Berberine Bridge Enzyme-like Oligosaccharide Oxidases Act as Enzymatic Transducers Between Microbial Glycoside Hydrolases and Plant Peroxidases

Oligogalacturonide (OG)-oxidase 1 (OGOX1) and cellodextrin (CD)-oxidase (CELLOX) are plant berberine bridge enzyme-like oligosaccharide oxidases that oxidize OGs and CDs, cell-wall fragments with the nature of damage-associated molecular patterns. The oxidation of OGs and CDs attenuates their elicit...

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Main Authors: Anna Scortica, Moira Giovannoni, Valentina Scafati, Francesco Angelucci, Felice Cervone, Giulia De Lorenzo, Manuel Benedetti, Benedetta Mattei
Format: Article
Language:English
Published: The American Phytopathological Society 2022-10-01
Series:Molecular Plant-Microbe Interactions
Subjects:
Online Access:https://apsjournals.apsnet.org/doi/10.1094/MPMI-05-22-0113-TA
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author Anna Scortica
Moira Giovannoni
Valentina Scafati
Francesco Angelucci
Felice Cervone
Giulia De Lorenzo
Manuel Benedetti
Benedetta Mattei
author_facet Anna Scortica
Moira Giovannoni
Valentina Scafati
Francesco Angelucci
Felice Cervone
Giulia De Lorenzo
Manuel Benedetti
Benedetta Mattei
author_sort Anna Scortica
collection DOAJ
description Oligogalacturonide (OG)-oxidase 1 (OGOX1) and cellodextrin (CD)-oxidase (CELLOX) are plant berberine bridge enzyme-like oligosaccharide oxidases that oxidize OGs and CDs, cell-wall fragments with the nature of damage-associated molecular patterns. The oxidation of OGs and CDs attenuates their elicitor activity and concomitantly releases H2O2. By using a multiple enzyme–based assay, we demonstrate that the H2O2 generated downstream of the combined action between a fungal polygalacturonase and OGOX1 or an endoglucanase and CELLOX can be directed by plant peroxidases (PODs) either towards a reaction possibly involved in plant defense, such as the oxidation of monolignol or a reaction possibly involved in a developmental event, such as the oxidation of auxin (indole-3-acetic acid), pointing to OGOX1 and CELLOX as enzymatic transducers between microbial glycoside hydrolases and plant PODs. [Graphic: see text] Copyright © 2022 The Author(s). This is an open access article distributed under the CC BY-NC-ND 4.0 International license.
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spelling doaj.art-b963aa39ffae46b3acce508d7f6cf7782022-12-22T03:38:19ZengThe American Phytopathological SocietyMolecular Plant-Microbe Interactions0894-02821943-77062022-10-01351088188610.1094/MPMI-05-22-0113-TABerberine Bridge Enzyme-like Oligosaccharide Oxidases Act as Enzymatic Transducers Between Microbial Glycoside Hydrolases and Plant PeroxidasesAnna Scortica0Moira Giovannoni1Valentina Scafati2Francesco Angelucci3Felice Cervone4Giulia De Lorenzo5Manuel Benedetti6Benedetta Mattei7Department of Life, Health and Environmental Sciences, University of L'Aquila, 67100 L'Aquila, ItalyDepartment of Life, Health and Environmental Sciences, University of L'Aquila, 67100 L'Aquila, ItalyDepartment of Life, Health and Environmental Sciences, University of L'Aquila, 67100 L'Aquila, ItalyDepartment of Life, Health and Environmental Sciences, University of L'Aquila, 67100 L'Aquila, ItalyDepartment of Biology and Biotechnology “Charles Darwin”, Sapienza University of Rome, 00185 Rome, ItalyDepartment of Biology and Biotechnology “Charles Darwin”, Sapienza University of Rome, 00185 Rome, ItalyDepartment of Life, Health and Environmental Sciences, University of L'Aquila, 67100 L'Aquila, ItalyDepartment of Life, Health and Environmental Sciences, University of L'Aquila, 67100 L'Aquila, ItalyOligogalacturonide (OG)-oxidase 1 (OGOX1) and cellodextrin (CD)-oxidase (CELLOX) are plant berberine bridge enzyme-like oligosaccharide oxidases that oxidize OGs and CDs, cell-wall fragments with the nature of damage-associated molecular patterns. The oxidation of OGs and CDs attenuates their elicitor activity and concomitantly releases H2O2. By using a multiple enzyme–based assay, we demonstrate that the H2O2 generated downstream of the combined action between a fungal polygalacturonase and OGOX1 or an endoglucanase and CELLOX can be directed by plant peroxidases (PODs) either towards a reaction possibly involved in plant defense, such as the oxidation of monolignol or a reaction possibly involved in a developmental event, such as the oxidation of auxin (indole-3-acetic acid), pointing to OGOX1 and CELLOX as enzymatic transducers between microbial glycoside hydrolases and plant PODs. [Graphic: see text] Copyright © 2022 The Author(s). This is an open access article distributed under the CC BY-NC-ND 4.0 International license.https://apsjournals.apsnet.org/doi/10.1094/MPMI-05-22-0113-TAauxinberberine bridge enzyme-like proteinDAMPsglycoside hydrolaseH(2)O(2)lignin
spellingShingle Anna Scortica
Moira Giovannoni
Valentina Scafati
Francesco Angelucci
Felice Cervone
Giulia De Lorenzo
Manuel Benedetti
Benedetta Mattei
Berberine Bridge Enzyme-like Oligosaccharide Oxidases Act as Enzymatic Transducers Between Microbial Glycoside Hydrolases and Plant Peroxidases
Molecular Plant-Microbe Interactions
auxin
berberine bridge enzyme-like protein
DAMPs
glycoside hydrolase
H(2)O(2)
lignin
title Berberine Bridge Enzyme-like Oligosaccharide Oxidases Act as Enzymatic Transducers Between Microbial Glycoside Hydrolases and Plant Peroxidases
title_full Berberine Bridge Enzyme-like Oligosaccharide Oxidases Act as Enzymatic Transducers Between Microbial Glycoside Hydrolases and Plant Peroxidases
title_fullStr Berberine Bridge Enzyme-like Oligosaccharide Oxidases Act as Enzymatic Transducers Between Microbial Glycoside Hydrolases and Plant Peroxidases
title_full_unstemmed Berberine Bridge Enzyme-like Oligosaccharide Oxidases Act as Enzymatic Transducers Between Microbial Glycoside Hydrolases and Plant Peroxidases
title_short Berberine Bridge Enzyme-like Oligosaccharide Oxidases Act as Enzymatic Transducers Between Microbial Glycoside Hydrolases and Plant Peroxidases
title_sort berberine bridge enzyme like oligosaccharide oxidases act as enzymatic transducers between microbial glycoside hydrolases and plant peroxidases
topic auxin
berberine bridge enzyme-like protein
DAMPs
glycoside hydrolase
H(2)O(2)
lignin
url https://apsjournals.apsnet.org/doi/10.1094/MPMI-05-22-0113-TA
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