Study reveals how plant immune receptor LORE recognizes bacterial fatty acid signals
Researchers used structural analysis and molecular simulations to determine how the plant immune receptor LORE binds medium-chain 3-hydroxy fatty acids from bacteria. The binding occurs in a hydrophobic pocket within the lectin 2 domain, with a flexible loop acting as a dynamic gate that controls access and stabilizes the ligand. This mechanism explains how plants detect bacterial pathogens and activate immune responses.
Scientists studying the Arabidopsis thaliana plant immune receptor LORE identified the molecular mechanism by which it recognizes bacterial medium-chain 3-hydroxy fatty acids (mc-3-OH-FAs) as danger signals. Using protein structure prediction, molecular dynamics simulations, and experimental binding assays, the team mapped the ligand-binding site to a hydrophobic pocket in the lectin 2 domain. A flexible loop within this domain functions as a dynamic gate, first allowing the fatty acid's acyl tail to enter the pocket, then using polar interactions to stabilize the bound state and trigger signaling. The researchers also discovered that modified fatty acids with bulky headgroups can bind the pocket but act as antagonists by preventing the loop from adopting its active conformation. These findings provide a detailed mechanistic framework for how plants sense and respond to bacterial pathogens at the molecular level.
Limitations & open questions
The study does not discuss potential applications of these findings for crop improvement or disease resistance breeding, nor does it address whether similar binding mechanisms exist in other plant immune receptors.
What different sources said
- bioRxivCenter
The plant immune receptor LORE binds agonistic and antagonistic 3-hydroxy fatty acid ligands via a dynamic loop in its G-type lectin domain
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