2026年9月10日，瑞士洛桑大学Julia Santiago等科学家在《科学》（Science）发表研究，揭示了植物损伤感知免疫受体IGP1识别聚糖的机制。

病原体靶向并降解植物细胞周围的细胞外基质。一个核心问题是，细胞壁来源的损伤相关分子模式（DAMPs）如何被识别并整合以触发免疫反应。研究人员通过解析IGP1受体胞外多结构域在无配体形式以及与纤维素来源的DAMP纤维三糖结合状态下的结构，回答了这一问题。结构分析揭示，富含亮氨酸重复（LRR）-malectin结构域的组成性相互作用使IGP1预先构型以进行配体识别，并且该受体在LRR结构域中具有一个高度特异性的糖结合口袋，能够区分聚糖结构的细微变化。通过直接感知纤维寡糖，IGP1作为细胞壁监视受体发挥作用，将病原体诱导的细胞壁降解与免疫预警联系起来，使植物能够启动快速而稳健的防御反应。

附：英文原文

Title: Glycan recognition by a plant damage-sensing immune receptor

Author: Pedro Jiménez-Sandoval, Owen Kentish, Caroline Broyart, Hyun Kyung Lee, Klara Culjak, Uwe Osswald, Meriem Aitouguinane, Emanuele Tettamanti, Manon Schmidli, Lu Zhang, Louis-Philippe Maier, Charles Roussin-Léveillée, Diego José Berlanga, Marina Martin-Dacal, Miguel Angel Torres, Varun Kumar, Patricia Fernández-Calvo, José M. Jimenez-Gomez, Philippe Reymond, Alberto P. Macho, Fabian Pfrengle, Lucía Jordá, Antonio Molina, Julia Santiago

Issue&Volume: 2026-09-10

Abstract: Pathogens target and degrade the extracellular matrix surrounding plant cells. A central question is how cell wall-derived damage-associated molecular patterns (DAMPs) are recognized and integrated to trigger immune responses. We address this question by determining the structure of the extracellular multidomain of the IGP1 receptor in both apo form and bound to the cellulose-derived DAMP cellotriose. Structural analyses reveal that constitutive interactions of Leucine Rich Repeat (LRR)-malectin domains preconfigure IGP1 for ligand recognition and that the receptor features a highly specific sugar-binding pocket in the LRR domain capable of distinguishing fine variations in glycan structures. By directly sensing cello-oligomers, IGP1 operates as a cell wall surveillance receptor that links pathogen-induced wall degradation to immune alerting, equipping plants to mount rapid and robust defense responses.

DOI: 10.1126/science.aec6740

Source: https://www.science.org/doi/10.1126/science.aec6740