Glycan recognition by a plant sentinel immune receptor
Jimenez-Sandoval, P.; Broyart, C.; Kentish, O.; Lee, H. K.; Culjak, K.; Osswald, U.; Aitouguinane, M.; Tettamanti, E.; Schmidli, M.; Zhang, L.; Roussin-Leveillee, C.; Berlanga, D. J.; Martin-Dacal, M.; Torres, M. A.; Kumar, V.; Fernandez-Calvo, P.; Jimenez-Gomez, J. M.; Macho, A. M.; Pfrengle, F.; Jorda, L.; Molina, A.; Santiago, J.
Show 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 multidomain receptor IGP1 in both apo form and bound to the cellulose-derived DAMP cellotriose. Structural analyses reveal that constitutive Leucine Rich Repeat-malectin interactions 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 acts as a cell wall sentinel that links pathogen-induced wall degradation to immune alerting, equipping plants to mount rapid and robust defense responses.
Matching journals
The top 2 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Molecular mechanism for the recognition of sequence-divergent CIF peptides by the plant receptor kinases GSO1/SGN3 and GSO2. 97%
- Structural basis for recognition of RALF peptides by LRX proteins during pollen tube growth 96%
- Structural mechanism for bi-directional actin crosslinking by T-plastin 95%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.