Glycan recognition by a plant damage-sensing immune receptor

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.

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Publication Details

Journal
Science
Published
2026-09-10
DOI
https://doi.org/10.1126/science.aec6740
Primary Topic
Polysaccharides and Plant Cell Walls
Type
article
Field-Weighted Citation Impact
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article

Glycan recognition by a plant damage-sensing immune receptor

Marina Martín‐Dacal, Charles Roussin‐Léveillée, Julia Santiago, Pedro Jiménez‐Sandoval et al.
Science
Polysaccharides and Plant Cell Walls
article

Glycan recognition by a plant damage-sensing immune receptor

Marina Martín‐Dacal, Charles Roussin‐Léveillée, Julia Santiago, Pedro Jiménez‐Sandoval, Philippe Reymond, Fabian Pfrengle, Antonio Molina, Diego José Berlanga, Lucía Jordá, Patricia Fernández‐Calvo, Uwe Osswald, Caroline Broyart, José M. Jiménez‐Gómez, Klara Čuljak, Miguel Ángel Medina Torres, Meriem Aitouguinane, Alberto P. Macho, Louis-Philippe Maier, Hyun Kyung Lee, Varun Kumar, Lu Zhang, Owen Kentish, Emanuele Tettamanti, Manon Schmidli
article en

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.

Science
Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (ES), Center for Excellence in Molecular Plant Sciences (CN), Universidad Politécnica de Madrid (ES), BOKU University (AT), University of Lausanne (CH)
Openalex Percentile: Top 12%
Polysaccharides and Plant Cell Walls
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