Plant Antimicrobial Peptides

  • Tatyana Odintsova
  • Tsezi Egorov
Part of the Signaling and Communication in Plants book series (SIGCOMM, volume 16)


Antimicrobial peptides (AMPs) are natural antibiotics produced by all living organisms to resist infection by pathogens. They are important effector molecules of the innate immune system both in animals and plants. AMPs are diverse in structure and mode of action and display broad-spectrum antimicrobial activity and thus show promise for engineering pathogen resistance in crops and development of novel pharmaceuticals. A variety of AMP classes have been discriminated, which include defensins, thionins, lipid-transfer proteins, hevein- and knottin-like peptides, and macrocyclic peptides. In this review, the role of AMPs in the plant immune system is briefly discussed, and different families of plant AMPs with respect to their structural peculiarities and biological role are considered. Special emphasis is given to AMPs of wild plants. Defensins belong to the largest AMP family widely distributed throughout the plant and animal kingdoms with a wide range of in vitro biological activities. Current evidence indicates that they interact with specific molecules on the fungal membranes and act on intracellular targets. Thionins show high inhibitory activity against diverse fungi and bacteria including human pathogens and are toxic to some other types of cells, such as mammalian, insect, and plant cells. The antimicrobial effect of thionins is associated with membrane permeabilization through pore formation. Lipid-transfer proteins are not only antimicrobial agents but are also involved in signaling. Hevein-like AMPs comprise peptides with a conserved chitin-binding domain, a variable number of disulfide bridges, and divergent precursor structures. Knottin-like and macrocyclic AMPs form the cystine knot and exhibit insecticidal, antimicrobial, anti-HIV, hemolytic, and uterotonic activities. Due to exclusive structural and chemical stability, plant cyclotides are regarded as templates into which diverse biological activities may be introduced.


Antifungal Activity Plant Defensin Defensin Gene Eucommia Ulmoides Polyploid Wheat Species 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


  1. Aerts AM, Francois IE, Meert EMK, Li QT, Cammue BPA, Thevissen K (2007) The antifungal activity of RsAFP2, a plant defensin from Raphanus sativus, involves the induction of reactive oxygen species in Candida albicans. J Mol Microbiol Biotechnol 13:243–247PubMedGoogle Scholar
  2. Aerts AM, Francois IEJA, Cammue BPA, Thevissen K (2008) The mode of antifungal action of plant, insect and human defensins. Cell Mol Life Sci 65:2069–2079PubMedGoogle Scholar
  3. Ajesh K, Sreejith K (2009) Peptide antibiotics: an alternative and antimicrobial strategy to circumvent fungal infections. Peptides 30:999–1006PubMedGoogle Scholar
  4. Allan A, Snyder AK, Preuss M, Nielsen EE, Shah DM, Smith TJ (2008) Plant defensins and virally encoded fungal toxin KP4 inhibit plant root growth. Planta 227:331–339Google Scholar
  5. Anaya-Lopez JL, Lopez-Meza JE, Baizabal-Aguirre VM, Cano-Camacho H, Ochoa-Zarzosa A (2006) Fungicidal and cytotoxic activity of Capsicum chinense defensin expressed by endothelial cells. Biotechnol Lett 28:1101–1108PubMedGoogle Scholar
  6. Beintema JJ (1994) Structural features of plant chitinases and chitin-binding proteins. FEBS Lett 350:159–163PubMedGoogle Scholar
  7. Benko-Iseppon AM, Galdino SL, Calsa T Jr, Kido EA, Tossi A, Belarmino LC, Crovella S (2010) Overview on plant antimicrobial peptides. Curr Protein Pept Sci 11:181–188PubMedGoogle Scholar
  8. Bloch CJ, Richardson M (1991) A new family of small (5 kDa) protein inhibitors of insect α-amylases from seeds of sorghum (Sorghum bicolor (L.) Moebch.) have sequence homologies with wheat γ-purothionins. FEBS J 279:101–104Google Scholar
  9. Broekaert WF, Mariën W, Terras FRG, De Bolle MFC, Proost P, Van Damme J, Dillen L, Claeys M, Rees SB, Vanderleyden J, Cammue BPA (1992) Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine-glycine-rich domain of chitin-binding proteins. Biochemistry 31:4308–4314PubMedGoogle Scholar
  10. Broekaert WF, Terras FRG, Cammue BPA, Osborn RW (1995) Plant defensins: novel antimicrobial peptides as components of the host defense system. Plant Physiol 108:1353–1358PubMedGoogle Scholar
  11. Broekaert WF, Cammue BPA, De Bolle MFC, Thevissen K, De Samblanx GW, Osborn RW (1997) Antimicrobial peptides from plants. Crit Rev Plant Sci 16:297–323Google Scholar
  12. Broekaert WF, Terras FRG, Cammue BPA (2000) Induced and preformed antimicrobial proteins. In: Slusarenko AJ, Fraser RSS, van Loon LC (eds) Mechanisms of resistance to plant diseases. Kluwer, The Netherlands, pp 371–479Google Scholar
  13. Cammue BPA, De Bolle MFC, Terras FRG, Proost P, Van Damme J, Rees SB, Vanderleyden J, Broekaert WF (1992) Isolation and characterization of a novel class of plant antimicrobial peptides from Mirabilis jalapa L. seeds. J Biol Chem 267:2228–2233PubMedGoogle Scholar
  14. Carmona MJ, Molina A, Fernandez JA, Lopez-Fando JJ, Garcia-Olmedo F (1993) Expression of the α-thionin gene from barley in tobacco confers enhanced resistance to bacterial pathogens. Plant J 3:457–462PubMedGoogle Scholar
  15. Carvalho AO, Gomes VM (2007) Role of plant lipid transfer proteins in plant cell physiology–A concise review. Peptides 28:1144–1153Google Scholar
  16. Carvalho AO, Gomes VM (2009) Plant defensins–prospects for the biological functions and biotechnological properties. Peptides 30:1007–1020Google Scholar
  17. Castro MS, Fontes W (2005) Plant defense and antimicrobial peptides. Protein Pept Lett 12:13–18PubMedGoogle Scholar
  18. Chagolla-Lopez A, Blanco-Labra A, Patthy A, Sanchez R, Pongor S (1994) A novel α-amylase inhibitor from amaranth (Amaranthus hypochondriacus) seeds. J Biol Chem 269:23475–23680Google Scholar
  19. Colilla FJ, Rocher A, Mendez E (1990) Gamma-purothionins: amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm. FEBS Lett 270:191–194PubMedGoogle Scholar
  20. Craik DJ (2001) Plant cyclotides: circular, knotted peptide toxins. Toxicon 39:1809–1813PubMedGoogle Scholar
  21. Craik DJ, Clark RJ, Daly NL (2007) Potential therapeutic applications of the cyclotides and related cystine knot mini-proteins. Expert Opin Investig Drugs 16:595–604PubMedGoogle Scholar
  22. da Rocha Pitta MG, da Rocha Pitta MG, Galdino SL (2010) Development of novel therapeutic drugs in humans from plant antimicrobial peptides. Curr Protein Pept Sci 11:236–247PubMedGoogle Scholar
  23. Dangl JL, Jones JDG (2001) Plant pathogens and integrated defence responses to infection. Nature 411:826–833PubMedGoogle Scholar
  24. De Samblanx GW, Goderis IJ, Thevissen K, Raemaekers R, Fant F, Borremans F, Acland DP, Osborn RW, Patel S, Broekaert WF (1997) Mutational analysis of a plant defensin from radish (Raphanus sativus L.) reveals two adjacent sites important for antifungal activity. J Biol Chem 272:1171–1179PubMedGoogle Scholar
  25. de Zélicourt A, Letousey P, Thoiron S, Campion C, Simoneau P, Elmorjani K, Marion D, Simier P, Delavault P (2007) Ha-DEF1, a sunflower defensin, induces cell death in Orobanche parasitic plants. Planta 226:591–600PubMedGoogle Scholar
  26. Diz MSS, Carvalho AO, Rodrigues R, Neves-Ferreira AGC, Da Cunha M, Alves EW, Okorokova-Façanha AL, Oliveira MA, Perales J, Machado OL, Gomes VM (2006) Antimicrobial peptides from chilli pepper seeds causes yeast plasma membrane permeabilization and inhibits the acidification of the medium by yeasts. Biochim Biophys Acta 1760:1323–1332PubMedGoogle Scholar
  27. Egorov TA, Odintsova TI, Pukhalsky VA, Grishin EV (2005) Diversity of wheat antimicrobial peptides. Peptides 26:2064–2073PubMedGoogle Scholar
  28. Farrokhi N, Whitelegge JP, Brusslan JA (2008) Plant peptides and peptidomics. Plant Biotechnol J 6:105–134PubMedGoogle Scholar
  29. Garcia-Olmedo F, Molina A, Alamillo JM, Rodriguez-Palenzuela P (1998) Plant defense peptides. Biopolymers (Pept Sci) 47:479–491Google Scholar
  30. Garcia-Olmedo F, Rodriguez-Palenzuela P, Molina A, Alamillo JM, Lopez-Solanilla E, Berrocal-Lobo M, Poza-Carrion C (2001) Antibiotic activities of peptides, hydrogen peroxide and peroxynitrite in plant defence. FEBS Lett 498:219–222PubMedGoogle Scholar
  31. Hammani R, Hamida JB, Vergoten G, Fliss I (2009) PhytAMP: a database dedicated to antimicrobial plant peptides. Nucl Acids Res 963(Database Issue):8–15Google Scholar
  32. Hancock REW, Sahl H-G (2006) Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat Biotechnol 24:1551–1557PubMedGoogle Scholar
  33. Huang R-H, Xiang Y, Liu X-Z, Zhang Y, Hu Z, Wang D-C (2002) Two novel antifungal peptides distinct with a five-disulfide motif from the bark of Eucommia ulmoides Oliv. FEBS Lett 521:87–90PubMedGoogle Scholar
  34. Huang R-H, Xiang Y, Tu G-Z, Zhang Y, Wang D-C (2004) Solution structure of Eucommia antifungal peptide: a novel structural model distinct with a five-disulfide motif. Biochemistry 43:6005–6012PubMedGoogle Scholar
  35. Iwai T, Kaku H, Honkura R, Nakamura S, Ochiai H, Sasaki T, Ohashi Y (2002) Enhanced resistance to seed-transmitted bacterial diseases in transgenic rice plants overproducing an oat cell-wall-bound thionin. Mol Plant Microbe Interact 15:515–521PubMedGoogle Scholar
  36. Jones JDG, Dangl JL (2006) The plant immune system. Nature 444:323–329PubMedGoogle Scholar
  37. Jung HW, Kim KD, Hwang BK (2003) Three pathogen-inducible genes encoding lipid-transfer proteins from pepper are differentially activated by pathogens, abiotic and environmental stresses. Plant Cell Environ 26:915–928PubMedGoogle Scholar
  38. Jung HW, Kim KD, Hwang BK (2005) Identification of pathogen-responsive regions in the promoter of a pepper lipid transfer protein gene (CALTP1) and the enhanced resistance of the CALTP1 transgenic Arabidopsis against pathogen and environmental stresses. Planta 221:361–373PubMedGoogle Scholar
  39. Kido EA, Pandolfi V, Houllou-Kido LM, Andrade PP, Marcelino FC, Nepomuceno AL, Abdelnoor RV, Burnquist WL, Benko-Iseppon AM (2010) Plant antimicrobial peptides: an overview of SuperSAGE transcriptional profile and a functional review. Curr Protein Pept Sci 11:220–230PubMedGoogle Scholar
  40. Koike M, Okamoto T, Tsuda S, Imai R (2002) A novel plant defensin-like gene of winter wheat is specifically induced during cold acclimation. Biochem Biophys Res Commun 298:46–53PubMedGoogle Scholar
  41. Koo JC, Lee SY, Chun HJ, Cheong YH, Choi JS, Kawabata S-I, Miyagi M, Tsunasawa S, Ha KS, Bae DW, Han C-D, Lee BL, Cho MJ (1998) Two hevein homologs isolated from the seed of Pharbitis nil L. exhibit potent antifungal activity. Biochim Biophys Acta 1382:80–90PubMedGoogle Scholar
  42. Koo JC, Chun HJ, Park HC, Kim MC, Koo YD, Koo SC, Ok HM, Park SJ, Lee S-H, Yun D-J, Lim CO, Bahk JD, Lee SY, Cho MJ (2002) Over-expression of a seed hevein-like antimicrobial peptide from Pharbitis nil enhances resistance to a fungal pathogen in transgenic tobacco plants. Plant Mol Biol 50:441–452PubMedGoogle Scholar
  43. Koo JC, Lee B, Young ME, Koo SC, Cooper JA, Baek D, Lim CO, Lee SY, Yun D-J, Cho MJ (2004) Pn-AMP1, a plant defense protein, induces actin depolarization in yeasts. Plant Cell Physiol 45:1669–1680PubMedGoogle Scholar
  44. Kushmerick C, de Souza CM, Santos Cruz J, Bloch C, Beirao PS (1998) Functional and structural features of gamma-zeathionins, a new class of sodium channel blockers. FEBS Lett 440:302–306PubMedGoogle Scholar
  45. Lay FT, Anderson MA (2005) Defensins–components of the innate immune system in plants. Curr Protein Pept Sci 6:85–101PubMedGoogle Scholar
  46. Lee OS, Lee B, Park N, Koo JC, Kim YH, Prasad D, Karigar C, Chun HJ, Jeong BR, Kim DH, Nam J, Yun J-G, Kwak S-S, Cho MJ, Yun D-J (2003) Pn-AMPs, the hevein-like proteins from Pharbitis nil confer disease resistance against phytopathogenic fungi in tomato, Lycopersicum esculentum. Phytochemistry 62:1073–1079PubMedGoogle Scholar
  47. Li S-S, Claeson P (2003) Cys/Gly-rich proteins with a putative single chitin-binding domain from oat (Avena sativa) seeds. Phytochemistry 63:249–255PubMedGoogle Scholar
  48. Li SS, Gullbo J, Lindholm P, Larsson R, Thunberg E, Samuelsson G, Bohlin L, Claeson P (2002) Ligatoxin B, a new cytotoxic protein with a novel helix-turn-helix DNA-binding domain from the mistletoe Phoradendron liga. Biochem J 361:405–413Google Scholar
  49. Lipkin A, Anisimova V, Nikonorova A, Babakov A, Krause A, Bienert M, Grishin E, Egorov T (2005) An antimicrobial peptide Ar-AMP from amaranth (Amaranthus retroflexus L.) seeds. Phytochemistry 66:2426–2431PubMedGoogle Scholar
  50. Lobo DS, Pereira IB, Fragel-Madeira L, Medeiros LN, Cabral LM, Faria J, Bellio M, Campos RC, Linden R, Kurtenbach E (2007) Antifungal Pisum sativum defensin 1 interacts with Neurospora crassa cyclin F related to the cell cycle. Biochemistry 46:987–996PubMedGoogle Scholar
  51. Loeza-Ángeles H, Sagrero-Cisneros E, Lara-Zárate L, Villagόmes-Gόmez E, Lόpez-Meza JE, Ochoa-Zarzosa A (2008) Thionin Thi2.1 from Arabidopsis thaliana expressed in endothelial cells shows antibacterial, antifungal and cytotoxic activity. Biotechnol Lett 10:1713–1719Google Scholar
  52. Manners JM (2007) Hidden weapons of microbial destruction in plant genomes. Genome Biol 8:225–234PubMedGoogle Scholar
  53. Matsumura H, Reich S, Ito A, Saitoh H, Kamoun S, Winter P, Kahl G, Reuter M, Kruger DH, Terauchi R (2003) Gene expression analysis of plant host-pathogen interactions by SuperSAGE. Proc Natl Acad Sci USA 100:15718–15723PubMedGoogle Scholar
  54. Melo FR, Rigden DJ, Franco OL, Mello LV, Ary MB, Grossi-de-Sa MF, Bloch C (2002) Inhibition of trypsin by cowpea thionin: characterization, molecular modeling and docking. Proteins 48:311–319PubMedGoogle Scholar
  55. Mendez E, Moreno A, Colilla FJ, Pelaez F, Limas GG, Mendez R, Soriano F, Salinas M, de Haro C (1990) Primary structure and inhibition of protein synthesis in eukaryotic cell–free system of a novel thionin, gamma-hordothionin, from barley endosperm. J Biochem 194:533–539Google Scholar
  56. Mendez E, Rocher A, Calero M, Girbes T, Citores L, Soriano F (1996) Primary structure of omega-hordothionin, a member of a novel family of thionins from barley endosperm, and its inhibition of protein synthesis in eukaryotic and prokaryotic cell-free systems. Eur J Biochem 239:67–73PubMedGoogle Scholar
  57. Mirouze M, Sels J, Richard O, Czernic P, Loubet S, Jacquier A, Francois IEJA, Cammue BPA, Lebrun M, Berthomieu P, Marques L (2006) A putative novel role for plant defensins: a defensin from zinc hyper-accumulating plant, Arabidopsis halleri, confers zinc tolerance. Plant J 47:329–342PubMedGoogle Scholar
  58. Nielsen KK, Nielsen JE, Madrid SM, Mikkelsen JD (1997) Characterization of a new antifungal chitin-binding peptide from sugar beet leaves. Plant Physiol 113:83–91PubMedGoogle Scholar
  59. Odintsova TI, TsA E, Musolyamov AKh, Odintsova MS, Pukhalsky VA, Grishin EV (2007) Seed defensins from T. kiharae and related species: genome localization of defensin-encoding genes. Biochimie 89:605–612PubMedGoogle Scholar
  60. Odintsova TI, Rogozhin EA, Baranov Y, Musolyamov AK, Yalpani N, Egorov TA, Grishin EV (2008) Seed defensins of barnyard grass Echinochloa crusgalli (L.) Beauv. Biochimie 90:1667–1673PubMedGoogle Scholar
  61. Odintsova TI, Vassilevski AA, Slavokhotova AA, Musolyamov AK, Finkina EI, Khadeeva NV, Rogozhin EA, Korostyleva TV, Pukhalsky VA, Grishin EV, Egorov TA (2009) A novel antifungal hevein-type peptide from Triticum kiharae seeds with a unique 10-cysteine motif. FEBS J 276:4266–4275PubMedGoogle Scholar
  62. Okuda S, Tsutsui H, Shiina K, Sprunck S, Takeuchi H, Yui R, Kasahara RD, Hamamura Y, Mizukami A, Susaki D, Kawano N, Sakakibara T, Namiki S, Itoh K, Otsuka K, Matsuzaki M, Nozaki H, Kuroiwa T, Nakano A, Kanaoka MM, Dresselhaus T, Sasaki N, Higashiyama T (2009) Defensin-like polypeptide LUREs are pollen tube attractants secreted from synergid cells. Nature 458:357–361PubMedGoogle Scholar
  63. Osborn RW, De Samblanx GW, Thevissen K, Goderis I, Torrekens S, Van Leuven F (1995) Isolation and characterization of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae. FEBS Lett 368:257–262PubMedGoogle Scholar
  64. Osbourn AE (1996) Preformed antimicrobial compounds and plant defense against fungal attack. Plant Cell 8:1821–1831PubMedGoogle Scholar
  65. Padovan L, Scocchi M, Tossi A (2010) Structural aspects of plant antimicrobial peptides. Curr Protein Pept Sci 11:210–219PubMedGoogle Scholar
  66. Pelegrini PB, Lay FT, Murad AM, Anderson MA, Franco OL (2008) Novel insights on the mechanism of action of alpha-amylase inhibitors from the plant defensin family. Proteins 73:719–729PubMedGoogle Scholar
  67. Pellegrini PB, Franco OL (2005) Plant gamma-thionins: novel insights on the mechanism of action of a multi-functional class of defense proteins. Int J Biochem Cell Biol 37:2239–2253Google Scholar
  68. Pieterse CMJ, Leon-Reyes A, Van der Ent S, Van Wees SCM (2009) Networking by small-molecule hormones in plant immunity. Nat Chem Biol 5:308–316PubMedGoogle Scholar
  69. Raikhel NV, Lee H-I (1993) Structure and function of chitin-binding proteins. Annu Rev Plant Physiol Plant Mol Biol 44:591–615Google Scholar
  70. Regente MC, Giudici AM, Villalain J, de la Canal L (2005) The cytotoxic properties of a plant lipid transfer protein involve membrane permeabilization of target cells. Lett Appl Microbiol 40:183–189PubMedGoogle Scholar
  71. Rivillas-Acevedo LA, Soriano-Garcia M (2007) Isolation and biochemical characterization of an antifungal peptide from Amaranthus hypochondriacus seeds. J Agric Food Chem 55:10156–10161PubMedGoogle Scholar
  72. Rogozhin EA, Odintsova TI, Musoliamov AKh, Smirnov AN, Babakov AV, TsA E, Grishin EV (2009) The purification and characterization of a novel lipid transfer protein from caryopsis of barnyard grass (Echinochloa crusgalli). Prikl Biokhim Mikrobiol 45:403–409PubMedGoogle Scholar
  73. Rogozhin EA, Oshchepkova YI, Odintsova TI, Khadeeva NV, Veshkurova ON, Egorov TA, Grishin EV, Salikhov SI (2011) Novel antifungal defensins from Nigella sativa L. seeds. Plant Physiol Biochem 49:131–137PubMedGoogle Scholar
  74. Schöpke T, Hasan Agha MI, Kraft R, Otto A, Hiller K (1993) Hämolytisch aktive komponenten aus Viola tricolor L. und Viola arvensis Murray. Sci Pharm 61:145–153Google Scholar
  75. Sels J, Mathys J, De Coninck BM, Cammue BP, De Bolle MF (2008) Plant pathogenesis-related (PR) proteins: a focus on PR peptides. Plant Physiol Biochem 46:941–950PubMedGoogle Scholar
  76. Shao F, Hu Z, Xiong Y, Huang Q, Wang C, Zhu R, Wang D (1999) A new antifungal peptide from the seeds of Phytolacca americana: characterization, amino acid sequence and cDNA cloning. Biochem Biophys Acta 1430:262–268PubMedGoogle Scholar
  77. Sharma P, Lönneborg A (1996) Isolation and characterization of a cDNA encoding a plant defensin-like protein from roots of Norway spruce. Plant Mol Biol 31:707–712PubMedGoogle Scholar
  78. Silverstein KA, Graham MA, Paape TD, VandenBosch KA (2005) Genome organization of more than 300 defensin-like genes in Arabidopsis. Plant Physiol 138:600–610PubMedGoogle Scholar
  79. Silverstein KA, Moskal WA Jr, Wu HC, Underwood BA, Graham MA, Town CD, VandenBosch KA (2007) Small cysteine-rich peptides resembling antimicrobial peptides have been under-predicted in plants. Plant J 51:262–280PubMedGoogle Scholar
  80. Slavokhotova AA, Odintsova TI, Rogozhin EA, Musolyamov AK, Andreev YA, Grishin EV, Egorov TA (2011) Isolation, molecular cloning and antimicrobial activity of novel defensins from common chickweed (Stellaria media L.) seeds. Biochimie 93:450–456PubMedGoogle Scholar
  81. Spelbrink RG, Dilmac N, Allen A, Smith TJ, Shah DM, Hockerman GH (2004) Differential antifungal and calcium channel-blocking activity among structurally related plant defensins. Plant Physiol 135:2055–2067PubMedGoogle Scholar
  82. Stec B (2006) Plant thionins – the structural perspective. Cell Mol Life Sci 63:1370–1385PubMedGoogle Scholar
  83. Stec B, Markman O, Rao U, Heffron G, Henderson S, Vernon LP, Brumfeld V, Teeter MM (2004) Proposal for molecular mechanism of thionins deduced from physico-chemical studies of plant toxins. J Pept Res 64:210–224PubMedGoogle Scholar
  84. Stotz HU, Spence B, Wang Y (2009a) A defensin from tomato with dual function in defense and development. Plant Mol Biol 71:131–143PubMedGoogle Scholar
  85. Stotz HU, Thomson JG, Wang Y (2009b) Plant defensins: defense, development and application. Plant Signal Behav 4:1010–1012PubMedGoogle Scholar
  86. Stuart LS, Harris TH (1942) Bactericidal and fungicidal properties of a crystalline protein from unbleached wheat flour. Cereal Chem 19:288–300Google Scholar
  87. Taji Y, Seki M, Satou M, Sakurai T, Kobayashi M, Ishiyama K, Narusaka Y, Narusaka M, Zhu JK, Shinozaki K (2004) Comparative genomics in salt tolerance between Arabidopsis and Arabidopsis–related halophyte salt cress using Arabidopsis microarray. Plant Physiol 135:1697–1709PubMedGoogle Scholar
  88. Tassin S, Broekaert WF, Marion D, Acland DP, Ptak M, Vovelle F, Sodano P (1998) Solution structure of Ace-AMP1, a potent antimicrobial protein extracted from onion seeds. Structural analogies with plant non-specific lipid transfer proteins. Biochemistry 37:3623–3637PubMedGoogle Scholar
  89. Tavares LS, de Santos M, Viccini LF, Mereira JS, Miller RNG, Franco OL (2008) Biotechnological potential of antimicrobial peptides from flowers. Peptides 29:1842–1851PubMedGoogle Scholar
  90. Terras FRG, Torrekens S, Van Leuven F, Osborn RW, Vanderleyden J, Cammue BPA, Broekaert WF (1993) A new family of basic cysteine-rich plant antifungal proteins from Brassicaceae species. FEBS Lett 316:233–240PubMedGoogle Scholar
  91. Thevissen K, Ghazi A, De Samblanx GW, Brownlee C, Osborn RW, Broekaert WF (1996) Fungal membrane responses induced by plant defensins and thionins. J Biol Chem 271:15018–15025PubMedGoogle Scholar
  92. Thevissen K, Warnecke DC, Francois IEJA, Leipelt M, Heinz E, Ott C (2004) Defensins from insects and plants interact with fungal glucosylceramides. J Biol Chem 279:3900–3905PubMedGoogle Scholar
  93. Thomma BP, Cammue BP, Thevissen K (2002) Plant defensins. Planta 216:193–202PubMedGoogle Scholar
  94. Titarenko E, Lopez-Solanilla E, Garcia-Olmedo F, Rodriguez-Palenzuela P (1997) Mutants of Ralstonia (Pseudomonas solanacearum) sensitive to antimicrobial peptides are altered in their LPS structure and are avirulent. J Bacteriol 179:6699–6704PubMedGoogle Scholar
  95. Torres MA, Jones JDG, Dangl JL (2006) Reactive oxygen species signaling in response to pathogens. Plant Physiol 141:373–378PubMedGoogle Scholar
  96. Utkina LL, Zhabon EO, Slavokhotova AA, Rogozhin EA, Shiyan AN, Grishin EV, Egorov TA, Odintsova TI, Pukhalskii VA (2010) Heterologous expression in Escherichia coli cells of a synthetic gene encoding a novel hevein-like peptide of Leymus arenarius. Russ J Genet 46:1–7Google Scholar
  97. Van den Bergh KPB, Proost P, Van Damme J, Coosemans J, Van Damme EJM, Peumans WJ (2002) Five disulfide bridges stabilize a hevein-type antimicrobial peptide from the bark of spindle tree (Euonymus europaeus L.). FEBS Lett 530:181–185PubMedGoogle Scholar
  98. Van den Bergh KPB, Rougé P, Proost P, Coosemans J, Krouglova T, Engelborghs Y, Peumans WJ, Van Damme EJM (2004) Synergistic antifungal activity of two chitin-binding proteins from spindle tree (Euonymus europaeus L.). Planta 219:221–232PubMedGoogle Scholar
  99. Van der Weerden NL, Lay FT, Anderson MA (2008) The plant defensin, NaD1, enters the cytoplasm of Fusarium oxysporum hyphae. J Biol Chem 283:14445–14452PubMedGoogle Scholar
  100. Van der Weerden NL, Hancock REW, Anderson MA (2010) Permeabilization of fungal hyphae by the plant defensin NaD1 occurs through a cell wall dependent process. J Biol Chem 285:37513–37520PubMedGoogle Scholar
  101. Van Loon LC, Rep M, Pieterse CM (2006) Significance of inducible defense-related proteins in infected plants. Annu Rev Phytopathol 44:135–162PubMedGoogle Scholar
  102. Van Parijs J, Broekaert WF, Goldstein IJ, Peumans WJ (1991) Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex. Planta 183:258–264Google Scholar
  103. Vila-Perello M, Sanchez-Vallet A, Garcia-Olmedo F, Molina A, Andreu D (2005) Structural dissection of a highly knotted peptide reveals minimal motif with antimicrobial activity. J Biol Chem 280:1661–1668PubMedGoogle Scholar
  104. Vila-Perello M, Tognon S, Sanchez-Vallet A, Garcia-Olmedo F, Molina A, Andreu D (2006) A minimalist design approach to antimicrobial agents based on a thionin template. J Med Chem 49:448–451PubMedGoogle Scholar
  105. Wang SY, Wu JH, Ng TB, Ye XY, Rao PF (2004) A non-specific lipid transfer protein with antifungal and antibacterial activities from the mung bean. Peptides 25:1235–1242PubMedGoogle Scholar
  106. Wijaya R, Neumann GM, Condron R, Hughes AB, Polya GM (2000) Defense proteins from seed of Cassia fistula include a lipid transfer protein homologue and a protease inhibitory plant defensin. Plant Sci 159:243–255PubMedGoogle Scholar
  107. Xiang Y, Huang R-H, Liu X-Z, Zhang Y, Wang D-C (2004) Crystal structure of a novel antifungal protein distinct with five disulfide bridges from Eucommia ulmoides Oliver at an atomic resolution. J Struct Biol 148:86–97PubMedGoogle Scholar
  108. Yeats TH, Rose JKC (2008) The biochemistry and biology of extracellular plant lipid-transfer proteins (LTPs). Protein Sci 17:191–198PubMedGoogle Scholar
  109. Yount NY, Yeaman MR (2004) Multidimensional signatures in antimicrobial peptides. Proc Natl Acad Sci USA 101:7363–7368PubMedGoogle Scholar
  110. Zaiou M (2007) Multifunctional antimicrobial peptides: therapeutic targets in several human diseases. J Mol Med 85:317–329PubMedGoogle Scholar
  111. Zottich U, Da Cunha M, Carvalho AO, Dias GB, Silva NC, Santos IS, do Nacimento VV, Miguel EC, Machado OL, Gomes VM (2011) Purification, biochemical characterization and antifungal activity of a new lipid transfer protein (LTP) from Coffea canephora seeds with α-amylase inhibitor properties. Biochim Biophys Acta 1810:375–383PubMedGoogle Scholar

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© Springer-Verlag Berlin Heidelberg 2012

Authors and Affiliations

  1. 1.Vavilov Institute of General GeneticsRussian Academy of SciencesMoscowRussian Federation
  2. 2.Shemyakin and Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of SciencesMoscowRussian Federation

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