An activated wheat CC G10 -NLR immune receptor forms an octameric resistosome

作者：Guanghao Guo, He Zhao, Kaihong Bai, Qiuhong Wu, Lingli Dong, Lei Lu, Yongxing Chen, Yikun Hou, Jian Lü, Ping Lu, Miaomiao Li, Huaizhi Zhang, Gaojie Wang, Keyu Zhu, Baoge Huang, Xuejia Cui, H. Y. Fu, Chenchen Hu, Zhiying Chu, Xue Lv, Sophien Kamoun, Chao Wang, Zhiyong Liu, Muniyandi Selvaraj, Jonathan D. G. Jones · 发表于：bioRxiv (Cold Spring Harbor Laboratory) · 年份：2025 · DOI：10.1101/2025.08.26.672026 · 被引用次数：8 · 研究领域：Ubiquitin and proteasome pathways、Glycosylation and Glycoproteins Research、Galectins and Cancer Biology

SUMMARY Nucleotide-binding and leucine-rich repeat (LRR) receptors (NLRs) are widespread intracellular immune sensors across kingdoms. In plants, the G10-type coiled-coil (CC G10 )-NLRs form a distinct phylogenetic clade that remains poorly characterized. Here, we identified a gain-of-function (GOF) mutant of Wheat Autoimmunity 3 ( WAI3 ), designated WAI3 GOF , which encodes a constitutively activated CC G10 -NLR protein due to an amino acid substitution. Cryo-EM structural analysis revealed that activated WAI3 assembles into a distinctive octameric resistosome. Arabidopsis RPS2, another CC G10 -NLR, also forms an octamer, indicating a conserved structural property across monocot and dicot plants. The WAI3 resistosome mediates a prolonged and sustained increase in cytosolic calcium influx, facilitated by a unique channel architecture arising from its divergent CC domain configuration. Notably, this domain arrangement may be shared by many plant NLRs that lack the conserved EDVID motif in their CC domains. Our findings uncover a previously uncharacterized resistosome structure and provide insights into plant immune receptor plasticity.