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

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...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2020-12, Vol.370 (6521)
Main Authors: Martin, Raoul, Qi, Tiancong, Zhang, Haibo, Liu, Furong, King, Miles, Toth, Claire, Nogales, Eva, Staskawicz, Brian J
Format: Article
Language:English
Subjects:
Adenine
Adenosine
Adenosine diphosphate
Adenosine triphosphate
Animal diseases
Animals
Antibodies
Antigens
Apaf-1 protein
Apoptosis
ATP
Bacterial Proteins - chemistry
Binding
Calcium influx
Calcium ions
Cell activation
Cell death
Coils
Cryoelectron Microscopy
Cytokines
Dimers
Disease Resistance
Domains
Effectors
Electron microscopy
Exposure
Host-Pathogen Interactions
Hydrolase
Immune response
Immunoglobulins
Interfaces
Interleukin 1
Intracellular
Leucine
Microscopy
Mortality
NAD
Nicotiana - immunology
Nicotiana - microbiology
Nicotiana benthamiana
NLR Proteins - chemistry
Nucleotides
Oligomerization
Pathogens
Plant bacterial diseases
Plant diseases
Plant Diseases - immunology
Plant Proteins - chemistry
Protein Binding
Protein Domains
Protein Multimerization
Proteins
Proteomes
Recognition
Residues
Ribose
Sandwich structures
Substrate specificity
Substrates
Xanthomonas
Xanthomonas - pathogenicity
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Summary: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 with a Toll-like interleukin-1 receptor (TIR) domain bound to the effector XopQ ( 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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.abd9993