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Insect peptide metchnikowin confers on barley a selective capacity for resistance to fungal ascomycetes pathogens

The potential of metchnikowin, a 26-amino acid residue proline-rich antimicrobial peptide synthesized in the fat body of Drosophila melanogaster was explored to engineer disease resistance in barley against devastating fungal plant pathogens. The synthetic peptide caused strong in vitro growth inhib...

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Autores principales: Rahnamaeian, Mohammad, Langen, Gregor, Imani, Jafargholi, Khalifa, Walaa, Altincicek, Boran, von Wettstein, Diter, Kogel, Karl-Heinz, Vilcinskas, Andreas
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2755027/
https://www.ncbi.nlm.nih.gov/pubmed/19734262
http://dx.doi.org/10.1093/jxb/erp240
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author Rahnamaeian, Mohammad
Langen, Gregor
Imani, Jafargholi
Khalifa, Walaa
Altincicek, Boran
von Wettstein, Diter
Kogel, Karl-Heinz
Vilcinskas, Andreas
author_facet Rahnamaeian, Mohammad
Langen, Gregor
Imani, Jafargholi
Khalifa, Walaa
Altincicek, Boran
von Wettstein, Diter
Kogel, Karl-Heinz
Vilcinskas, Andreas
author_sort Rahnamaeian, Mohammad
collection PubMed
description The potential of metchnikowin, a 26-amino acid residue proline-rich antimicrobial peptide synthesized in the fat body of Drosophila melanogaster was explored to engineer disease resistance in barley against devastating fungal plant pathogens. The synthetic peptide caused strong in vitro growth inhibition (IC(50) value ∼1 μM) of the pathogenic fungus Fusarium graminearum. Transgenic barley expressing the metchnikowin gene in its 52-amino acid pre-pro-peptide form under the control of the inducible mannopine synthase (mas) gene promoter from the T(i) plasmid of Agrobacterium tumefaciens displayed enhanced resistance to powdery mildew as well as Fusarium head blight and root rot. In response to these pathogens, metchnikowin accumulated in plant apoplastic space, specifying that the insect signal peptide is functional in monocotyledons. In vitro and in vivo tests revealed that the peptide is markedly effective against fungal pathogens of the phylum Ascomycota but, clearly, less active against Basidiomycota fungi. Importantly, germination of the mutualistic basidiomycete mycorrhizal fungus Piriformospora indica was affected only at concentrations beyond 50 μM. These results suggest that antifungal peptides from insects are a valuable source for crop plant improvements and their differential activities toward different phyla of fungi denote a capacity for insect peptides to be used as selective measures on specific plant diseases.
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spelling pubmed-27550272009-10-02 Insect peptide metchnikowin confers on barley a selective capacity for resistance to fungal ascomycetes pathogens Rahnamaeian, Mohammad Langen, Gregor Imani, Jafargholi Khalifa, Walaa Altincicek, Boran von Wettstein, Diter Kogel, Karl-Heinz Vilcinskas, Andreas J Exp Bot Research Papers The potential of metchnikowin, a 26-amino acid residue proline-rich antimicrobial peptide synthesized in the fat body of Drosophila melanogaster was explored to engineer disease resistance in barley against devastating fungal plant pathogens. The synthetic peptide caused strong in vitro growth inhibition (IC(50) value ∼1 μM) of the pathogenic fungus Fusarium graminearum. Transgenic barley expressing the metchnikowin gene in its 52-amino acid pre-pro-peptide form under the control of the inducible mannopine synthase (mas) gene promoter from the T(i) plasmid of Agrobacterium tumefaciens displayed enhanced resistance to powdery mildew as well as Fusarium head blight and root rot. In response to these pathogens, metchnikowin accumulated in plant apoplastic space, specifying that the insect signal peptide is functional in monocotyledons. In vitro and in vivo tests revealed that the peptide is markedly effective against fungal pathogens of the phylum Ascomycota but, clearly, less active against Basidiomycota fungi. Importantly, germination of the mutualistic basidiomycete mycorrhizal fungus Piriformospora indica was affected only at concentrations beyond 50 μM. These results suggest that antifungal peptides from insects are a valuable source for crop plant improvements and their differential activities toward different phyla of fungi denote a capacity for insect peptides to be used as selective measures on specific plant diseases. Oxford University Press 2009-10 2009-09-04 /pmc/articles/PMC2755027/ /pubmed/19734262 http://dx.doi.org/10.1093/jxb/erp240 Text en © 2009 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)
spellingShingle Research Papers
Rahnamaeian, Mohammad
Langen, Gregor
Imani, Jafargholi
Khalifa, Walaa
Altincicek, Boran
von Wettstein, Diter
Kogel, Karl-Heinz
Vilcinskas, Andreas
Insect peptide metchnikowin confers on barley a selective capacity for resistance to fungal ascomycetes pathogens
title Insect peptide metchnikowin confers on barley a selective capacity for resistance to fungal ascomycetes pathogens
title_full Insect peptide metchnikowin confers on barley a selective capacity for resistance to fungal ascomycetes pathogens
title_fullStr Insect peptide metchnikowin confers on barley a selective capacity for resistance to fungal ascomycetes pathogens
title_full_unstemmed Insect peptide metchnikowin confers on barley a selective capacity for resistance to fungal ascomycetes pathogens
title_short Insect peptide metchnikowin confers on barley a selective capacity for resistance to fungal ascomycetes pathogens
title_sort insect peptide metchnikowin confers on barley a selective capacity for resistance to fungal ascomycetes pathogens
topic Research Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2755027/
https://www.ncbi.nlm.nih.gov/pubmed/19734262
http://dx.doi.org/10.1093/jxb/erp240
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