    • 84860389243 scopus 로고    scopus 로고
    • The Arabidopsis extracellular unusual serine protease inhibitor functions in resistance to necrotrophic fungi and insect herbivory
    • Laluk, K., and Mengiste, T. (2011). The Arabidopsis extracellular unusual serine protease inhibitor functions in resistance to necrotrophic fungi and insect herbivory. Plant J. 68, 480-494. doi: 10. 1111/j. 1365-313X. 2011. 04702. x.
    • (2011) Plant J , vol.68 , pp. 480-494
    • Laluk, K.1    Mengiste, T.2
  • 21
    • 0030220995 scopus 로고    scopus 로고
    • Proteolytic processing of class IV chitinase in the compatible interaction of bean roots with Fusarium solani
    • Lange, J., Mohr, U., Wiemken, A., Boller, T., and Vögeli-Lange, R. (1996). Proteolytic processing of class IV chitinase in the compatible interaction of bean roots with Fusarium solani. Plant Physiol. 111, 1135-1144. doi: 10. 1104/pp. 111. 4. 1135.
    • (1996) Plant Physiol , vol.111 , pp. 1135-1144
    • Lange, J.1    Mohr, U.2    Wiemken, A.3    Boller, T.4    Vögeli-Lange, R.5
  • 22
    • 84862580444 scopus 로고    scopus 로고
    • Dual disease resistance mediated by the immune receptor Cf-2 in tomato requires a common virulence target of a fungus and a nematode
    • Lozano-Torres, J. L., Wilbers, R. H. P., Gawronski, P., Boshoven, J. C., Finkers-Tomczak, A., Cordewener, J. H. G., et al. (2012). Dual disease resistance mediated by the immune receptor Cf-2 in tomato requires a common virulence target of a fungus and a nematode. Proc. Natl. Acad. Sci. U. S. A. 109, 10119-10124. doi: 10. 1073/pnas. 1202867109.
    • (2012) Proc. Natl. Acad. Sci. U.S.A , vol.109 , pp. 10119-10124
    • Lozano-Torres, J.L.1    Wilbers, R.H.P.2    Gawronski, P.3    Boshoven, J.C.4    Finkers-Tomczak, A.5    Cordewener, J.H.G.6
  • 23
    • 33747826864 scopus 로고    scopus 로고
    • Over-expression of a cacao class I chitinase gene in Theobroma cacao L. Enhances resistance against the pathogen, Colletotrichum gloeosporioides
    • Maximova, S., Marelli, J. P., Young, A., Pishak, S., Verica, J., and Guiltinan, M. (2006). Over-expression of a cacao class I chitinase gene in Theobroma cacao L. Enhances resistance against the pathogen, Colletotrichum gloeosporioides. Planta 224, 740-749. doi: 10. 1007/s00425-005-0188-6.
    • (2006) Planta , vol.224 , pp. 740-749
    • Maximova, S.1    Marelli, J.P.2    Young, A.3    Pishak, S.4    Verica, J.5    Guiltinan, M.6
  • 24
    • 84957850427 scopus 로고    scopus 로고
    • A conserved proline residue in Dothideomycete Avr4 effector proteins is required to trigger a Cf-4-dependent hypersensitive response
    • Mesarich, C. H., Stergiopoulos, I., Beenen, H. G., Cordovez, V., Guo, Y., Karimi Jashni, M., et al. (2015). A conserved proline residue in Dothideomycete Avr4 effector proteins is required to trigger a Cf-4-dependent hypersensitive response Mol. Plant Pathol. doi: 10. 1111/mpp. 12265 [Epub ahead of print].
    • (2015) Mol. Plant Pathol
    • Mesarich, C.H.1    Stergiopoulos, I.2    Beenen, H.G.3    Cordovez, V.4    Guo, Y.5    Karimi Jashni, M.6
  • 25
    • 23044525385 scopus 로고    scopus 로고
    • Involvement of proteolytic enzymes and their inhibitors in plant protection (review)
    • Mosolov, V. V., Grigor'eva, L. I., and Valueva, T. A. (2001). Involvement of proteolytic enzymes and their inhibitors in plant protection (review). Appl. Biochem. Microbiol. 37, 115-123. doi: 10. 1023/A: 1002824527463.
    • (2001) Appl. Biochem. Microbiol , vol.37 , pp. 115-123
    • Mosolov, V.V.1    Grigor'eva, L.I.2    Valueva, T.A.3
  • 26
    • 84874787430 scopus 로고    scopus 로고
    • Compatibility in the Ustilago maydis-maize interaction requires inhibition of host cysteine proteases by the fungal effector Pit2
    • Mueller, A. N., Ziemann, S., Treitschke, S., Aßmann, D., and Doehlemann, G. (2013). Compatibility in the Ustilago maydis-maize interaction requires inhibition of host cysteine proteases by the fungal effector Pit2. PLoS Pathog. 9: e1003177. doi: 10. 1371/journal. ppat. 1003177.
    • (2013) PLoS Pathog , vol.9
    • Mueller, A.N.1    Ziemann, S.2    Treitschke, S.3    Aßmann, D.4    Doehlemann, G.5
  • 27
    • 79953269003 scopus 로고    scopus 로고
    • Modification of recombinant maize ChitA chitinase by fungal chitinase-modifying proteins
    • Naumann, T. A. (2011). Modification of recombinant maize ChitA chitinase by fungal chitinase-modifying proteins. Mol. Plant Pathol. 12, 365-372. doi: 10. 1111/j. 1364-3703. 2010. 00677. x.
    • (2011) Mol. Plant Pathol , vol.12 , pp. 365-372
    • Naumann, T.A.1
  • 28
    • 84938821897 scopus 로고    scopus 로고
    • Polyglycine hydrolases: Fungal β-lactamase-like endoproteases that cleave polyglycine regions within plant class IV chitinases
    • Naumann, T. A., Naldrett, M. J., Ward, T. J., and Price, N. P. J. (2015). Polyglycine hydrolases: fungal β-lactamase-like endoproteases that cleave polyglycine regions within plant class IV chitinases. Protein Sci. 24, 1147-1157. doi: 10. 1002/pro. 2705.
    • (2015) Protein Sci , vol.24 , pp. 1147-1157
    • Naumann, T.A.1    Naldrett, M.J.2    Ward, T.J.3    Price, N.P.J.4
  • 29
    • 80053928338 scopus 로고    scopus 로고
    • Identification of a chitinase-modifying protein from Fusarium verticillioides
    • Naumann, T. A., Wicklow, D. T., and Price, N. P. J. (2011). Identification of a chitinase-modifying protein from Fusarium verticillioides. J. Biol. Chem. 286, 35358-35366. doi: 10. 1074/jbc. M111. 279646.
    • (2011) J. Biol. Chem , vol.286 , pp. 35358-35366
    • Naumann, T.A.1    Wicklow, D.T.2    Price, N.P.J.3
  • 30
    • 84900500040 scopus 로고    scopus 로고
    • Polyglycine hydrolases secreted by Pleosporineae fungi that target the linker region of plant class IV chitinases
    • Naumann, T. A., Wicklow, D. T., and Price, N. P. J. (2014). Polyglycine hydrolases secreted by Pleosporineae fungi that target the linker region of plant class IV chitinases. Biochem. J. 460, 187-198. doi: 10. 1042/BJ20140268.
    • (2014) Biochem. J , vol.460 , pp. 187-198
    • Naumann, T.A.1    Wicklow, D.T.2    Price, N.P.J.3
  • 31
    • 84868159385 scopus 로고    scopus 로고
    • Diverse lifestyles and strategies of plant pathogenesis encoded in the genomes of eighteenDothideomycetes fungi
    • Ohm, R. A., Feau, N., Henrissat, B., Schoch, C. L., Horwitz, B. A., Barry, K. W., et al. (2012). Diverse lifestyles and strategies of plant pathogenesis encoded in the genomes of eighteenDothideomycetes fungi. PLoS Pathog. 8: e1003037. doi: 10. 1371/journal. ppat. 1003037.
    • (2012) PLoS Pathog , vol.8
    • Ohm, R.A.1    Feau, N.2    Henrissat, B.3    Schoch, C.L.4    Horwitz, B.A.5    Barry, K.W.6
  • 32
    • 0036187423 scopus 로고    scopus 로고
    • Characterization of an extracellular serine protease of Fusarium eumartii and its action on pathogenesis related proteins
    • Olivieri, F., Eugenia Zanetti, M., Oliva, C. R., Covarrubias, A. A., and Casalongué, C. A. (2002). Characterization of an extracellular serine protease of Fusarium eumartii and its action on pathogenesis related proteins. Eur. J. Plant Pathol. 108, 63-72. doi: 10. 1023/A: 1013920929965.
    • (2002) Eur. J. Plant Pathol , vol.108 , pp. 63-72
    • Olivieri, F.1    Eugenia Zanetti, M.2    Oliva, C.R.3    Covarrubias, A.A.4    Casalongué, C.A.5
  • 33
    • 34247251798 scopus 로고    scopus 로고
    • Kinetics of the inhibition of Fusariumserine proteinases by barley (Hordeum vulgare L.) inhibitors
    • Pekkarinen, A. I., Longstaff, C., and Jones, B. L. (2007). Kinetics of the inhibition of Fusariumserine proteinases by barley (Hordeum vulgare L.) inhibitors. J. Agric. Food Chem. 55, 2736-2742. doi: 10. 1021/jf0631777.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 2736-2742
    • Pekkarinen, A.I.1    Longstaff, C.2    Jones, B.L.3
  • 34
    • 1842482426 scopus 로고    scopus 로고
    • Analysis of a secreted aspartic peptidase disruption mutant of Glomerella cingulata
    • Plummer, K. M., Clark, S. J., Ellis, L. M., Loganathan, A., Al-Samarrai, T. H., Rikkerink, E. H. A., et al. (2004). Analysis of a secreted aspartic peptidase disruption mutant of Glomerella cingulata. Eur. J. Plant Pathol. 110, 265-274. doi: 10. 1023/b: ejpp. 0000019796. 78598. 8c.
    • (2004) Eur. J. Plant Pathol , vol.110 , pp. 265-274
    • Plummer, K.M.1    Clark, S.J.2    Ellis, L.M.3    Loganathan, A.4    Al-Samarrai, T.H.5    Rikkerink, E.H.A.6
  • 35
    • 20544475699 scopus 로고    scopus 로고
    • Cladosporium Avr2 inhibits tomato Rcr3 protease required for Cf-2-dependent disease resistance
    • Rooney, H. C. E., van't Klooster, J. W., van der Hoorn, R. A. L., Joosten, M. H. A. J., Jones, J. D. G., and de Wit, P. J. (2005). Cladosporium Avr2 inhibits tomato Rcr3 protease required for Cf-2-dependent disease resistance. Science 308, 1783-1786. doi: 10. 1126/science. 1111404.
    • (2005) Science , vol.308 , pp. 1783-1786
    • Rooney, H.C.E.1    van't Klooster, J.W.2    van der Hoorn, R.A.L.3    Joosten, M.H.A.J.4    Jones, J.D.G.5    de Wit, P.J.6
  • 36
    • 0000180578 scopus 로고
    • Protease inhibitors in plants: Genes for improving defenses against insects and pathogens
    • Ryan, C. A. (1990). Protease inhibitors in plants: genes for improving defenses against insects and pathogens. Annu. Rev. Phytopathol. 28, 425-449. doi: 10. 1146/annurev. py. 28. 090190. 002233.
    • (1990) Annu. Rev. Phytopathol , vol.28 , pp. 425-449
    • Ryan, C.A.1
  • 37
    • 0030834003 scopus 로고    scopus 로고
    • Heterologous chitinase gene expression to improve plant defense against phytopathogenic fungi
    • Schickler, H., and Chet, I. (1997). Heterologous chitinase gene expression to improve plant defense against phytopathogenic fungi. J. Ind. Microbiol. Biotechnol. 19, 196-201. doi: 10. 1038/sj. jim. 2900447.
    • (1997) J. Ind. Microbiol. Biotechnol , vol.19 , pp. 196-201
    • Schickler, H.1    Chet, I.2
  • 40
    • 48049091892 scopus 로고    scopus 로고
    • Fungal effector protein AVR2 targets diversifying defense-related Cys proteases of tomato
    • Shabab, M., Shindo, T., Gu, C., Kaschani, F., Pansuriya, T., Chintha, R., et al. (2008). Fungal effector protein AVR2 targets diversifying defense-related Cys proteases of tomato. Plant Cell 20, 1169-1183. doi: 10. 1105/tpc. 107. 056325.
    • (2008) Plant Cell , vol.20 , pp. 1169-1183
    • Shabab, M.1    Shindo, T.2    Gu, C.3    Kaschani, F.4    Pansuriya, T.5    Chintha, R.6
  • 41
    • 84915746092 scopus 로고    scopus 로고
    • Novel mode of action of plant defense peptides-hevein-like antimicrobial peptides from wheat inhibit fungal metallo-proteases
    • Slavokhotova, A. A., Naumann, T. A., Price, N. P. J., Rogozhin, E. A., Andreev, Y. A., Vassilevski, A. A., et al. (2014). Novel mode of action of plant defense peptides-hevein-like antimicrobial peptides from wheat inhibit fungal metallo-proteases. FEBS J. 281, 4754-4764. doi: 10. 1111/febs. 13015.
    • (2014) FEBS J , vol.281 , pp. 4754-4764
    • Slavokhotova, A.A.1    Naumann, T.A.2    Price, N.P.J.3    Rogozhin, E.A.4    Andreev, Y.A.5    Vassilevski, A.A.6
  • 42
    • 60849124275 scopus 로고    scopus 로고
    • Apoplastic effectors secreted by two unrelated eukaryotic plant pathogens target the tomato defense protease Rcr3
    • Song, J., Win, J., Tian, M., Schornack, S., Kaschani, F., Ilyas, M., et al. (2009). Apoplastic effectors secreted by two unrelated eukaryotic plant pathogens target the tomato defense protease Rcr3. Proc. Natl. Acad. Sci. U. S. A. 106, 1654-1659. doi: 10. 1073/pnas. 0809201106.
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 1654-1659
    • Song, J.1    Win, J.2    Tian, M.3    Schornack, S.4    Kaschani, F.5    Ilyas, M.6
  • 43
    • 84856170491 scopus 로고    scopus 로고
    • How do plants achieve immunity? Defence without specialized immune cells
    • Spoel, S. H., and Dong, X. (2012). How do plants achieve immunity? Defence without specialized immune cells. Nat. Rev. Immunol. 12, 89-100. doi: 10. 1038/nri3141.
    • (2012) Nat. Rev. Immunol , vol.12 , pp. 89-100
    • Spoel, S.H.1    Dong, X.2
  • 44
    • 47549112457 scopus 로고    scopus 로고
    • Combined expression of chitinase and β-1, 3-glucanase genes in indica rice (Oryza sativa L.) enhances resistance against Rhizoctonia solani
    • Sridevi, G., Parameswari, C., Sabapathi, N., Raghupathy, V., and Veluthambi, K. (2008). Combined expression of chitinase and β-1, 3-glucanase genes in indica rice (Oryza sativa L.) enhances resistance against Rhizoctonia solani. Plant Sci. 175, 283-290. doi: 10. 1016/j. plantsci. 2008. 04. 011.
    • (2008) Plant Sci , vol.175 , pp. 283-290
    • Sridevi, G.1    Parameswari, C.2    Sabapathi, N.3    Raghupathy, V.4    Veluthambi, K.5
  • 45
    • 67649550674 scopus 로고    scopus 로고
    • Fungal effector proteins
    • Stergiopoulos, I., and de Wit, P. J. (2009). Fungal effector proteins. Annu. Rev. Phytopathol. 47, 233-263. doi: 10. 1146/annurev. phyto. 112408. 132637.
    • (2009) Annu. Rev. Phytopathol , vol.47 , pp. 233-263
    • Stergiopoulos, I.1    de Wit, P.J.2
  • 46
    • 77952190425 scopus 로고    scopus 로고
    • Tomato Cf resistance proteins mediate recognition of cognate homologous effectors from fungi pathogenic on dicots and monocots
    • Stergiopoulos, I., van den Burg, H. A., Ökmen, B., Beenen, H. G., van Liere, S., Kema, G. H. J., et al. (2010). Tomato Cf resistance proteins mediate recognition of cognate homologous effectors from fungi pathogenic on dicots and monocots. Proc. Natl. Acad. Sci. U. S. A. 107, 7610-7615. doi: 10. 1073/pnas. 1002910107.
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 7610-7615
    • Stergiopoulos, I.1    van den Burg, H.A.2    Ökmen, B.3    Beenen, H.G.4    van Liere, S.5    Kema, G.H.J.6
  • 47
    • 0034987652 scopus 로고    scopus 로고
    • Substrate specificity and antifungal activity of recombinant tobacco class I chitinases
    • Suarez, V., Staehelin, C., Arango, R., Holtorf, H., Hofsteenge, J., and Meins, F. Jr. (2001). Substrate specificity and antifungal activity of recombinant tobacco class I chitinases. Plant Mol. Biol. 45, 609-618. doi: 10. 1023/A: 1010619421524.
    • (2001) Plant Mol. Biol , vol.45 , pp. 609-618
    • Suarez, V.1    Staehelin, C.2    Arango, R.3    Holtorf, H.4    Hofsteenge, J.5    Meins, F.6
  • 50
    • 25644432194 scopus 로고    scopus 로고
    • A second Kazal-like protease inhibitor fromPhytophthora infestans inhibits and interacts with the apoplastic pathogenesis-related protease P69b of tomato
    • Tian, M., Benedetti, B., and Kamoun, S. (2005). A second Kazal-like protease inhibitor fromPhytophthora infestans inhibits and interacts with the apoplastic pathogenesis-related protease P69b of tomato. Plant Physiol. 138, 1785-1793. doi: 10. 1104/pp. 105. 061226.
    • (2005) Plant Physiol , vol.138 , pp. 1785-1793
    • Tian, M.1    Benedetti, B.2    Kamoun, S.3
  • 51
    • 2942748298 scopus 로고    scopus 로고
    • A Kazal-like extracellular serine protease inhibitor from Phytophthora infestans targets the tomato pathogenesis-related protease P69b
    • Tian, M., Huitema, E., da Cunha, L., Torto-Alalibo, T., and Kamoun, S. (2004). A Kazal-like extracellular serine protease inhibitor from Phytophthora infestans targets the tomato pathogenesis-related protease P69b. J. Biol. Chem. 279, 26370-26377. doi: 10. 1074/jbc. m400941200.
    • (2004) J. Biol. Chem , vol.279 , pp. 26370-26377
    • Tian, M.1    Huitema, E.2    da Cunha, L.3    Torto-Alalibo, T.4    Kamoun, S.5
  • 52
    • 66649092883 scopus 로고    scopus 로고
    • Arabidopsis actin-depolymerizing factor AtADF4 mediates defense signal transduction triggered by the Pseudomonas syringae effector AvrPphB
    • Tian, M., Chaudhry, F., Ruzicka, D. R., Meagher, R. B., Staiger, C. J., and Day, B. (2009). Arabidopsis actin-depolymerizing factor AtADF4 mediates defense signal transduction triggered by the Pseudomonas syringae effector AvrPphB. Plant Physiol. 150, 815-824. doi: 10. 1104/pp. 109. 137604.
    • (2009) Plant Physiol , vol.150 , pp. 815-824
    • Tian, M.1    Chaudhry, F.2    Ruzicka, D.R.3    Meagher, R.B.4    Staiger, C.J.5    Day, B.6
  • 53
    • 33846379634 scopus 로고    scopus 로고
    • APhytophthora infestans cystatin-like protein targets a novel tomato papain-like apoplastic protease
    • Tian, M., Win, J., Song, J., van der Hoorn, R., van der Knaap, E., and Kamoun, S. (2007). APhytophthora infestans cystatin-like protein targets a novel tomato papain-like apoplastic protease. Plant Physiol. 143, 364-377. doi: 10. 1104/pp. 106. 090050.
    • (2007) Plant Physiol , vol.143 , pp. 364-377
    • Tian, M.1    Win, J.2    Song, J.3    van der Hoorn, R.4    van der Knaap, E.5    Kamoun, S.6
  • 54
    • 11144245139 scopus 로고    scopus 로고
    • Role of inhibitors of proteolytic enzymes in plant defense against phytopathogenic microorganisms
    • Valueva, T., and Mosolov, V. (2004). Role of inhibitors of proteolytic enzymes in plant defense against phytopathogenic microorganisms. Biochemistry 69, 1305-1309. doi: 10. 1007/s10541-005-0015-5.
    • (2004) Biochemistry , vol.69 , pp. 1305-1309
    • Valueva, T.1    Mosolov, V.2
  • 55
    • 33751578407 scopus 로고    scopus 로고
    • Cladosporium fulvum Avr4 protects fungal cell walls against hydrolysis by plant chitinases accumulating during infection
    • van den Burg, H. A., Harrison, S. J., Joosten, M. H. A. J., Vervoort, J., and de Wit, P. J. (2006). Cladosporium fulvum Avr4 protects fungal cell walls against hydrolysis by plant chitinases accumulating during infection. Mol. Plant Microbe Interact. 19, 1420-1430. doi: 10. 1094/MPMI-19-1420.
    • (2006) Mol. Plant Microbe Interact , vol.19 , pp. 1420-1430
    • van den Burg, H.A.1    Harrison, S.J.2    Joosten, M.H.A.J.3    Vervoort, J.4    de Wit, P.J.5
  • 56
    • 84891735700 scopus 로고    scopus 로고
    • Pseudogenization in pathogenic fungi with different host plants and lifestyles might reflect their evolutionary past
    • van der Burgt, A., Karimi Jashni, M., Bahkali, A. H., and de Wit, P. J. (2014). Pseudogenization in pathogenic fungi with different host plants and lifestyles might reflect their evolutionary past. Mol. Plant Pathol. 15, 133-144. doi: 10. 1111/mpp. 12072.
    • (2014) Mol. Plant Pathol , vol.15 , pp. 133-144
    • van der Burgt, A.1    Karimi Jashni, M.2    Bahkali, A.H.3    de Wit, P.J.4
  • 57
    • 44949258132 scopus 로고    scopus 로고
    • Plant proteases: From phenotypes to molecular mechanisms
    • van der Hoorn, R. A. L. (2008). Plant proteases: from phenotypes to molecular mechanisms. Annu. Rev. Plant Biol. 59, 191-223. doi: 10. 1146/annurev. arplant. 59. 032607. 092835.
    • (2008) Annu. Rev. Plant Biol , vol.59 , pp. 191-223
    • van der Hoorn, R.A.L.1
  • 59
    • 84860129593 scopus 로고    scopus 로고
    • A maize cystatin suppresses host immunity by inhibiting apoplastic cysteine proteases
    • van der Linde, K., Hemetsberger, C., Kastner, C., Kaschani, F., van der Hoorn, R. A. L., Kumlehn, J., et al. (2012b). A maize cystatin suppresses host immunity by inhibiting apoplastic cysteine proteases. Plant Cell 24, 1285-1300. doi: 10. 1105/tpc. 111. 093732.
    • (2012) Plant Cell , vol.24 , pp. 1285-1300
    • van der Linde, K.1    Hemetsberger, C.2    Kastner, C.3    Kaschani, F.4    van der Hoorn, R.A.L.5    Kumlehn, J.6
  • 60
    • 57749105343 scopus 로고    scopus 로고
    • The Cladosporium fulvum virulence protein Avr2 inhibits host proteases required for basal defense
    • van Esse, H. P., van't Klooster, J. W., Bolton, M. D., Yadeta, K. A., van Baarlen, P., Boeren, S., et al. (2008). The Cladosporium fulvum virulence protein Avr2 inhibits host proteases required for basal defense. Plant Cell 20, 1948-1963. doi: 10. 1105/tpc. 108. 059394.
    • (2008) Plant Cell , vol.20 , pp. 1948-1963
    • van Esse, H.P.1    van't Klooster, J.W.2    Bolton, M.D.3    Yadeta, K.A.4    van Baarlen, P.5    Boeren, S.6
  • 61
    • 0030087622 scopus 로고    scopus 로고
    • Differential induction of chitinase and 1, 3-β-glucanase gene expression in tomato by Cladosporium fulvum and its race-specific elicitors
    • Wubben, J. P., Lawrence, C. B., and de Wit, P. J. (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, 105-116. doi: 10. 1006/pmpp. 1996. 0010.
    • (1996) Physiol. Mol. Plant Pathol , vol.48 , pp. 105-116
    • Wubben, J.P.1    Lawrence, C.B.2    de Wit, P.J.3
  • 62
    • 0035941043 scopus 로고    scopus 로고
    • A Bowman-Birk-type trypsin-chymotrypsin inhibitor from broad beans
    • Ye, X. Y., Ng, T. B., and Rao, P. F. (2001). A Bowman-Birk-type trypsin-chymotrypsin inhibitor from broad beans. Biochem. Biophys. Res. Commun. 289, 91-96. doi: 10. 1006/bbrc. 2001. 5965.
    • (2001) Biochem. Biophys. Res. Commun , vol.289 , pp. 91-96
    • Ye, X.Y.1    Ng, T.B.2    Rao, P.F.3


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