Yeast surface display reveals structure-dependent β-glucan association with the plant immune receptor AtIGP1

Arabidopsis thaliana AtIGP1 extracellular domain shows a specific, competitively displaceable association with MLG-derived DP2 laminaribiose (G3G), not with DP3 or DP4 structures.

• Why it matters: Direct recognition of MLG-derived oligosaccharides by AtIGP1 is unclear, limiting understanding of which glycan structures trigger AtIGP1-linked pattern-triggered immunity.
• What they did: A Saccharomyces cerevisiae surface-display system presented the AtIGP1 extracellular domain to test binding to fluorescent MLG oligosaccharides across DP2, DP3, and DP4, then validated relevance by treating A. thaliana seedlings with unlabeled MLG DP2.
• The result: MLG DP2 induced a cytosolic Ca2+ response in seedlings that was markedly reduced in the igp1-3 mutant, supporting laminaribiose as an additional AtIGP1 candidate ligand.

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