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Scortica, A.

Publications and source records attributed to Scortica, A..

3 recordsLinked to original sources

The reducing end of cell wall oligosaccharides is critical for DAMP activity in Arabidopsis thaliana and can be exploited by oligosaccharide oxidases in the scavenging of phenolic radicals.

O_LIThe enzymatic hydrolysis of cell wall polysaccharides results in the production of oligosaccharides with nature of damage-associated molecular patterns (DAMPs) that are perceived by plants as danger signals. In vitro, the oxidation of oligogalacturonides and cellodextrins by plant FAD-dependent oligosaccharide-oxidases (OSOXs) suppresses their elicitor activity, suggesting a protective role of OSOXs against a prolonged activation of defense responses potentially deleterious for plant health. However, OSOXs are also produced by phytopathogens and saprotrophs, complicating the understanding of their role in plant-microbe interactions. C_LIO_LIThe oxidation catalyzed by specific fungal OSOXs also converts the elicitor-active cello-tetraose and xylo-tetraose into elicitor-inactive forms, indicating that the oxidation state of cell wall oligosaccharides is crucial for their DAMP function, irrespective of whether the OSOX originates from fungi or plants. C_LIO_LICertain OSOXs can transfer the electrons from the reducing end of these oligosaccharides to phenolic radicals instead of molecular O2, highlighting an unexpected sub-functionalization of these enzymes. C_LIO_LIThe activity of OSOXs may be crucial for a thorough understanding of cell wall metabolism since these enzymes can redirect the reducing power from sugars to phenolic components of the plant cell wall, an insight with relevant implications for both plant physiology and green technologies. C_LI

plant biology↗

RADICAL CATION SCAVENGING ACTIVITY OF BERBERINE BRIDGE ENZYME-LIKE OLIGOSACCHARIDE OXIDASES ACTING ON SHORT CELL WALL FRAGMENTS.

Oligogalacturonide-oxidases (OGOXs) and cellodextrin-oxidase (CELLOX) are plant berberine bridge enzyme-like oligosaccharide-oxidases (OSOXs) that oxidize, respectively, oligogalacturonides (OGs) and cellodextrins (CDs), thereby inactivating their elicitor nature and concomitantly releasing H2O2. Little is known about the physiological role of OSOX activity. By using an ABTS*+-reduction assay, we identified a novel reaction mechanism through which the activity of OSOXs on cell wall oligosaccharides scavenged the radical cation ABTS*+ with an efficiency dependent on the type and length of the oxidized oligosaccharide. In contrast to the oxidation of longer oligomers such as OGs (degree of polymerization from 10 to 15), the activity of OSOXs on short galacturonan- and cellulose-oligomers (degree of polymerization [≤] 4) successfully counteracted the radical cation-generating activity of a fungal laccase, suggesting that OSOXs can generate radical cation scavenging activity in the apoplast with a power proportional to the extent of degradation of plant cell wall, with possible implications for redox homeostasis and defense against oxidative stress.

plant biology↗

Berberine Bridge Enzyme-Like Oligosaccharide Oxidases Act As Enzymatic Transducers Between Microbial Glycoside Hydrolases And Plant Peroxidases

OG-oxidases (OGOXs) and CD-oxidase (CELLOX) are plant berberine bridge enzyme-like oligosaccharide oxidases that oxidize oligogalacturonides (OGs) and cellodextrins (CDs), cell wall fragments with nature of damage-associated molecular patterns (DAMPs). The oxidation of OGs and CDs attenuates their elicitor activity by concomitantly releasing H2O2. Here, 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 defence such as the oxidation of monolignol or a reaction possibly involved in a developmental event such as the oxidation of auxin (IAA), pointing to OGOX1 and CELLOX as enzymatic transducers between microbial glycoside hydrolases and plant PODs.

plant biology↗