A fungal monooxygenase-derived jasmonate attenuates host innate immunity.

Nat Chem Biol

1] Temasek Life Sciences Laboratory, Singapore. [2] Department of Biological Sciences, National University of Singapore, Singapore. [3] School of Biological Sciences, Nanyang Technological University, Singapore.

Published: September 2015

AI Article Synopsis

  • Distinct modifications of jasmonic acid (JA) regulate plant growth and immunity, with hydroxylated JA (12OH-JA) promoting certain plant developments while inhibiting defense mechanisms.
  • The study identifies an enzyme, antibiotic biosynthesis monooxygenase (Abm), that converts JA into 12OH-JA in the rice blast fungus, aiding the fungus in evading plant defenses upon invasion.
  • Loss of Abm in the fungus results in increased plant defense responses, while 12OH-JA can dampen these responses, highlighting the dynamic interaction between plants and pathogens and revealing potential antifungal targets.

Article Abstract

Distinct modifications fine-tune the activity of jasmonic acid (JA) in regulating plant growth and immunity. Hydroxylated JA (12OH-JA) promotes flower and tuber development but prevents induction of JA signaling, plant defense or both. However, biosynthesis of 12OH-JA has remained elusive. We report here an antibiotic biosynthesis monooxygenase (Abm) that converts endogenous free JA into 12OH-JA in the model rice blast fungus Magnaporthe oryzae. Such fungal 12OH-JA is secreted during host penetration and helps evade the defense response. Loss of Abm in M. oryzae led to accumulation of methyl JA (MeJA), which induces host defense and blocks invasive growth. Exogenously added 12OH-JA markedly attenuated abmΔ-induced immunity in rice. Notably, Abm itself is secreted after invasion and most likely converts plant JA into 12OH-JA to facilitate host colonization. This study sheds light on the chemical arms race during plant-pathogen interaction, reveals Abm as an antifungal target and outlines a synthetic strategy for transformation of a versatile small-molecule phytohormone.

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http://dx.doi.org/10.1038/nchembio.1885DOI Listing

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