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A saponin-detoxifying enzyme mediates suppression of plant defences

Author

Listed:
  • K. Bouarab

    (Sainsbury Laboratory, John Innes Centre)

  • R. Melton

    (Sainsbury Laboratory, John Innes Centre)

  • J. Peart

    (Sainsbury Laboratory, John Innes Centre)

  • D. Baulcombe

    (Sainsbury Laboratory, John Innes Centre)

  • A. Osbourn

    (Sainsbury Laboratory, John Innes Centre)

Abstract

Plant disease resistance can be conferred by constitutive features such as structural barriers or preformed antimicrobial secondary metabolites. Additional defence mechanisms are activated in response to pathogen attack and include localized cell death (the hypersensitive response)1,2. Pathogens use different strategies to counter constitutive and induced plant defences, including degradation of preformed antimicrobial compounds3 and the production of molecules that suppress induced plant defences4,5,6. Here we present evidence for a two-component process in which a fungal pathogen subverts the preformed antimicrobial compounds of its host and uses them to interfere with induced defence responses. Antimicrobial saponins are first hydrolysed by a fungal saponin-detoxifying enzyme. The degradation product of this hydrolysis then suppresses induced defence responses by interfering with fundamental signal transduction processes leading to disease resistance.

Suggested Citation

  • K. Bouarab & R. Melton & J. Peart & D. Baulcombe & A. Osbourn, 2002. "A saponin-detoxifying enzyme mediates suppression of plant defences," Nature, Nature, vol. 418(6900), pages 889-892, August.
    • Handle: RePEc:nat:nature:v:418:y:2002:i:6900:d:10.1038_nature00950
    DOI: 10.1038/nature00950
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    Cited by:

    1. Yaohua You & H. M. Suraj & Linda Matz & A. Lorena Herrera Valderrama & Paul Ruigrok & Xiaoqian Shi-Kunne & Frank P. J. Pieterse & Anne Oostlander & Henriek G. Beenen & Edgar A. Chavarro-Carrero & Si Q, 2024. "Botrytis cinerea combines four molecular strategies to tolerate membrane-permeating plant compounds and to increase virulence," Nature Communications, Nature, vol. 15(1), pages 1-17, December.

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