Chinese Academy of Sciences identifies first octameric resistosome in wheat, uncovering a unique plant immune mechanism

A team led by the Chinese Academy of Sciences reveals the first eight-unit resistosome in plants, identifying a conserved immune mechanism in wheat and Arabidopsis.

By: AXL Media

Published: Mar 21, 2026, 6:02 AM EDT

Source: Information for this report was sourced from Chinese Academy of Sciences Headquarters

The Cellular Autonomy of Plant Immunity

Unlike the centralized immune systems found in animals, plant immunity is initiated at the individual cellular level. Each cell is equipped with intracellular receptors known as nucleotide-binding, leucine-rich repeat (NLR) receptors, which detect pathogen effector proteins injected into the host. These NLRs are categorized into two primary classes—Toll/interleukin-1 receptor-like (TIR) or coiled-coil (CC) NLRs—depending on their N-terminal structure. Once activated, these receptors form multi-protein complexes called resistosomes that orchestrate the plant's defensive response.

Breaking the Pentameric and Hexameric Mold

Prior to this study, scientists had identified resistosomes that formed as pentamers (five units) or hexamers (six units). These complexes typically initiate immune responses by triggering a calcium (Ca2+) influx into the cytoplasm. However, the activation mechanism of the CCG10-NLR clade remained poorly understood. A collaborative team led by Professor Liu Zhiyong of the Institute of Genetics and Developmental Biology has now identified an octameric (eight-unit) resistosome, representing a previously unknown assembly mechanism in plant biology.

The Role of the Wheat Autoimmunity 3 Gene

The discovery originated from the study of a specific wheat mutant, "Zhongke 331," which exhibited a spontaneous immune response that hindered its own growth. Through map-based cloning, the researchers identified the Wheat Autoimmunity 3 (WAI3) gene, which encodes a CCG10-NLR protein. A single gain-of-function mutation in this gene's leucine-rich repeat domain caused it to auto-activate, providing a unique opportunity for the team to freeze the protein in its active state and examine its structure using cryo-electron microscopy.