메뉴 건너뛰기




Volumn 9, Issue 10, 2014, Pages

New insights into the structure and mode of action of Mo-CBP3, an antifungal chitin-binding protein of Moringa oleifera seeds

Author keywords

[No Author keywords available]

Indexed keywords

ANTIFUNGAL AGENT; BINDING PROTEIN; CHITIN; FUNGICIDE; MO CBP3 PROTEIN; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; PROTEIN BINDING; VEGETABLE PROTEIN;

EID: 84908614550     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0111427     Document Type: Article
Times cited : (47)

References (42)
  • 1
    • 84875035025 scopus 로고    scopus 로고
    • Some 2S albumin from peanut seeds exhibits inhibitory activity against aspergillus flavus
    • Duan XH, Jiang R, Wen Y.J., Bin JH (2013) Some 2S albumin from peanut seeds exhibits inhibitory activity against Aspergillus flavus. Plant Physiol Biochem 66: 84-90.
    • (2013) Plant Physiol Biochem , vol.66 , pp. 84-90
    • Duan, X.H.1    Jiang, R.2    Wen, Y.J.3    Bin, J.H.4
  • 2
    • 79952258944 scopus 로고    scopus 로고
    • Purification, biochemical characterization and antifungal activity of a new lipid transfer protein (LTP) from coffea canephora seeds with alfa-amylase inhibitor properties
    • Zottich U, Da Cunha M, Carvalho AO, Dias G.B., Silva NC, et al. (2011) Purification, biochemical characterization and antifungal activity of a new lipid transfer protein (LTP) from Coffea canephora seeds with alfa-amylase inhibitor properties. Biochim Biophys Acta 1810: 375-383.
    • (2011) Biochim Biophys Acta , vol.1810 , pp. 375-383
    • Zottich, U.1    Da Cunha, M.2    Carvalho, A.O.3    Dias, G.B.4    Silva, N.C.5
  • 4
    • 84877656207 scopus 로고    scopus 로고
    • Transcriptomic changes following the compatible interaction vitis vinifera-erysiphe necator. Paving the way towards an enantioselective role in plant defence modulation
    • Borges AF, Ferreira RB, Monteiro S (2013) Transcriptomic changes following the compatible interaction Vitis vinifera-Erysiphe necator. Paving the way towards an enantioselective role in plant defence modulation. Plant Physiol Biochem 68: 71-80.
    • (2013) Plant Physiol Biochem , vol.68 , pp. 71-80
    • Borges, A.F.1    Ferreira, R.B.2    Monteiro, S.3
  • 5
    • 84863914438 scopus 로고    scopus 로고
    • A defensin-like peptide from phaseolus vulgaris cv. 'King pole bean'
    • Wong JH, Ip DCW, Ng TB, Chan Y.S., Fang F., et al. (2012) A defensin-like peptide from Phaseolus vulgaris cv. 'King Pole Bean'. Food Chem 135: 408-414.
    • (2012) Food Chem , vol.135 , pp. 408-414
    • Wong, J.H.1    Ip, D.C.W.2    Ng, T.B.3    Chan, Y.S.4    Fang, F.5
  • 6
    • 78049265483 scopus 로고    scopus 로고
    • Soybean toxin (SBTX), a protein from soybeans that inhibits the life cycle of plant and human pathogenic fungi
    • Morais JKS, Gomes VM, Oliveira JTA, Santos IS, Da Cunha M, et al. (2010) Soybean toxin (SBTX), a protein from soybeans that inhibits the life cycle of plant and human pathogenic fungi. J Agric Food Chem 58: 10356-10363.
    • (2010) J Agric Food Chem , vol.58 , pp. 10356-10363
    • Morais, J.K.S.1    Gomes, V.M.2    Oliveira, J.T.A.3    Santos, I.S.4    Da Cunha, M.5
  • 7
    • 84859917391 scopus 로고    scopus 로고
    • Antifungal property of dihydrodehydrodiconiferyl alcohol 99-O-b-d-glucoside and its pore-forming action in plasma membrane of candida albicans
    • Choi H, Cho J, Jin Q., Woo ER, Lee DG (2012) Antifungal property of dihydrodehydrodiconiferyl alcohol 99-O-b-d-glucoside and its pore-forming action in plasma membrane of Candida albicans. Biochim Biophys Acta 1818: 1648-1655.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1648-1655
    • Choi, H.1    Cho, J.2    Jin, Q.3    Woo, E.R.4    Lee, D.G.5
  • 8
    • 47549098966 scopus 로고    scopus 로고
    • Transgenic indica rice expressing mirabilis jalapa antimicrobial protein (Mj-AMP2) shows enhanced resistance to the rice blast fungus magnaporthe oryzae
    • Deo Prasad B, Jha S, Chattoo BB (2008) Transgenic indica rice expressing Mirabilis jalapa antimicrobial protein (Mj-AMP2) shows enhanced resistance to the rice blast fungus Magnaporthe oryzae. Plant Sci 175: 364-371.
    • (2008) Plant Sci , vol.175 , pp. 364-371
    • Deo Prasad, B.1    Jha, S.2    Chattoo, B.B.3
  • 9
    • 33644836650 scopus 로고    scopus 로고
    • Structural characterization of novel chitin-binding lectins from the genus artocarpus and their antifungal activity
    • Trindade MB, Lopes JLS, Soares-Costa A, Monteiro-Moreira AC, Moreira R.A., et al. (2006) Structural characterization of novel chitin-binding lectins from the genus Artocarpus and their antifungal activity. Biochim Biophys Acta 1764: 146-152.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 146-152
    • Trindade, M.B.1    Lopes, J.L.S.2    Soares-Costa, A.3    Monteiro-Moreira, A.C.4    Moreira, R.A.5
  • 10
    • 33344467122 scopus 로고    scopus 로고
    • A two component chitin-binding protein from french bean - Association of a proline-rich protein with a cysteine-rich polypeptide
    • Bindschedler LV, Whitelegge JP, Millar D.J., Bowell GP (2006) A two component chitin-binding protein from French bean - Association of a proline-rich protein with a cysteine-rich polypeptide. FEBS Lett 580: 1541-1546.
    • (2006) FEBS Lett , vol.580 , pp. 1541-1546
    • Bindschedler, L.V.1    Whitelegge, J.P.2    Millar, D.J.3    Bowell, G.P.4
  • 11
    • 0032763530 scopus 로고    scopus 로고
    • Characterization of a novel, antifungal, chitin-binding protein from streptomyces tendae tü901 that interferes with growth polarity
    • Bormann C, Baier D, Hörr I, Raps C., Berger J, et al. (1999) Characterization of a novel, antifungal, chitin-binding protein from Streptomyces tendae Tü901 that interferes with growth polarity. J Bacteriol 181: 7421-7429.
    • (1999) J Bacteriol , vol.181 , pp. 7421-7429
    • Bormann, C.1    Baier, D.2    Hörr, I.3    Raps, C.4    Berger, J.5
  • 12
    • 77955049649 scopus 로고    scopus 로고
    • A new chitin-binding lectin from rhizome of setcreasea purpurea with antifungal, antiviral and apoptosis-inducing activities
    • Yao Q, Wu CF, Luo P, Xiang X.C., Liu JJ, et al. (2010) A new chitin-binding lectin from rhizome of Setcreasea purpurea with antifungal, antiviral and apoptosis-inducing activities. Proc Biochem 45: 1477-1485.
    • (2010) Proc Biochem , vol.45 , pp. 1477-1485
    • Yao, Q.1    Wu, C.F.2    Luo, P.3    Xiang, X.C.4    Liu, J.J.5
  • 13
    • 84872027638 scopus 로고    scopus 로고
    • A novel chitin-binding protein from moringa oleifera seed with potential for plant disease control
    • Gifoni JM, Oliveira JTA, Oliveira HD, Batista A.B., Pereira ML, et al. (2012) A novel chitin-binding protein from Moringa oleifera seed with potential for plant disease control. Biopolymers 98: 406-415.
    • (2012) Biopolymers , vol.98 , pp. 406-415
    • Gifoni, J.M.1    Oliveira, J.T.A.2    Oliveira, H.D.3    Batista, A.B.4    Pereira, M.L.5
  • 14
    • 0000203898 scopus 로고
    • Cleavage of structural proteins during the assembly of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of bacteriophage T4. Nature 277: 685-689.
    • (1970) Nature , vol.277 , pp. 685-689
    • Laemmli, U.K.1
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set
    • Sreerama N, Woody RW (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set. Anal Biochem 287: 252-260.
    • (2000) Anal Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 17
    • 0030265181 scopus 로고    scopus 로고
    • Antifungal activity of cucumber b-1,3-glucanase and chitinase
    • Ji C, Kuc J (1996) Antifungal activity of cucumber b-1,3-glucanase and chitinase. J Physiol Mol Plant Pathol 49: 257-265.
    • (1996) J Physiol Mol Plant Pathol , vol.49 , pp. 257-265
    • Ji, C.1    Kuc, J.2
  • 19
    • 0030748530 scopus 로고    scopus 로고
    • 2 accumulation in papillae and hypersensitive response during the barley-powdery mildew interaction
    • 2 accumulation in papillae and hypersensitive response during the barley-powdery mildew interaction. Plant J 11: 1187-1194.
    • (1997) Plant J , vol.11 , pp. 1187-1194
    • Thordal-Christensen, H.1    Zhang, Z.2    Wei, Y.3    Collinge, D.B.4
  • 20
    • 33746067918 scopus 로고    scopus 로고
    • Antimicrobial activity of potato aspartic proteases (StAPs) involves membrane permeabilization
    • Mendieta JR, Pagano MR, Muñoz FF, Daleo G.R., Guevara MG (2006) Antimicrobial activity of potato aspartic proteases (StAPs) involves membrane permeabilization. Microbiology 152: 2039-2047.
    • (2006) Microbiology , vol.152 , pp. 2039-2047
    • Mendieta, J.R.1    Pagano, M.R.2    Muñoz, F.F.3    Daleo, G.R.4    Guevara, M.G.5
  • 21
    • 0027160539 scopus 로고
    • A rapid and sensitive hemolysis neutralization assay for palytoxin
    • Bignami GS (1993) A rapid and sensitive hemolysis neutralization assay for palytoxin. Toxicon 31: 817-820.
    • (1993) Toxicon , vol.31 , pp. 817-820
    • Bignami, G.S.1
  • 22
    • 67651241140 scopus 로고    scopus 로고
    • Circular dichroism techniques: Biomolecular and nanostructural analyses
    • Ranjbar B, Gill P (2009) Circular dichroism techniques: biomolecular and nanostructural analyses. Chem Biol Drug Des 74: 101-120.
    • (2009) Chem Biol Drug Des , vol.74 , pp. 101-120
    • Ranjbar, B.1    Gill, P.2
  • 23
    • 0027969049 scopus 로고
    • Structural features of plant chitinases and chitin-binding proteins
    • Beintema JJ (1994) Structural features of plant chitinases and chitin-binding proteins. FEBS Lett 350: 159-163.
    • (1994) FEBS Lett , vol.350 , pp. 159-163
    • Beintema, J.J.1
  • 24
    • 0343602841 scopus 로고    scopus 로고
    • Structural basis for chitin recognition by defense proteins: Glcnac residues are bound in a multivalent fashion by extended binding sites in hevein domains
    • Asensio JL, Cañada FJ, Siebert H.C., Laynez J., Poveda A, et al. (2000) Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains. Chem Biol 7: 529-543.
    • (2000) Chem Biol , vol.7 , pp. 529-543
    • Asensio, J.L.1    Cañada, F.J.2    Siebert, H.C.3    Laynez, J.4    Poveda, A.5
  • 26
    • 0026734641 scopus 로고
    • Antimicrobial peptides from amaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins
    • Broekaert WF, Marien W, Terras FRG, De Bolle MFC, Proost P, et al. (1992) Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins. Biochemistry 31: 4308-4314.
    • (1992) Biochemistry , vol.31 , pp. 4308-4314
    • Broekaert, W.F.1    Marien, W.2    Terras, F.R.G.3    De Bolle, M.F.C.4    Proost, P.5
  • 27
    • 77955049649 scopus 로고    scopus 로고
    • A new chitin-binding lectin from rhizome of setcreasea purpurea with antifungal, antiviral and apoptosis-inducing activities
    • Yao Q, Wu C, Luo P., Xiang X, Liu J, et al. (2010) A new chitin-binding lectin from rhizome of Setcreasea purpurea with antifungal, antiviral and apoptosis-inducing activities. Proc Biochem 45: 1477-1485.
    • (2010) Proc Biochem , vol.45 , pp. 1477-1485
    • Yao, Q.1    Wu, C.2    Luo, P.3    Xiang, X.4    Liu, J.5
  • 28
    • 84978598116 scopus 로고
    • On the mechanism of Yeast flocculation
    • Lindquist W (1953) On the mechanism of yeast flocculation. J Inst Brew 59: 59-61.
    • (1953) J Inst Brew , vol.59 , pp. 59-61
    • Lindquist, W.1
  • 30
    • 0037310294 scopus 로고    scopus 로고
    • The antifungal protein from aspergillus giganteus causes membrane permeabilization
    • Theis T, Wedde M, Meyer V., Stahl U (2003) The antifungal protein from Aspergillus giganteus causes membrane permeabilization. Antimicrob Agents Chemoter 47: 588-593.
    • (2003) Antimicrob Agents Chemoter , vol.47 , pp. 588-593
    • Theis, T.1    Wedde, M.2    Meyer, V.3    Stahl, U.4
  • 31
    • 84861309985 scopus 로고    scopus 로고
    • Plant defensins and defensin-like peptides - Biological activities and biotechnological applications
    • Carvalho AO, Gomes VM (2011) Plant defensins and defensin-like peptides - biological activities and biotechnological applications. Curr Pharm Des 17: 4270-4293.
    • (2011) Curr Pharm Des , vol.17 , pp. 4270-4293
    • Carvalho, A.O.1    Gomes, V.M.2
  • 32
    • 49649131306 scopus 로고
    • Comparative phospholipid compositions of adult female xyleborus ferrugineus and its mutualistic fungal ectosymbionts
    • Koka LT, Norris DM (1972) Comparative phospholipid compositions of adult female Xyleborus ferrugineus and its mutualistic fungal ectosymbionts. Comp Biochem Physiol B 42: 245-254.
    • (1972) Comp Biochem Physiol B , vol.42 , pp. 245-254
    • Koka, L.T.1    Norris, D.M.2
  • 33
    • 79954421385 scopus 로고    scopus 로고
    • Antifungal activity of PvD1 defensin involves plasma membrane permeabilization, inhibition of medium acidification, and induction of ROS in fungi cells
    • Mello EO, Ribeiro SFF, Carvalho AO, Santos I.S., Da Cunha M, et al. (2011) Antifungal activity of PvD1 defensin involves plasma membrane permeabilization, inhibition of medium acidification, and induction of ROS in fungi cells. Curr Microbiol 62: 1209-1217.
    • (2011) Curr Microbiol , vol.62 , pp. 1209-1217
    • Mello, E.O.1    Ribeiro, S.F.F.2    Carvalho, A.O.3    Santos, I.S.4    Da Cunha, M.5
  • 34
    • 34548511597 scopus 로고    scopus 로고
    • The antifungal activity of rs-AFP2, a plant defensin from raphanus sativus, involves the induction of reactive oxygen species in candida albicans
    • Aerts AM, François IEJA, Meert EMK, Li QT, Cammue BPA, et al. (2007) The antifungal activity of Rs-AFP2, a plant defensin from Raphanus sativus, involves the induction of reactive oxygen species in Candida albicans. J Mol Microbiol Biotechnol 13: 243-247.
    • (2007) J Mol Microbiol Biotechnol , vol.13 , pp. 243-247
    • Aerts, A.M.1    François, I.E.J.A.2    Meert, E.M.K.3    Li, Q.T.4    Cammue, B.P.A.5
  • 35
    • 35648946853 scopus 로고    scopus 로고
    • Reactive oxygen species in regulation of fungal development
    • Gessler NN, Aver'yanov AA, Belozerskaya TA (2007) Reactive oxygen species in regulation of fungal development. Biochemistry 72: 1091-1109.
    • (2007) Biochemistry , vol.72 , pp. 1091-1109
    • Gessler, N.N.1    Aver'yanov, A.A.2    Belozerskaya, T.A.3
  • 36
    • 33746636871 scopus 로고    scopus 로고
    • The antifungal properties of a 2S albumin-homologous protein from passion fruit seeds involve plasma membrane permeabilization and ultrastructural alterations in Yeast cells
    • Agizzio AP, Da Cunha M, Carvalho AO, Oliveira M.A., Ribeiro SFF, et al. (2006) The antifungal properties of a 2S albumin-homologous protein from passion fruit seeds involve plasma membrane permeabilization and ultrastructural alterations in yeast cells. Plant Sci 171: 515-522.
    • (2006) Plant Sci , vol.171 , pp. 515-522
    • Agizzio, A.P.1    Da Cunha, M.2    Carvalho, A.O.3    Oliveira, M.A.4    Ribeiro, S.F.F.5
  • 38
    • 0034764911 scopus 로고    scopus 로고
    • A plant defense response effector induces microbial apoptosis
    • Narasimham ML, Damsz B, Coca M.A., Ibeas JI, Yun DJ, et al. (2001) A plant defense response effector induces microbial apoptosis. Mol Cell 8: 921-930.
    • (2001) Mol Cell , vol.8 , pp. 921-930
    • Narasimham, M.L.1    Damsz, B.2    Coca, M.A.3    Ibeas, J.I.4    Yun, D.J.5
  • 39
    • 77957843604 scopus 로고    scopus 로고
    • Lipopeptide induces apoptosis in fungal cells by a mitochondria-dependent pathway
    • Qi G, Zhu F, Du P., Yang X, Qiu D, et al. (2010) Lipopeptide induces apoptosis in fungal cells by a mitochondria-dependent pathway. Peptides 31: 1978-1986.
    • (2010) Peptides , vol.31 , pp. 1978-1986
    • Qi, G.1    Zhu, F.2    Du, P.3    Yang, X.4    Qiu, D.5
  • 40
    • 0030908830 scopus 로고    scopus 로고
    • Fluorescent probes for wall porosity and membrane integrity in filamentous fungi
    • Brul S, Nussbaum J, Dielbandhoesing SK (1997) Fluorescent probes for wall porosity and membrane integrity in filamentous fungi. J Microbiol Methods 28: 169-178.
    • (1997) J Microbiol Methods , vol.28 , pp. 169-178
    • Brul, S.1    Nussbaum, J.2    Dielbandhoesing, S.K.3
  • 41
    • 84871600294 scopus 로고    scopus 로고
    • In vitro antimicrobial, antioxidant, cytotoxicity and GC-MS analysis of mazus good-enifolius
    • Riaz M, Rasool N, Bukhari I.H., Shahid M., Zubair M, et al. (2012) In vitro antimicrobial, antioxidant, cytotoxicity and GC-MS analysis of Mazus good-enifolius. Molecules 17: 14275-14287.
    • (2012) Molecules , vol.17 , pp. 14275-14287
    • Riaz, M.1    Rasool, N.2    Bukhari, I.H.3    Shahid, M.4    Zubair, M.5
  • 42
    • 84860116439 scopus 로고    scopus 로고
    • Isolation and purification of a novel deca-antifungal peptide from potato (Solanum tuberosum L cv. Jopung) against candida albicans
    • Lee J-K, Gopal R., Seo CH, Cheong H, Park Y (2012) Isolation and purification of a novel deca-antifungal peptide from potato (Solanum tuberosum L cv. Jopung) against Candida albicans. Int J Mol Sci 13: 4021-4032.
    • (2012) Int J Mol Sci , vol.13 , pp. 4021-4032
    • Lee, J.-K.1    Gopal, R.2    Seo, C.H.3    Cheong, H.4    Park, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.