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A conserved GH17 glycosyl hydrolase from plant pathogenic Dothideomycetes releases a DAMP causing cell death in tomato

To facilitate infection, pathogens deploy a plethora of effectors to suppress basal host immunity induced by exogenous microbe‐associated or endogenous damage‐associated molecular patterns (DAMPs). In this study, we have characterized family 17 glycosyl hydrolases of the tomato pathogen Cladosporium...

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Autores principales: Ökmen, Bilal, Bachmann, Daniel, de Wit, Pierre J.G.M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6859711/
https://www.ncbi.nlm.nih.gov/pubmed/31603622
http://dx.doi.org/10.1111/mpp.12872
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author Ökmen, Bilal
Bachmann, Daniel
de Wit, Pierre J.G.M.
author_facet Ökmen, Bilal
Bachmann, Daniel
de Wit, Pierre J.G.M.
author_sort Ökmen, Bilal
collection PubMed
description To facilitate infection, pathogens deploy a plethora of effectors to suppress basal host immunity induced by exogenous microbe‐associated or endogenous damage‐associated molecular patterns (DAMPs). In this study, we have characterized family 17 glycosyl hydrolases of the tomato pathogen Cladosporium fulvum (CfGH17) and studied their role in infection. Heterologous expression of CfGH17‐1 to 5 by potato virus X in different tomato cultivars showed that CfGH17‐1 and CfGH17‐5 enzymes induce cell death in Cf‐0, Cf‐1 and Cf‐5 but not in Cf‐Ecp3 tomato cultivars or tobacco. Moreover, CfGH17‐1 orthologues from other phytopathogens, including Dothistroma septosporum and Mycosphaerella fijiensis, also trigger cell death in tomato. CfGH17‐1 and CfGH17‐5 are predicted to be β‐1,3‐glucanases and their enzymatic activity is required for the induction of cell death. CfGH17‐1 hydrolyses laminarin, a linear 1,3‐β‐glucan with 1,6‐β linkages. CfGH17‐1 expression is down‐regulated during the biotrophic phase of infection and up‐regulated during the necrotrophic phase. Deletion of CfGH17‐1 in C. fulvum did not reduce virulence on tomato, while constitutive expression of CfGH17‐1 decreased virulence, suggesting that abundant presence of CfGH17‐1 during biotrophic growth may release a DAMP that activates plant defence responses. Under natural conditions CfGH17‐1 is suggested to play a role during saprophytic growth when the fungus thrives on dead host tissue, which is in line with its high levels of expression at late stages of infection when host tissues have become necrotic. We suggest that CfGH17‐1 releases a DAMP from the host cell wall that is recognized by a yet unknown host plant receptor.
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spelling pubmed-68597112019-12-12 A conserved GH17 glycosyl hydrolase from plant pathogenic Dothideomycetes releases a DAMP causing cell death in tomato Ökmen, Bilal Bachmann, Daniel de Wit, Pierre J.G.M. Mol Plant Pathol Original Articles To facilitate infection, pathogens deploy a plethora of effectors to suppress basal host immunity induced by exogenous microbe‐associated or endogenous damage‐associated molecular patterns (DAMPs). In this study, we have characterized family 17 glycosyl hydrolases of the tomato pathogen Cladosporium fulvum (CfGH17) and studied their role in infection. Heterologous expression of CfGH17‐1 to 5 by potato virus X in different tomato cultivars showed that CfGH17‐1 and CfGH17‐5 enzymes induce cell death in Cf‐0, Cf‐1 and Cf‐5 but not in Cf‐Ecp3 tomato cultivars or tobacco. Moreover, CfGH17‐1 orthologues from other phytopathogens, including Dothistroma septosporum and Mycosphaerella fijiensis, also trigger cell death in tomato. CfGH17‐1 and CfGH17‐5 are predicted to be β‐1,3‐glucanases and their enzymatic activity is required for the induction of cell death. CfGH17‐1 hydrolyses laminarin, a linear 1,3‐β‐glucan with 1,6‐β linkages. CfGH17‐1 expression is down‐regulated during the biotrophic phase of infection and up‐regulated during the necrotrophic phase. Deletion of CfGH17‐1 in C. fulvum did not reduce virulence on tomato, while constitutive expression of CfGH17‐1 decreased virulence, suggesting that abundant presence of CfGH17‐1 during biotrophic growth may release a DAMP that activates plant defence responses. Under natural conditions CfGH17‐1 is suggested to play a role during saprophytic growth when the fungus thrives on dead host tissue, which is in line with its high levels of expression at late stages of infection when host tissues have become necrotic. We suggest that CfGH17‐1 releases a DAMP from the host cell wall that is recognized by a yet unknown host plant receptor. John Wiley and Sons Inc. 2019-10-11 /pmc/articles/PMC6859711/ /pubmed/31603622 http://dx.doi.org/10.1111/mpp.12872 Text en © 2019 The Authors. Molecular Plant Pathology published by British Society for Plant Pathology and John Wiley & Sons Ltd This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.
spellingShingle Original Articles
Ökmen, Bilal
Bachmann, Daniel
de Wit, Pierre J.G.M.
A conserved GH17 glycosyl hydrolase from plant pathogenic Dothideomycetes releases a DAMP causing cell death in tomato
title A conserved GH17 glycosyl hydrolase from plant pathogenic Dothideomycetes releases a DAMP causing cell death in tomato
title_full A conserved GH17 glycosyl hydrolase from plant pathogenic Dothideomycetes releases a DAMP causing cell death in tomato
title_fullStr A conserved GH17 glycosyl hydrolase from plant pathogenic Dothideomycetes releases a DAMP causing cell death in tomato
title_full_unstemmed A conserved GH17 glycosyl hydrolase from plant pathogenic Dothideomycetes releases a DAMP causing cell death in tomato
title_short A conserved GH17 glycosyl hydrolase from plant pathogenic Dothideomycetes releases a DAMP causing cell death in tomato
title_sort conserved gh17 glycosyl hydrolase from plant pathogenic dothideomycetes releases a damp causing cell death in tomato
topic Original Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6859711/
https://www.ncbi.nlm.nih.gov/pubmed/31603622
http://dx.doi.org/10.1111/mpp.12872
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