A platform for identifying structural rewiring in immunometabolism-associated proteins

To defend themselves against invading microbes, plants rely on either a pathogen-associated molecular pattern (PAMP)-triggered system or an effector-triggered system. The latter is mainly mediated by the class of intracellular nucleotide-binding leucine-rich repeat (NLR) receptors, which can be divided into two groups that differ in their N-terminal structural element. CC-NLRs are characterized by an N-terminal coiled-coil element and are thought to act by assembling into ion channels upon activation. In contrast, TIR-NLRs are characterized by an N-terminal Toll/interleukin-1 receptor domain and act as either NADases and/or synthetases of cNMP derivatives. For both groups, structural biology tools have provided important insights into the mechanisms of activation and activity of these cornerstone proteins of plant immunometabolism. Using cryo-electron microscopy, we aim to support other i-HEAD projects in their quest to unravel the mechanisms of plant immunometabolism and to better understand the molecular components that allow plants to differentiate between beneficial and detrimental microbial interactions.

Researchers