Abstract
Disease afflicts crop productivity as well as nutritional attributes. Pathogens have the ability to mutate rapidly and thereby develop resistance to pesticides. Despite plant’s multilayer of innate defence against pathogens, often the latter are able to penetrate and establish themselves on plant host. The discovery of antimicrobial peptides (AMPs) has the promise of durable defence by quickly eliminating pathogens through membrane lysis. AMPs characteristically are made up of from fewer than 20 amino acids to about 100 amino acids, and yet are structurally diverse. AMPs in plants are classified into cyclotides, defensins, lipid transfer proteins (LTPs), thionins, snakins, hevein-like peptides, knottin-type peptides, and others. It is important to characterize and study mechanism of their action in order to develop a wide range of structures with the potential to provide durable plant immunity against pathogens. We bring together recent information on the mechanisms by which AMPs are able to help the plant to thwart pathogen attack. Although permeabilizing cellular membrane is a major mechanism known for AMP action, new and diverse modes of action have recently been unearthed, including targeting of intracellular function of the pathogen.
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References
Aerts AM, FranÅois IEJA, Cammue BPA, Thevissen K (2008) The mode of antifungal action of plant, insect and human defensins. Cell Mol Life Sci 65:2069–2079
Amien S, Kliwer I, Márton ML, Debener T, Geiger D, Becker D, Dresselhaus T (2010) Defensin-like ZmES4 mediates pollen tube burst in maize via opening of the potassium channel KZM1. PLoS Biol 8:e1000388
Bolton MD (2009) Primary metabolism and plant defense—fuel for the fire. MPMI 22:487–497
Brogden KA (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3:238–250
Brown JKM (2002) Yield penalties of disease resistance in crops. Curr Opin Plant Biol 5:1–6
Burman R, Gunasekera S, Strömstedt AA, Göransson U (2014) Chemistry and biology of cyclotides: circular plant peptides outside the box. J Nat Prod 77:724–736
Cammue BP, De Bolle MF, Terras FR, Proost P, Van Damme J, Rees SB, Vanderleyden J, Broekaert WF (1992) Isolation and characterization of a novel class of plant antimicrobial peptides form Mirabilis jalapa L seeds. J Biol Chem 267:2228–2233
Chae K, Kieslich CA, Morikis D, Kim SC, Lord EM (2009) A gain-of-function mutation of Arabidopsis lipid transfer protein 5 disturbs pollen tube tip growth and fertilization. Plant Cell 21:3902–3914
Chisholm ST, Coaker G, Day B, Staskawicz BJ (2006) Host-microbe interactions: shaping the evolution of the plant immune response. Cell 124:803–814
Choi KY, Chow LN, Mookherjee N (2012) Cationic host defence peptides: multifaceted role in immune modulation and inflammation. J Innate Immun 4:361–370
DeBono A, Yeats TH, Rose JKC, Bird D, Jetter R, Kunst L, Samuels L (2009) Arabidopsis LTPG is a glycosylphosphatidylinositol-anchored lipid transfer protein required for export of lipids to the plant surface. Plant Cell 21:1230–1238
Doughty J, Dixon S, Hiscock SJ, Willis AC, Parkin IAP, Dickinson HG (1998) PCP–A1, a defensin-like Brassica pollen coat protein that binds the S locus glycoprotein, is the product of gametophytic gene expression. Plant Cell 10:1333–1347
Gennaro R, Zanetti M (2000) Structural features and biological activities of the cathelicidin-derived antimicrobial peptides. Pept Sci 55:31–49
Goyal RK, Mattoo AK (2014) Multitasking antimicrobial peptides in plant development and host defense against biotic/abiotic stress. Plant Sci 228:135–149. doi:10.1016/j.plantsci.2014.05.012
Goyal RK, Hancock REW, Mattoo AK, Misra S (2013) Expression of an engineered heterologous antimicrobial peptide in potato alters plant development and mitigates normal abiotic and biotic responses. PLoS ONE 8:e82838
Graham MA, Silverstein KAT, Cannon SB, VandenBosch KA (2004) Computational identification and characterization of novel genes from legumes. Plant Physiol 135:1179–1197
Hammami R, Hamida JB, Vergoten G, Fliss I (2009) PhytAMP: a database dedicated to plant antimicrobial peptides. Nucleic Acids Res 37:D963–D968. doi:10.1093/nar/gkn655
Henriques ST, Melo MN, Castanho MA (2006) Cell-penetrating peptides and antimicrobial peptides: how different are they? Biochem J 399:1–7
Hilchie AL, Wuerth K, Hancock REW (2013) Immune modulation by multifaceted cationic host defense (antimicrobial) peptides. Nat Chem Biol 9:61–768
Holaskova E, Galuszka P, Frebort I, Oz MT (2015) Antimicrobial peptide production and plant-based expression systems for medical and agricultural biotechnology. Biotechnol Adv 33:1005–1023
Kim DH, Lee DG, Kim KL, Lee Y (2001) Internalization of tenecin 3 by a fungal cellular process is essential for its fungicidal effect on Candida albicans. Eur J Biochem 268:4449–4458
Lacerda AF, Vasconcelos ÉAR, Pelegrini PB, Grossi de Sa MF (2014) Antifungal defensins and their role in plant defense. Front Microbiol 5:116. doi:10.3389/fmicb.2014.00116
Liew PS, Hair-Bejo H (2015) Farming of plant-based veterinary vaccines and their applications for disease prevention in animals. Adv Virol 2015:936940. doi:10.1155/2015/936940
Marshall E, Costa LM, Gutierrez-Marcos J (2011) Cysteine-rich peptides (CRPs) mediate diverse aspects of cell-cell communication in plant reproduction and development. J Exp Bot 62:1677–1686
Molina A, García-Olmedo F (1997) Enhanced tolerance to bacterial pathogens caused by the transgenic expression of barley lipid transfer protein LTP2. Plant J 12:669–675
Muñoz A, Gandía M, Harries E, Carmona L, Read ND, Marcos JF (2013) Understanding the mechanism of action of cell-penetrating antifungal peptides using the rationally designed hexapeptide PAF26 as a model. Fungal Biol Rev 26:146–155
Nahirñak V, Almasia NI, Fernandez PV, Hopp HE, Estevez JM, Carrari F, Vazquez-Rovere C (2012) Potato Snakin-1 gene silencing affects cell division, primary metabolism, and cell wall composition. Plant Physiol 158:252–263
Nawrot R, Barylski J, Nowicki G, Broniarczyk J, Buchwald W, Goździcka-Józefiaket A (2014) Plant antimicrobial peptides. Folia Microbiol 59:181–196
Nieuwland J, Feron R, Huisman BAH, Fasolino A, Hilbers CW, Derksen J, Mariani C (2005) Lipid transfer proteins enhance cell wall extension in tobacco. Plant Cell 17:2009–2019
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 458:357–361
Paiva AD and Breukink E (2013) Antimicrobial peptides produced by microorganisms. In: Hiemstra PS, Zaat SAJ (eds) Antimicrobial peptides and innate immunity—progress in inflammation research. Springer, Basel, pp 53–95. doi:10.1007/978-3-0348-0541-4_2
Park SY, Jauh GY, Mollet JC, Eckard KJ, Nothnagel EA, Walling LL, Lord EM (2000) A lipid transfer-like protein is necessary for lily pollen tube adhesion to an in vitro stylar matrix. Plant Cell 12:151–163
Pelegrini PB, del Sarto RP, Silva ON, Franco OL, Grossi-De-Sa MF (2011) Antibacterial peptides from plants: what they are and how they probably work. Biochem Res Int 2011:250349
Penterman J, Abo RP, De Nisco NJ, Arnold MF, Longhi R, Zanda M, Walker GC (2014) Host plant peptides elicit a transcriptional response to control the Sinorhizobium meliloti cell cycle during symbiosis. Proc Nat Acad Sci USA 111:3561–3566
Plattner S, Gruber C, Stadlmann J, Widmann S, Gruber CW, Altmann F, Bohlmann H (2015) Isolation and characterization of a thionin proprotein-processing enzyme from barley. J Biol Chem 290:18056–18067. doi:10.1074/jbc.M115.647859
Ponz F, Paz-Ares J, Hernandez-Lucas C, Carbonero P, Garcia-Olmedo F (1983) Synthesis and processing of thionin precursors in developing endosperm from barley (Hordeum vulgare L.). EMBO J 2:1035–1040
Sagaram US, Pandurangi R, Karu J, Smith TJ, Shah DM (2011) Structure-activity determinants in antifungal plant defensins MsDef1 and MtDef4 with different modes of action against Fusarium graminearum. PLoS ONE 6:e18550. doi:10.1371/journal.pone.0018550
Segura A, Moreno M, Madueno F, Garcia-Olmedo F (1993) Snakin-1, a peptide from potato that is active against plant pathogens. MPMI 12:16–23
Shai Y (2002) Mode of action of membrane active antimicrobial peptides. Biopolymers (Pept Sci) 66:236–248
Stec B (2006) Plant thionins—the structural perspective. Cell Mol Life Sci 63:1370–1385
Stotz HU, Spence B, Wang Y (2009) A defensin from tomato with dual function in defense and development. Plant Mol Biol 71:131–143
Stotz HU, Waller F and Wang K (2013) Innate immunity in plants: the role of antimicrobial peptides. In: Hiemstra PS, Zaat SAJ (eds) Antimicrobial peptides and innate immunity, progress in inflammation research, Springer, Basel, pp 29–51. doi:10.1007/978-3-0348-0541-4_2
Takayama S, Shimosato H, Shiba H, Funato M, Che FS, Watanabe M, Iwano M, Isogai A (2001) Direct ligand-receptor complex interaction controls Brassica self-incompatibility. Nature 413:534–538
Takeuchi H, Higashiyama T (2012) A species-specific cluster of defensin-like genes encodes diffusible pollen tube attractants in Arabidopsis. PLoS Biol 10:e1001449. doi:10.1371/journal.pbio.1001449
Tavormina P, Coninck B, Nikonorova N, Smet I, Cammuea BPA (2015) The plant peptidome: an expanding repertoire of structural features and biological functions. Plant Cell 27:2095–2118
Thevissen K, Ferket KKA, François IEJA, Cammue BPA (2003) Interactions of antifungal plant defensins with fungal membrane components. Peptides 24:1705–1712
van der Weerden NL, Bleackley MR, Anderson MA (2013) Properties and mechanisms of action of naturally occurring antifungal peptides. Cell Mol Life Sci 70:3545–3570
Van Parijs J, Broekaert WF, Goldstein IJ, Peumans WJ (1991) Hevein an antifungal protein from rubber-tree (Hevea braziliensis) latex. Planta 183:258–264
Vriens K, Cammue BPA, Thevissen K (2014) Antifungal plant defensins: mechanisms of action and production. Molecules 19:12280–12303. doi:10.3390/molecules190812280
Wimley WC (2010) Describing the mechanism of antimicrobial peptide action with the interfacial activity model. ACS Chem Biol 5:905–917
Yeaman MR, Yount NY (2003) Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev 55:27–55
Yount NY, Yeaman MR (2013) Peptide antimicrobials: cell wall as a bacterial target. Ann N Y Acad Sci 1277:127–138
Zasloff M (2002) Antimicrobial peptides of multicellular organisms. Nature 415:389–395
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Goyal, R.K., Mattoo, A.K. (2016). Plant Antimicrobial Peptides. In: Epand, R. (eds) Host Defense Peptides and Their Potential as Therapeutic Agents. Springer, Cham. https://doi.org/10.1007/978-3-319-32949-9_5
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