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A kiwellin disarms the metabolic activity of a secreted fungal virulence factor

Author

Listed:
  • Xiaowei Han

    (Max Planck Institute for Terrestrial Microbiology)

  • Florian Altegoer

    (Philipps-University Marburg, Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry)

  • Wieland Steinchen

    (Philipps-University Marburg, Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry)

  • Lynn Binnebesel

    (Philipps-University Marburg, Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry)

  • Jan Schuhmacher

    (Philipps-University Marburg, Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry
    Max Planck Institute of Molecular Cell Biology and Genetics)

  • Timo Glatter

    (Max Planck Institute for Terrestrial Microbiology)

  • Pietro I. Giammarinaro

    (Philipps-University Marburg, Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry)

  • Armin Djamei

    (Max Planck Institute for Terrestrial Microbiology
    Gregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna Biocenter (VBC))

  • Stefan A. Rensing

    (Philipps-University
    University of Freiburg)

  • Stefanie Reissmann

    (Max Planck Institute for Terrestrial Microbiology)

  • Regine Kahmann

    (Max Planck Institute for Terrestrial Microbiology)

  • Gert Bange

    (Philipps-University Marburg, Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry)

Abstract

Fungi-induced plant diseases affect global food security and plant ecology. The biotrophic fungus Ustilago maydis causes smut disease in maize (Zea mays) plants by secreting numerous virulence effectors that reprogram plant metabolism and immune responses1,2. The secreted fungal chorismate mutase Cmu1 presumably affects biosynthesis of the plant immune signal salicylic acid by channelling chorismate into the phenylpropanoid pathway3. Here we show that one of the 20 maize-encoded kiwellins (ZmKWL1) specifically blocks the catalytic activity of Cmu1. ZmKWL1 hinders substrate access to the active site of Cmu1 through intimate interactions involving structural features that are specific to fungal Cmu1 orthologues. Phylogenetic analysis suggests that plant kiwellins have a versatile scaffold that can specifically counteract pathogen effectors such as Cmu1. We reveal the biological activity of a member of the kiwellin family, a widely conserved group of proteins that have previously been recognized only as important human allergens.

Suggested Citation

  • Xiaowei Han & Florian Altegoer & Wieland Steinchen & Lynn Binnebesel & Jan Schuhmacher & Timo Glatter & Pietro I. Giammarinaro & Armin Djamei & Stefan A. Rensing & Stefanie Reissmann & Regine Kahmann , 2019. "A kiwellin disarms the metabolic activity of a secreted fungal virulence factor," Nature, Nature, vol. 565(7741), pages 650-653, January.
    • Handle: RePEc:nat:nature:v:565:y:2019:i:7741:d:10.1038_s41586-018-0857-9
    DOI: 10.1038/s41586-018-0857-9
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