Activation of plant immunity through conversion of a helper NLR homodimer into a resistosome

Nucleotide-binding domain and leucine-rich repeat (NLR) proteins can engage in complex interactions to detect pathogens and execute a robust immune response via downstream helper NLRs. However, the biochemical mechanisms of helper NLR activation by upstream sensor NLRs remain poorly understood. Here, we show that the coiled-coil helper NLR NRC2 from Nicotiana benthamiana accumulates in vivo as a homodimer that converts into a higher-order oligomer upon activation by its upstream virus disease resistance protein Rx. The cryo-EM structure of NbNRC2 in its resting state revealed intermolecular interactions that mediate homodimer formation and contribute to immune receptor autoinhibition. These dimerization interfaces have diverged between paralogous NRC proteins to insulate critical network nodes and enable redundant immune pathways, possibly to minimise undesired cross-activation and evade pathogen suppression of immunity. Our results expand the molecular mechanisms of NLR activation pointing to transition from homodimers to higher-order oligomeric resistosomes.

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Publication Details

Journal
PLoS Biology
Published
2024-10-18
DOI
https://doi.org/10.1371/journal.pbio.3002868
Citations
37
Primary Topic
Plant-Microbe Interactions and Immunity
Type
article
Field-Weighted Citation Impact
22.19

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article

Activation of plant immunity through conversion of a helper NLR homodimer into a resistosome

Tarhan Ibrahim, Benjamin Pêtre, Abbas Maqbool, Tolga O. Bozkurt et al.
37 citations
PLoS Biology
Plant-Microbe Interactions and Immunity
22.19
article

Activation of plant immunity through conversion of a helper NLR homodimer into a resistosome

Tarhan Ibrahim, Benjamin Pêtre, Abbas Maqbool, Tolga O. Bozkurt, Lida Derevnina, Sophien Kamoun, AmirAli Toghani, Hsuan Pai, Rongrong Xie, Mark J. Banfield, David M. Lawson, Juan Carlos De la Concepción, Jiorgos Kourelis, Enoch Lok Him Yuen, Chih‐Hang Wu, Yu Sugihara, Mauricio P. Contreras, Muniyandi Selvaraj, He Zhao
article en
37 citations

Abstract

Nucleotide-binding domain and leucine-rich repeat (NLR) proteins can engage in complex interactions to detect pathogens and execute a robust immune response via downstream helper NLRs. However, the biochemical mechanisms of helper NLR activation by upstream sensor NLRs remain poorly understood. Here, we show that the coiled-coil helper NLR NRC2 from Nicotiana benthamiana accumulates in vivo as a homodimer that converts into a higher-order oligomer upon activation by its upstream virus disease resistance protein Rx. The cryo-EM structure of NbNRC2 in its resting state revealed intermolecular interactions that mediate homodimer formation and contribute to immune receptor autoinhibition. These dimerization interfaces have diverged between paralogous NRC proteins to insulate critical network nodes and enable redundant immune pathways, possibly to minimise undesired cross-activation and evade pathogen suppression of immunity. Our results expand the molecular mechanisms of NLR activation pointing to transition from homodimers to higher-order oligomeric resistosomes.

PLoS BiologyVol. 22(10)
John Innes Centre (GB), University of East Anglia (GB), Norwich Research Park (GB), Sainsbury Laboratory (GB), Imperial College London (GB)
Wellcome Trust, Gatsby Charitable Foundation, Academia Sinica, John Innes Foundation, National Science and Technology Council, Directorate for Biological Sciences, Biotechnology and Biological Sciences Research Council, Birkbeck, University of London, Agricultural Biotechnology Research Center, Academia Sinica, HORIZON EUROPE European Research Council
Openalex Percentile: Top 0%
Plant-Microbe Interactions and Immunity
22.19
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