bioRxiv · 10.64898/2025.12.17.694812
Structural basis for heat tolerance in plant NLR immune receptors.
Abstract
Nucleotide-binding leucine-rich repeat (NLR) immune receptors sense pathogen molecules and oligomerize, initiating defense signaling. Some NLRs function poorly at elevated temperatures for unknown reasons. We show that temperature-sensitive NLRs retain ligand binding at elevated temperatures but are impaired in oligomerization. We identify key residues involved in temperature resilience. Structural modeling reveals stabilizing intramolecular interactions of the NB-ARC domain with surface residues of the adjacent leucine-rich repeat (LRR) that preserve receptor integrity and functionality under heat stress. These insights enable in silico classification of NLRs as temperature-sensitive or -tolerant and underpin design of temperature tolerant variants of temperature sensitive NLRs. These findings provide a mechanistic basis for temperature sensitivity in plant immune receptors and enable engineering of temperature-tolerant disease resistance in crops.
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Grech-Baran, M., Witek, K., Ahn, H.-K., Lichocka, M., Vargas-Cortez, T., Barymow-Filoniuk, I., Witek, A. I., Hennig, J., Jones, J. D., Poznanski, J. T.. 2025-12-17. Structural basis for heat tolerance in plant NLR immune receptors.. https://doi.org/10.64898/2025.12.17.694812
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