植物依赖NLR (nucleotide-binding, leucine-rich repeat)免疫受体识别病原菌分泌的效应蛋白来激活免疫反应。近年来，科学家们已相继解析了多种NLR“抗病小体(resistosome)”的结构，但对于进化上古老且广泛存在的CC_G10-NLR免疫受体的作用机制始终未知。为探究这一科学问题，中国科学院遗传与发育生物学研究所刘志勇团队联合国内外多个团队鉴定出编码CC_G10-NLR蛋白的小麦自发免疫基因WAI3 (wheat autoimmunity 3)，并利用冷冻电镜技术首次揭示了其激活后形成八聚体抗病小体结构，并诱导持续的钙离子(Ca²⁺)内流，进而激活下游免疫反应。拟南芥中的CC_G10-NLR同源蛋白RPS2同样能够形成八聚体且引发Ca²⁺内流，表明该作用机制在单子叶与双子叶植物中高度保守。此外，WAI3抗病小体具有独特的CC (coiled-coil)结构域构象，这一特征可能与CC_G10-NLR的CC结构域缺少EDVID (Glu-Asp-Val-Ile-Asp)基序相关。该研究首次揭示了植物CC_G10-NLR蛋白的抗病小体组装及免疫信号传导的新机制，拓展了人们对植物免疫受体多样性与可塑性的认知。

Plants rely on nucleotide-binding, leucine-rich repeat (NLR) receptors to recognize effector proteins, activating immune responses. In recent years, researchers have elucidated the structures of various plant NLR resistosomes. However, the activation mechanism of the evolutionarily ancient and widely distributed CC_G10-NLR phylogenetic clade has remained elusive. To investigate this scientific question, the research group led by Zhiyong Liu from Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, in collaboration with multiple research groups, identified the wheat spontaneous immunity gene wheat autoimmunity 3 (WAI3), which encodes a CC_G10-NLR protein. Cryo-electron microscopy (cryo-EM) analysis reveals that that activated WAI3 assembles into a distinctive octameric resistosome, which triggers sustained calcium influx. The homologous CC_G10-NLR protein RPS2 in Arabidopsis was also shown to form an octamer and induce calcium influx, indicating that this mechanism is conserved in both monocot and dicot plants. Furthermore, the WAI3 resistosome exhibits a unique conformation of the coiled-coil (CC) domain, which may be associated with the absence of the EDVID (Glu-Asp-Val-Ile-Asp) motif in the CC domain of CC_G10-NLRs. This study reveals a novel mechanism of resistosome assembly and immune signal transduction in plant CC_G10-NLR proteins, broadening the understanding of the diversity and plasticity of plant immune receptors.