Skip to main content
ISMPMI Congress 2025 Main banner
Icon Legend
This session is not in your schedule.
This session is in your schedule. Click again to remove it.

Concurrent Session

Session: Concurrent Session: Plant Regulation of biotic and abiotic stress – trade-offs

R immune receptors as potential targets for engineering pathogen-resistant plants resilient to climate change

Thursday, July 17, 2025
10:50 - 11:00  
Location: Room P+Q

    Presenting Author(s)

  • MG

    Marta Grech-Baran

    PhD
    Institute of Biochemistry and Biophysics, Polish Academy of Sciences
    Warsaw, POLAND

    • Author(s)

  • JP

    Jaroslaw Poznanski

    Institute of Biochemistry and Biophysics, Polish Academy of Sciences
    Warsaw, Mazowieckie, Poland

  • KW

    Kamil Witek

    Group leader
    2Blades, The Sainsbury Laboratory
    Norwich, England, United Kingdom

  • HA

    Hee-Kyung Ahn

    Royal Society University Research Fellow
    University of Edinburgh
    EDINBURGH, Scotland, United Kingdom

  • JJ

    Jonathan D. G. Jones

    Prof. Group leader
    The Sainsbury Laboratory
    Norwich, England, United Kingdom

  • JH

    Jacek Hennig

    Institute of Biochemistry and Biophysics, Polish Academy of Science
    Warsaw, Mazowieckie, Poland

Abstract Text:

Climate change threatens agriculture and sustainable food security. Nucleotide-binding leucine-rich repeat (NLR) immune receptors sense pathogen effectors and activate defense. Elevated temperatures can disrupt NLR function, rendering many immune receptors ineffective. Currently, NLRs can only be confirmed as temperature-tolerant or temperature-sensitive experimentally; there are no established indicators to predict temperature stability.



Using structural modelling, we identified a feature in NLR architecture that enables us to predict them as temperature-sensitive or tolerant in silico. Our model suggests that proteins lacking stabilizations in the junction region between NB-ARC and LRR domains may fail to detect the pathogen at elevated temperature due to LRR disruption. Conversely, proteins with electrostatic stabilization in the junction are more temperature-tolerant. We altered the temperature stability of Rysto, Roq1, NRG1, and NRC immune receptors and assessed the functionality and oligomerization of the variants at various temperatures in transient assays. We also developed transgenic plants with receptor variants to evaluate their resistance under different temperature conditions.



Our results indicate that the structure of NLR receptors significantly affects their ability to activate immunity at elevated temperatures, and that their structures can be altered to modulate their temperature tolerance.