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

Han, X., Altegoer, F., Steinchen, W., Binnebesel, L., Schuhmacher, J., Glatter, T., et al. (2019). A kiwellin disarms the metabolic activity of a secreted fungal virulence factor. NATURE, 565(7741), 650-+. doi:10.1038/s41586-018-0857-9.

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Han, Xiaowei1, Autor           
Altegoer, Florian2, Autor
Steinchen, Wieland2, Autor
Binnebesel, Lynn1, Autor           
Schuhmacher, Jan3, Autor           
Glatter, Timo4, Autor           
Giammarinaro, Pietro I.2, Autor
Djamei, Armin1, Autor           
Rensing, Stefan A.2, Autor
Reissmann, Stefanie1, Autor           
Kahmann, Regine1, Autor           
Bange, Gert5, Autor           
Affiliations:
1Department of Organismic Interactions, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266313              
2external, ou_persistent22              
3Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society, ou_2340692              
4Core Facility Mass Spectrometry and Proteomics, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266266              
5External Organizations, ou_persistent22              

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 Zusammenfassung: 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 responses(1,2). The secreted
fungal chorismate mutase Cmu1 presumably affects biosynthesis of the
plant immune signal salicylic acid by channelling chorismate into the
phenylpropanoid pathway(3). 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.

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 Datum: 2019-01-31
 Publikationsstatus: Erschienen
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 Ort, Verlag, Ausgabe: -
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 Art der Begutachtung: -
 Identifikatoren: ISI: 000457404000049
DOI: 10.1038/s41586-018-0857-9
 Art des Abschluß: -

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Titel: NATURE
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 565 (7741) Artikelnummer: - Start- / Endseite: 650 - + Identifikator: ISSN: 0028-0836