A wheat resistosome defines common principles of immune receptor channels

Alexander Förderer, Ertong Li, Aaron W. Lawson, Ya-nan Deng, Yue Sun, Elke Logemann, Xiaoxiao Zhang, Jie Wen, Zhifu Han, Junbiao Chang, Yuhang Chen (), Paul Schulze-Lefert () and Jijie Chai ()
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Alexander Förderer: University of Cologne
Ertong Li: University of Cologne
Aaron W. Lawson: Max Planck Institute for Plant Breeding Research
Ya-nan Deng: State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China; Innovative Academy of Seed Design, Chinese Academy of Sciences
Yue Sun: Tsinghua University
Elke Logemann: Max Planck Institute for Plant Breeding Research
Xiaoxiao Zhang: Tsinghua University
Jie Wen: Tsinghua University
Zhifu Han: Tsinghua University
Junbiao Chang: Henan Normal University, School of Pharmaceutical Sciences, Zhengzhou University
Yuhang Chen: State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China; Innovative Academy of Seed Design, Chinese Academy of Sciences
Paul Schulze-Lefert: Max Planck Institute for Plant Breeding Research
Jijie Chai: University of Cologne

Nature, 2022, vol. 610, issue 7932, 532-539

Abstract: Abstract Plant intracellular nucleotide-binding leucine-rich repeat receptors (NLRs) detect pathogen effectors to trigger immune responses1. Indirect recognition of a pathogen effector by the dicotyledonous Arabidopsis thaliana coiled-coil domain containing NLR (CNL) ZAR1 induces the formation of a large hetero-oligomeric protein complex, termed the ZAR1 resistosome, which functions as a calcium channel required for ZAR1-mediated immunity2–4. Whether the resistosome and channel activities are conserved among plant CNLs remains unknown. Here we report the cryo-electron microscopy structure of the wheat CNL Sr355 in complex with the effector AvrSr356 of the wheat stem rust pathogen. Direct effector binding to the leucine-rich repeats of Sr35 results in the formation of a pentameric Sr35–AvrSr35 complex, which we term the Sr35 resistosome. Wheat Sr35 and Arabidopsis ZAR1 resistosomes bear striking structural similarities, including an arginine cluster in the leucine-rich repeats domain not previously recognized as conserved, which co-occurs and forms intramolecular interactions with the 'EDVID' motif in the coiled-coil domain. Electrophysiological measurements show that the Sr35 resistosome exhibits non-selective cation channel activity. These structural insights allowed us to generate new variants of closely related wheat and barley orphan NLRs that recognize AvrSr35. Our data support the evolutionary conservation of CNL resistosomes in plants and demonstrate proof of principle for structure-based engineering of NLRs for crop improvement.

Date: 2022
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DOI: 10.1038/s41586-022-05231-w

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