A kiwellin disarms the metabolic activity of a secreted fungal virulence factor
| Autor: | Gert Bange, Pietro Ivan Giammarinaro, Stefanie Reissmann, Xiaowei Han, Timo Glatter, Regine Kahmann, Armin Djamei, Florian Altegoer, Lynn Binnebesel, Stefan A. Rensing, Wieland Steinchen, J.S. Schuhmacher |
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| Rok vydání: | 2019 |
| Předmět: |
Models
Molecular 0106 biological sciences Virulence Factors Ustilago Chorismic Acid Virulence Zea mays 01 natural sciences Virulence factor Microbiology 03 medical and health sciences Pathogen Phylogeny Plant Diseases 030304 developmental biology 0303 health sciences Multidisciplinary Phenylpropanoid biology Effector fungi food and beverages Antigens Plant biology.organism_classification Plant protein Chorismate mutase Salicylic Acid Chorismate Mutase 010606 plant biology & botany |
| Zdroj: | Nature. 565:650-653 |
| ISSN: | 1476-4687 0028-0836 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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