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TitleAn activated wheat CC-NLR immune receptor forms an octameric resistosome.
Journal, issue, pagesCell, Year 2026
Publish dateMar 20, 2026
AuthorsGuanghao Guo / He Zhao / Kaihong Bai / Jian Lu / Qiuhong Wu / Lei Lu / Yue Zhang / Lingli Dong / Guangwei Li / Yongxing Chen / Yikun Hou / Ping Lu / Miaomiao Li / Huaizhi Zhang / Gaojie Wang / Keyu Zhu / Baoge Huang / Xuejia Cui / Hongkui Fu / Chenchen Hu / Zhiying Chu / Xue Lyu / Sophien Kamoun / Chao Wang / Zhiyong Liu / Muniyandi Selvaraj / Jonathan D G Jones /
PubMed AbstractNucleotide-binding, leucine-rich repeat (NLR) receptors are widespread intracellular immune sensors across kingdoms. Plant G10-type coiled-coil (CC)-NLRs constitute a distinct phylogenetic clade that ...Nucleotide-binding, leucine-rich repeat (NLR) receptors are widespread intracellular immune sensors across kingdoms. Plant G10-type coiled-coil (CC)-NLRs constitute a distinct phylogenetic clade that remains poorly characterized. Here, we identified a gain-of-function mutant of wheat autoimmunity 3 (WAI3), which encodes a constitutively active CC-NLR resulting from a residue substitution in the leucine-rich repeat (LRR) domain. Cryo-electron microscopy (cryo-EM) analysis reveals that activated WAI3 assembles into a distinctive octameric resistosome. Arabidopsis RPS2, another CC-NLR, also forms an octamer, indicating a conserved structural property across monocot and dicot plants. The WAI3 resistosome induces a prolonged and sustained increase in cytosolic calcium, likely facilitated by a unique channel architecture arising from its divergent coiled-coil (CC) domain configuration. Notably, this domain arrangement may be shared by plant NLRs that lack the conserved EDVID (Glu-Asp-Val-Ile-Asp) motif in their CC domains. Together, our findings uncover a conserved yet previously uncharacterized NLR resistosome structure and provide insights into the plant immune receptor plasticity.
External linksCell / PubMed:41864205
MethodsEM (single particle)
Resolution3.6 - 4.6 Å
Structure data

51810

9h2l

EMDB-51810, PDB-9h2l:
Cryo-EM structure of an octameric G10-resistosome from wheat
Method: EM (single particle) / Resolution: 3.95 Å

51852

9h4i

EMDB-51852, PDB-9h4i:
Cryo-EM structure of an octameric G10-resistosome from wheat (N-to-N arrangement)
Method: EM (single particle) / Resolution: 4.6 Å

51910

9h73

EMDB-51910, PDB-9h73:
Cryo-EM structure of an octameric G10-resistosome from wheat in 'back-to-back' arrangement
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Source
  • triticum aestivum (bread wheat)
KeywordsPLANT PROTEIN / G10-NLR / Octamer / Resistance / LRR / Wheat / resistosome

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