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

Duxbury, Zane, Wang, Shanshan, MacKenzie, Craig I., Tenthorey, Jeannette L., Zhang, Xiaoxiao, Huh, Sung Un, Hu, Lanxi, Hill, Lionel, Ngou, Pok Man, Ding, Pingtao, Chen, Jian, Ma, Yan, Guo, Hailong, Castel, Baptiste, Moschou, Panagiotis N., Bernoux, Maud, Dodds, Peter N., 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 (31). pp. 18832-18839. ISSN 1091-6490

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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.

Item Type:	Article
Faculty \ School:	Faculty of Science > The Sainsbury Laboratory
UEA Research Groups:	Faculty of Science > Research Groups > Plant Sciences
Depositing User:	LivePure Connector
Date Deposited:	13 Aug 2020 23:58
Last Modified:	18 Oct 2024 23:54
URI:	https://ueaeprints.uea.ac.uk/id/eprint/76437
DOI:	10.1073/pnas.2001185117

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