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

被引:53
作者
Han, Xiaowei [1 ]
Altegoer, Florian [2 ,3 ]
Steinchen, Wieland [2 ,3 ]
Binnebesel, Lynn [2 ,3 ]
Schuhmacher, Jan [2 ,3 ,7 ]
Glatter, Timo [4 ]
Giammarinaro, Pietro I. [2 ,3 ]
Djamei, Armin [1 ,8 ]
Rensing, Stefan A. [5 ,6 ]
Reissmann, Stefanie [1 ]
Kahmann, Regine [1 ]
Bange, Gert [2 ,3 ]
机构
[1] Max Planck Inst Terr Microbiol, Dept Organism Interact, Marburg, Germany
[2] Philipps Univ Marburg, Ctr Synthet Microbiol SYNMIKRO, Marburg, Germany
[3] Dept Chem, Marburg, Germany
[4] Max Planck Inst Terr Microbiol, Facil Mass Spectrometry & Prote, Marburg, Germany
[5] Philipps Univ, Fac Biol, Marburg, Germany
[6] Univ Freiburg, BIOSS Ctr Biol Signalling Studies, Freiburg, Germany
[7] Max Planck Inst Mol Cell Biol & Genet, Dresden, Germany
[8] Austrian Acad Sci, GMI, Vienna Bioctr VBC, Vienna, Austria
关键词
MULTIPLE SEQUENCE ALIGNMENT; CHORISMATE MUTASE; USTILAGO-MAYDIS; ALLOSTERIC REGULATION; CRYSTAL-STRUCTURE; PROTEIN; GENES; MODEL; IDENTIFICATION; PRECURSOR;
D O I
10.1038/s41586-018-0857-9
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:650 / +
页数:21
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