AI Article Synopsis

  • Oligosaccharide fragments from plant cell walls activate immunity and can negatively influence growth and development, highlighting the importance of their balance in the growth-defense trade-off.
  • A newly discovered mechanism involving berberine bridge enzyme-like (BBE-like) proteins can control this balance by oxidizing two major DAMPs, oligogalacturonides (OGs) and cellodextrins (CDs), thereby inactivating their immune-stimulating properties.
  • The findings suggest that oxidation may be a broader strategy for plants to maintain homeostasis of DAMPs and open up avenues for discovering similar regulatory mechanisms in plants and animals.

Article Abstract

Several oligosaccharide fragments derived from plant cell walls activate plant immunity and behave as typical damage-associated molecular patterns (DAMPs). Some of them also behave as negative regulators of growth and development, and due to their antithetic effect on immunity and growth, their concentrations, activity, time of formation, and localization is critical for the so-called "growth-defense trade-off." Moreover, like in animals, over accumulation of DAMPs in plants provokes deleterious physiological effects and may cause hyper-immunity if the cellular mechanisms controlling their homeostasis fail. Recently, a mechanism has been discovered that controls the activity of two well-known plant DAMPs, oligogalacturonides (OGs), released upon hydrolysis of homogalacturonan (HG), and cellodextrins (CDs), products of cellulose breakdown. The potential homeostatic mechanism involves specific oxidases belonging to the family of berberine bridge enzyme-like (BBE-like) proteins. Oxidation of OGs and CDs not only inactivates their DAMP activity, but also makes them a significantly less desirable food source for microbial pathogens. The evidence that oxidation and inactivation of OGs and CDs may be a general strategy of plants for controlling the homeostasis of DAMPs is discussed. The possibility exists of discovering additional oxidative and/or inactivating enzymes targeting other DAMP molecules both in the plant and in animal kingdoms.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7773757PMC
http://dx.doi.org/10.3389/fpls.2020.613259DOI Listing

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