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Induced proximity of a TIR signaling domain on a plant-mammalian NLR chimera activates defense in plants

Duxbury, Zane and Wang, Shanshan and MacKenzie, Craig and Tenthorey, Jeannette L. and Zhang, Xiaoxiao and Huh, Sung Un and Hu, Lanxi and Hill, Lionel and Ngou, Pok N. and Ding, Pingtao and Chen, Jian and Ma, Yan and Guo, Hailong and Castel, Baptiste and Moschou, Panagiotis Nikolaou and Bernoux, Maud and Dodds, Peter N. and Vance, Russell E. and Jones, Jonathan D. G. (2020). Induced proximity of a TIR signaling domain on a plant-mammalian NLR chimera activates defense in plants. Proceedings of the National Academy of Sciences of the United States of America. 117 , 18832-18839
[Research article]

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Abstract

Plant and animal intracellular nucleotide-binding, leucine-rich repeat (NLR) immune receptors detect pathogen-derived molecules and activate defense. Plant NLRs can be divided into several classes based upon their N-terminal signaling domains, including TIR (Toll-like, Interleukin-1 receptor, Resistance protein)- and CC (coiled-coil)-NLRs. Upon ligand detection, mammalian NAIP and NLRC4 NLRs oligomerize, forming an inflammasome that induces proximity of its N-terminal signaling domains. Recently, a plant CC-NLR was revealed to form an inflammasome-like hetero-oligomer. To further investigate plant NLR signaling mechanisms, we fused the N-terminal TIR domain of several plant NLRs to the N terminus of NLRC4. Inflammasome-dependent induced proximity of the TIR domain in planta initiated defense signaling. Thus, induced proximity of a plant TIR domain imposed by oligomerization of a mammalian inflammasome is sufficient to activate authentic plant defense. Ligand detection and inflammasome formation is maintained when the known components of the NLRC4 inflammasome is transferred across kingdoms, indicating that NLRC4 complex can robustly function without any additional mammalian proteins. Additionally, we found NADase activity of a plant TIR domain is necessary for plant defense activation, but NADase activity of a mammalian or a bacterial TIR is not sufficient to activate defense in plants.

Authors/Creators:Duxbury, Zane and Wang, Shanshan and MacKenzie, Craig and Tenthorey, Jeannette L. and Zhang, Xiaoxiao and Huh, Sung Un and Hu, Lanxi and Hill, Lionel and Ngou, Pok N. and Ding, Pingtao and Chen, Jian and Ma, Yan and Guo, Hailong and Castel, Baptiste and Moschou, Panagiotis Nikolaou and Bernoux, Maud and Dodds, Peter N. and Vance, Russell E. and Jones, Jonathan D. G.
Title:Induced proximity of a TIR signaling domain on a plant-mammalian NLR chimera activates defense in plants
Series Name/Journal:Proceedings of the National Academy of Sciences of the United States of America
Year of publishing :2020
Volume:117
Page range:18832-18839
Number of Pages:8
Publisher:NATL ACAD SCIENCES
ISSN:0027-8424
Language:English
Publication Type:Research article
Article category:Scientific peer reviewed
Version:Published version
Copyright:Creative Commons: Attribution 4.0
Full Text Status:Public
Subjects:(A) Swedish standard research categories 2011 > 1 Natural sciences > 106 Biological Sciences (Medical to be 3 and Agricultural to be 4) > Immunology (Immunology in the medical area to be 30110)
Keywords:NLR immune receptors, plant immunity, inflammasome, effector-triggered, immunity
URN:NBN:urn:nbn:se:slu:epsilon-p-108297
Permanent URL:
http://urn.kb.se/resolve?urn=urn:nbn:se:slu:epsilon-p-108297
Additional ID:
Type of IDID
DOI10.1073/pnas.2001185117
Web of Science (WoS)000575493200004
ID Code:18742
Faculty:NJ - Fakulteten för naturresurser och jordbruksvetenskap
Department:(NL, NJ) > Dept. of Plant Biology and Forest Genetics (until 131231)
Deposited By: SLUpub Connector
Deposited On:25 Nov 2020 13:03
Metadata Last Modified:15 Jan 2021 19:20

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