An activated wheat CCG10-NLR immune receptor forms an octameric resistosome

  • Published:
  • Authors: Guo G, Zhao H, Bai K, Lu J, Wu Q, Lu L, Zhang Y, Dong L, Li G, Chen Y, Hou Y, Lu P, Li M, Zhang H, Wang G, Zhu K, Huang B, Cui X, Fu H, Hu C, Chu Z, Lyu X, Kamoun S, Wang C, Liu Z, Selvaraj M, Jones JDG (2026)
  • Reference: https://doi.org/10.1016/j.cell.2026.02.024

Nucleotide-binding, leucine-rich repeat (NLR) receptors are widespread intracellular immune sensors across kingdoms. Plant G10-type coiled-coil (CCG10)-NLRs constitute a distinct phylogenetic clade that remains poorly characterized. Here, we identified a gain-of-function mutant of wheat autoimmunity 3 (WAI3GOF), which encodes a constitutively active CCG10-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 CCG10-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.

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