Structure of the activated ROQ1 resistosome directly recognizing the pathogen effector XopQ.

Abstract

Plants and animals detect pathogen infection using intracellular nucleotide-binding leucine-rich repeat receptors (NLRs) that directly or indirectly recognize pathogen effectors and activate an immune response. How effector sensing triggers NLR activation remains poorly understood. Here we describe the 3.8-angstrom-resolution cryo-electron microscopy structure of the activated ROQ1 (recognition of XopQ 1), an NLR native to <i>Nicotiana benthamiana</i> with a Toll-like interleukin-1 receptor (TIR) domain bound to the <i>Xanthomonas</i> <i>euvesicatoria</i> effector XopQ (<i>Xanthomonas</i> outer protein Q). ROQ1 directly binds to both the predicted active site and surface residues of XopQ while forming a tetrameric resistosome that brings together the TIR domains for downstream immune signaling. Our results suggest a mechanism for the direct recognition of effectors by NLRs leading to the oligomerization-dependent activation of a plant resistosome and signaling by the TIR domain.