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Volumn 223, Issue 3, 2006, Pages 392-406

Enhanced resistance to the rice blast fungus Magnaporthe grisea conferred by expression of a cecropin A gene in transgenic rice

Author keywords

Antifungal; Cecropin A; Oryza; Rice blast fungus; Transgenic rice

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; CECROPIN A; HYBRID PROTEIN;

EID: 33644644450     PISSN: 00320935     EISSN: 14322048     Source Type: Journal    
DOI: 10.1007/s00425-005-0069-z     Document Type: Article
Times cited : (108)

References (53)
  • 2
    • 0028843285 scopus 로고
    • Erwinia soft rot resistance of potato cultivars transformed with a gene construct coding for antimicrobial peptide cecropin B is not altered
    • Allefs S, Florack DEA, Hoogendoorn C, Stiekema WJ (1995) Erwinia soft rot resistance of potato cultivars transformed with a gene construct coding for antimicrobial peptide cecropin B is not altered. Am Potato J 72:437-445
    • (1995) Am Potato J , vol.72 , pp. 437-445
    • Allefs, S.1    Florack, D.E.A.2    Hoogendoorn, C.3    Stiekema, W.J.4
  • 3
    • 0009129319 scopus 로고    scopus 로고
    • The role of thionins in the resistance of plants
    • Datta SK, Muthudrishan S (eds) CRC Press, New York
    • Bohlmann H (1999) The role of thionins in the resistance of plants. In: Datta SK, Muthudrishan S (eds) Pathogenesis-related proteins in plants. CRC Press, New York, pp 207-234
    • (1999) Pathogenesis-related Proteins in Plants , pp. 207-234
    • Bohlmann, H.1
  • 4
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman HG (1995) Peptide antibiotics and their role in innate immunity. Annu Rev Immunol 13:61-92
    • (1995) Annu Rev Immunol , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quentification of microgram quantities utilizing the principle of protein-dye binding
    • Bradford M (1976) A rapid and sensitive method for the quentification of microgram quantities utilizing the principle of protein-dye binding. Ann Biochem 72:248-254
    • (1976) Ann Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 7
    • 0029347190 scopus 로고
    • Plant defensins: Novel antimicrobial peptides as components of the host defense system
    • Broekaert WF, Terras FRG, Commue BP, Osborn RW (1995) Plant defensins: novel antimicrobial peptides as components of the host defense system. Plant Physiol 108:1353-1358
    • (1995) Plant Physiol , vol.108 , pp. 1353-1358
    • Broekaert, W.F.1    Terras, F.R.G.2    Commue, B.P.3    Osborn, R.W.4
  • 9
    • 0032568512 scopus 로고    scopus 로고
    • Generation of broad-spectrum disease resistance by overexpression of an essential regulatory gene in systemic acquired resistance
    • USA
    • Cao H, Li X, Dong X (1998) Generation of broad-spectrum disease resistance by overexpression of an essential regulatory gene in systemic acquired resistance. Proc Natl Acad Sci USA 95:6532-6536
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 6532-6536
    • Cao, H.1    Li, X.2    Dong, X.3
  • 10
  • 11
    • 0032031617 scopus 로고    scopus 로고
    • Cecropin A-derived peptides are potent inhibitors of fungal plant pathogens
    • Cavallarin L, Andreu D, San Segundo B (1998) Cecropin A-derived peptides are potent inhibitors of fungal plant pathogens. Mol Plant-Microbe Interact 11:218-227
    • (1998) Mol Plant-Microbe Interact , vol.11 , pp. 218-227
    • Cavallarin, L.1    Andreu, D.2    San Segundo, B.3
  • 12
    • 0026816010 scopus 로고
    • Maize polyubiquitin genes: Structure, thermal perturbation of expression and transcript splicing, and promoter activity following transfer to protoplasts by electroporation
    • Christensen AH, Scharrock RA, Quail PJ (1992) Maize polyubiquitin genes: structure, thermal perturbation of expression and transcript splicing, and promoter activity following transfer to protoplasts by electroporation. Plant Mol Biol 18:675-689
    • (1992) Plant Mol Biol , vol.18 , pp. 675-689
    • Christensen, A.H.1    Scharrock, R.A.2    Quail, P.J.3
  • 13
    • 0030138945 scopus 로고    scopus 로고
    • Ubiquitin promoter based vectors for high level expression of selectable and/or screenable marker genes in monocotyledoneus plants
    • Christensen AH, Quail PH (1996) Ubiquitin promoter based vectors for high level expression of selectable and/or screenable marker genes in monocotyledoneus plants. Transgenic Res 5:216-218
    • (1996) Transgenic Res , vol.5 , pp. 216-218
    • Christensen, A.H.1    Quail, P.H.2
  • 14
    • 0024040498 scopus 로고
    • Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes
    • USA
    • Christensen B, Fink J, Merrifield RB, Mauzerall D (1988) Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc Natl Acad Sci USA 85:5072-5076
    • (1988) Proc Natl Acad Sci , vol.85 , pp. 5072-5076
    • Christensen, B.1    Fink, J.2    Merrifield, R.B.3    Mauzerall, D.4
  • 15
    • 3442876757 scopus 로고    scopus 로고
    • Transgenic rice plants expressing the antifungal AFP protein from Aspergillus giganteus show enhanced resistance to the rice blast fungus Magnaporthe grisea
    • Coca M, Bortolotti C, Rufat M, Peñas G, Eritja R, Tharreau D, Martinez del Pozo A, Messeguer J, San Segundo B (2004) Transgenic rice plants expressing the antifungal AFP protein from Aspergillus giganteus show enhanced resistance to the rice blast fungus Magnaporthe grisea. Plant Mol Biol 54:245-259
    • (2004) Plant Mol Biol , vol.54 , pp. 245-259
    • Coca, M.1    Bortolotti, C.2    Rufat, M.3    Peñas, G.4    Eritja, R.5    Tharreau, D.6    Martinez Del Pozo, A.7    Messeguer, J.8    San Segundo, B.9
  • 17
    • 0002203074 scopus 로고    scopus 로고
    • Expression and function of PR proteins in transgenic plants
    • Datta SK, Muthudrishan S (eds) CRC Press, New York
    • Datta S, Muthukrisnan S, Datta SK (1999) Expression and function of PR proteins in transgenic plants. In: Datta SK, Muthudrishan S (eds) Pathogenesis-related proteins in plants. CRC Press, New York, pp 261-277
    • (1999) Pathogenesis-related Proteins in Plants , pp. 261-277
    • Datta, S.1    Muthukrisnan, S.2    Datta, S.K.3
  • 19
    • 0028028546 scopus 로고
    • The expression of cecropin peptide in transgenic tobacco does not confer resistance to Pseudomonas syringae pv tabaci
    • Hightower R, Baden C, Penzes E, Dunsmuir P (1994) The expression of cecropin peptide in transgenic tobacco does not confer resistance to Pseudomonas syringae pv tabaci. Plant Cell Rep 13:295-299
    • (1994) Plant Cell Rep , vol.13 , pp. 295-299
    • Hightower, R.1    Baden, C.2    Penzes, E.3    Dunsmuir, P.4
  • 21
    • 0030904451 scopus 로고    scopus 로고
    • Expression of an engineered cecropin gene cassette in transgenic tobacco plants confers disease resistance to Pseudomonas syringae pv. tabaci
    • Huang Y, Nordeen RO, Di M, Owens LD, McBeath JH (1997) Expression of an engineered cecropin gene cassette in transgenic tobacco plants confers disease resistance to Pseudomonas syringae pv. tabaci. Phytopathology 87:494-499
    • (1997) Phytopathology , vol.87 , pp. 494-499
    • Huang, Y.1    Nordeen, R.O.2    Di, M.3    Owens, L.D.4    McBeath, J.H.5
  • 23
    • 0029328434 scopus 로고
    • Enhanced quantitative resistance against fungal disease by combinatorial expression of different barley antifungal proteins in transgenic tobacco
    • Jach G, Gornhardt B, Mundy J, Logemann J, Pinsdorf E, Leah R, Schell J, Maas C (1995) Enhanced quantitative resistance against fungal disease by combinatorial expression of different barley antifungal proteins in transgenic tobacco. Plant J 8:97-103
    • (1995) Plant J , vol.8 , pp. 97-103
    • Jach, G.1    Gornhardt, B.2    Mundy, J.3    Logemann, J.4    Pinsdorf, E.5    Leah, R.6    Schell, J.7    Maas, C.8
  • 25
    • 0002262243 scopus 로고
    • Expression of a cecropin B lytic peptide analog in transgenic tobacco confers enhanced resistance to bacterial wilt caused by Pseudomonas solanacearum
    • Jaynes JM, Nagpala P, Destéfano-Beltrán L, Huang J-H, Kim J, Denny T, Cetiner S (1993) Expression of a cecropin B lytic peptide analog in transgenic tobacco confers enhanced resistance to bacterial wilt caused by Pseudomonas solanacearum. Plant Sci 89:43-53
    • (1993) Plant Sci , vol.89 , pp. 43-53
    • Jaynes, J.M.1    Nagpala, P.2    Destéfano-Beltrán, L.3    Huang, J.-H.4    Kim, J.5    Denny, T.6    Cetiner, S.7
  • 26
    • 2442517494 scopus 로고    scopus 로고
    • Synonymous codon usage bias in Oryza sativa
    • Liu Q, Feng Y, Zhao X, Dong H, Xue Q (2004) Synonymous codon usage bias in Oryza sativa. Plant Sci 167:101-105
    • (2004) Plant Sci , vol.167 , pp. 101-105
    • Liu, Q.1    Feng, Y.2    Zhao, X.3    Dong, H.4    Xue, Q.5
  • 27
    • 0023654956 scopus 로고
    • Improved method for the isolation of RNA from plant tissues
    • Logeman J, Schell J, Willmitzer L (1987) Improved method for the isolation of RNA from plant tissues. Ann Biochem 163:16-20
    • (1987) Ann Biochem , vol.163 , pp. 16-20
    • Logeman, J.1    Schell, J.2    Willmitzer, L.3
  • 29
    • 0029140775 scopus 로고
    • Coordinated activation of programmed cell death and defense mechanisms in transgenic tobacco platns expressing a bacterial proton pump
    • Mittler R, Shulaev V, Lam E (1995) Coordinated activation of programmed cell death and defense mechanisms in transgenic tobacco platns expressing a bacterial proton pump. Plant Cell 7:29-42
    • (1995) Plant Cell , vol.7 , pp. 29-42
    • Mittler, R.1    Shulaev, V.2    Lam, E.3
  • 30
    • 0027142573 scopus 로고
    • Effect of cecropin B on peach pathogens, protoplasts, and cells
    • Mills D, Hammerschlag FA (1993) Effect of cecropin B on peach pathogens, protoplasts, and cells. Plant Sci 93:143-150
    • (1993) Plant Sci , vol.93 , pp. 143-150
    • Mills, D.1    Hammerschlag, F.A.2
  • 31
    • 0028322569 scopus 로고
    • Evidence for the breakdown of cecropin B by proteinases in the intercellular fluid of peach leaves
    • Mills D, Hammerschlag FA, Nordeen RO, Owens LD (1994) Evidence for the breakdown of cecropin B by proteinases in the intercellular fluid of peach leaves. Plant Sci 104:17-22
    • (1994) Plant Sci , vol.104 , pp. 17-22
    • Mills, D.1    Hammerschlag, F.A.2    Nordeen, R.O.3    Owens, L.D.4
  • 34
    • 0242308193 scopus 로고    scopus 로고
    • Activity of the antifungal protein from Aspergillus giganteus against Botrytis cinerea
    • Moreno AB, Martinez del Pozo A, Borja M, San Segundo B (2003) Activity of the antifungal protein from Aspergillus giganteus against Botrytis cinerea. Phytopathology 93:1344-1353
    • (2003) Phytopathology , vol.93 , pp. 1344-1353
    • Moreno, A.B.1    Martinez Del Pozo, A.2    Borja, M.3    San Segundo, B.4
  • 35
    • 0019321718 scopus 로고
    • Rapid isolation of high molecular weight plant DNA
    • Murray MG, Thompson WF (1980) Rapid isolation of high molecular weight plant DNA. Nucl Acid Res 8:4321-4325
    • (1980) Nucl Acid Res , vol.8 , pp. 4321-4325
    • Murray, M.G.1    Thompson, W.F.2
  • 36
    • 0001449028 scopus 로고
    • Activity of cecropin SB37 against protoplasts from several plant species and their bacterial pathogens
    • Nordeen RO, Sinden SL, Jaynes JM, Owens LD (1992) Activity of cecropin SB37 against protoplasts from several plant species and their bacterial pathogens. Plant Sci 82:101-107
    • (1992) Plant Sci , vol.82 , pp. 101-107
    • Nordeen, R.O.1    Sinden, S.L.2    Jaynes, J.M.3    Owens, L.D.4
  • 37
    • 0033763238 scopus 로고    scopus 로고
    • Transgenic plants expressing cationic peptide chimeras exhibit broad-spectrum resistance to phytopathogens
    • Osusky M, Zhou G, Osuska L, Hancock E, Kay WW, Misra S (2000) Transgenic plants expressing cationic peptide chimeras exhibit broad-spectrum resistance to phytopathogens. Nature Biotechnol 18:1162-1166
    • (2000) Nature Biotechnol , vol.18 , pp. 1162-1166
    • Osusky, M.1    Zhou, G.2    Osuska, L.3    Hancock, E.4    Kay, W.W.5    Misra, S.6
  • 38
    • 3242882725 scopus 로고    scopus 로고
    • Transgenic potatoes expressing a novel cationic peptide are resistant to late blight and pink rot
    • Osusky M, Osuska L, Hancock RE, Kay WW, Misra S (2004) Transgenic potatoes expressing a novel cationic peptide are resistant to late blight and pink rot. Transgenic Res 13:181-190
    • (2004) Transgenic Res , vol.13 , pp. 181-190
    • Osusky, M.1    Osuska, L.2    Hancock, R.E.3    Kay, W.W.4    Misra, S.5
  • 39
    • 0004080812 scopus 로고
    • Commonwealth Mycological Institute, Kew, England
    • Ou SH (1985) Rice Diseases, second edition, Commonwealth Mycological Institute, Kew, England
    • (1985) Rice Diseases, Second Edition
    • Ou, S.H.1
  • 40
    • 0031149057 scopus 로고    scopus 로고
    • A single amino acid substitution in the antimicrobial defense protein cecropin B is associated with diminished degradation by leaf intercellular fluid
    • Owens LD, Heutte TM (1997) A single amino acid substitution in the antimicrobial defense protein cecropin B is associated with diminished degradation by leaf intercellular fluid. Mol Plant-Microbe Interact 10:525-528
    • (1997) Mol Plant-Microbe Interact , vol.10 , pp. 525-528
    • Owens, L.D.1    Heutte, T.M.2
  • 41
    • 0343953583 scopus 로고    scopus 로고
    • Regeneration and genetic transformation of Spanish rice cultivars using mature embryos
    • Pons MJ, Marfà V, Melé E, Messeguer J (2000) Regeneration and genetic transformation of Spanish rice cultivars using mature embryos. Euphytica 114:117-122
    • (2000) Euphytica , vol.114 , pp. 117-122
    • Pons, M.J.1    Marfà, V.2    Melé, E.3    Messeguer, J.4
  • 42
    • 0027050148 scopus 로고
    • Recursive PCR: A novel technique for total gene synthesis
    • Prodromou Ch, Pearl LH (1992) Recursive PCR: a novel technique for total gene synthesis. Protein Eng 5:827-829
    • (1992) Protein Eng , vol.5 , pp. 827-829
    • Prodromou, Ch.1    Pearl, L.H.2
  • 44
    • 0031239636 scopus 로고    scopus 로고
    • Interleukin 2 promoter/enhancer controlled expression of a synthetic cecropin-class lytic peptide in transgenic mice and subsequent resistance to Brucella abortus
    • Reed WA, Elzer PH, Enright FM, Jaynes JM, Morrey JD, White KL (1997) Interleukin 2 promoter/enhancer controlled expression of a synthetic cecropin-class lytic peptide in transgenic mice and subsequent resistance to Brucella abortus. Transgenic Res 6:337-347
    • (1997) Transgenic Res , vol.6 , pp. 337-347
    • Reed, W.A.1    Elzer, P.H.2    Enright, F.M.3    Jaynes, J.M.4    Morrey, J.D.5    White, K.L.6
  • 45
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Ann Biochem 166:368-379
    • (1987) Ann Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 46
    • 0034721744 scopus 로고    scopus 로고
    • Transgenic expression of cecropin B, an antibacterial peptide from Bombyx mori, confers enhanced resistance to bacterial leaf blight in rice
    • Sharma A, Sharma R, Imamura M, Yamakawa M, Machii H (2000) Transgenic expression of cecropin B, an antibacterial peptide from Bombyx mori, confers enhanced resistance to bacterial leaf blight in rice. FEBS Lett 484:7-11
    • (2000) FEBS Lett , vol.484 , pp. 7-11
    • Sharma, A.1    Sharma, R.2    Imamura, M.3    Yamakawa, M.4    Machii, H.5
  • 47
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and desestabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai Y (1999) Mechanism of the binding, insertion and desestabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochem Biophys Acta 1462:55-70
    • (1999) Biochem Biophys Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 48
    • 0033863799 scopus 로고    scopus 로고
    • Membrane-induced folding of cecropin A
    • Silvestro L, Axelsen PH (2000) Membrane-induced folding of cecropin A. Biophys J 79:1465-1477
    • (2000) Biophys J , vol.79 , pp. 1465-1477
    • Silvestro, L.1    Axelsen, P.H.2
  • 49
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner H, Hultmark D, Engström A, Bennich H, Boman HG (1981) Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292:246-248
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engström, A.3    Bennich, H.4    Boman, H.G.5
  • 50
    • 0023864293 scopus 로고
    • Binding and action of cecropin and cecropin analogs: Antibacterial peptides from insects
    • Steiner H, Andreu D, Merrifield RB (1988) Binding and action of cecropin and cecropin analogs: antibacterial peptides from insects. Biochim Biophys Acta 939:260-266
    • (1988) Biochim Biophys Acta , vol.939 , pp. 260-266
    • Steiner, H.1    Andreu, D.2    Merrifield, R.B.3
  • 52
    • 0028001451 scopus 로고
    • Enhanced protection against fungal attack by constitutive co-expression of chitinase and glucanase genes in transgenic tobacco
    • Zhu Q, Maher EA, Masoud S, Dixon RA, Lamb CJ (1994) Enhanced protection against fungal attack by constitutive co-expression of chitinase and glucanase genes in transgenic tobacco. Bio/Technology 12:807-812
    • (1994) Bio/Technology , vol.12 , pp. 807-812
    • Zhu, Q.1    Maher, E.A.2    Masoud, S.3    Dixon, R.A.4    Lamb, C.J.5
  • 53
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M (2002) Antimicrobial peptides of multicellular organisms. Nature 415:389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1


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