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The Extracellular Superoxide Dismutase Sod5 From Fusarium oxysporum Is Localized in Response to External Stimuli and Contributes to Fungal Pathogenicity

Reactive oxygen species (ROS) produced by hosts serve as a general defense mechanism against various pathogens. At the interaction site between the host and pathogen, host cells rapidly accumulate high concentrations of ROS, called the oxidative burst, that damage and kill the invading microbes. How...

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Autores principales: Wang, Qiang, Pokhrel, Ambika, Coleman, Jeffrey J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7960929/
https://www.ncbi.nlm.nih.gov/pubmed/33737941
http://dx.doi.org/10.3389/fpls.2021.608861
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author Wang, Qiang
Pokhrel, Ambika
Coleman, Jeffrey J.
author_facet Wang, Qiang
Pokhrel, Ambika
Coleman, Jeffrey J.
author_sort Wang, Qiang
collection PubMed
description Reactive oxygen species (ROS) produced by hosts serve as a general defense mechanism against various pathogens. At the interaction site between the host and pathogen, host cells rapidly accumulate high concentrations of ROS, called the oxidative burst, that damage and kill the invading microbes. However, successful pathogens usually survive in a high ROS environment and have evolved strategies to overcome these detrimental effects. Here we characterized the biological function of the extracellular superoxide dismutase (SOD) FoSod5 from Fusarium oxysporum f. sp. vasinfectum. FoSOD5 is strongly up-regulated during infection of cotton, and a ΔFoSOD5 mutant was significantly reduced in virulence on cotton. Purified 6 × His-FoSod5 could significantly inhibit the reduction of NBT and WST-1, indicating that FoSod5 was a functional SOD protein. Based on CRISPR/Cas9 technology, several different FoSod5 variants were generated and used to assess the secretion, expression, and subcellular localization of FoSod5 in F. oxysporum. The subcellular localization of FoSod5 is altered under different environmental conditions. During normal growth conditions, FoSod5 was primarily localized to the phialides; however, in a nutrient-limited environment, FoSod5 was localized to a wide array of fungal structures including the septum and cell wall. FoSod5 is an alkaline-induced glycosylphosphatidylinositol (GPI) protein and the GPI anchor was required for proper protein subcellular localization. The multiple mechanisms fungi utilize to tolerate the oxidative burst is indicative of the importance of this plant defense response; however, the presence of a conserved extracellular SOD in many phytopathogenic fungi suggests tolerance to ROS is initiated prior to the ROS entering the fungal cell.
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spelling pubmed-79609292021-03-17 The Extracellular Superoxide Dismutase Sod5 From Fusarium oxysporum Is Localized in Response to External Stimuli and Contributes to Fungal Pathogenicity Wang, Qiang Pokhrel, Ambika Coleman, Jeffrey J. Front Plant Sci Plant Science Reactive oxygen species (ROS) produced by hosts serve as a general defense mechanism against various pathogens. At the interaction site between the host and pathogen, host cells rapidly accumulate high concentrations of ROS, called the oxidative burst, that damage and kill the invading microbes. However, successful pathogens usually survive in a high ROS environment and have evolved strategies to overcome these detrimental effects. Here we characterized the biological function of the extracellular superoxide dismutase (SOD) FoSod5 from Fusarium oxysporum f. sp. vasinfectum. FoSOD5 is strongly up-regulated during infection of cotton, and a ΔFoSOD5 mutant was significantly reduced in virulence on cotton. Purified 6 × His-FoSod5 could significantly inhibit the reduction of NBT and WST-1, indicating that FoSod5 was a functional SOD protein. Based on CRISPR/Cas9 technology, several different FoSod5 variants were generated and used to assess the secretion, expression, and subcellular localization of FoSod5 in F. oxysporum. The subcellular localization of FoSod5 is altered under different environmental conditions. During normal growth conditions, FoSod5 was primarily localized to the phialides; however, in a nutrient-limited environment, FoSod5 was localized to a wide array of fungal structures including the septum and cell wall. FoSod5 is an alkaline-induced glycosylphosphatidylinositol (GPI) protein and the GPI anchor was required for proper protein subcellular localization. The multiple mechanisms fungi utilize to tolerate the oxidative burst is indicative of the importance of this plant defense response; however, the presence of a conserved extracellular SOD in many phytopathogenic fungi suggests tolerance to ROS is initiated prior to the ROS entering the fungal cell. Frontiers Media S.A. 2021-03-02 /pmc/articles/PMC7960929/ /pubmed/33737941 http://dx.doi.org/10.3389/fpls.2021.608861 Text en Copyright © 2021 Wang, Pokhrel and Coleman. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Wang, Qiang
Pokhrel, Ambika
Coleman, Jeffrey J.
The Extracellular Superoxide Dismutase Sod5 From Fusarium oxysporum Is Localized in Response to External Stimuli and Contributes to Fungal Pathogenicity
title The Extracellular Superoxide Dismutase Sod5 From Fusarium oxysporum Is Localized in Response to External Stimuli and Contributes to Fungal Pathogenicity
title_full The Extracellular Superoxide Dismutase Sod5 From Fusarium oxysporum Is Localized in Response to External Stimuli and Contributes to Fungal Pathogenicity
title_fullStr The Extracellular Superoxide Dismutase Sod5 From Fusarium oxysporum Is Localized in Response to External Stimuli and Contributes to Fungal Pathogenicity
title_full_unstemmed The Extracellular Superoxide Dismutase Sod5 From Fusarium oxysporum Is Localized in Response to External Stimuli and Contributes to Fungal Pathogenicity
title_short The Extracellular Superoxide Dismutase Sod5 From Fusarium oxysporum Is Localized in Response to External Stimuli and Contributes to Fungal Pathogenicity
title_sort extracellular superoxide dismutase sod5 from fusarium oxysporum is localized in response to external stimuli and contributes to fungal pathogenicity
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7960929/
https://www.ncbi.nlm.nih.gov/pubmed/33737941
http://dx.doi.org/10.3389/fpls.2021.608861
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