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

58Citations
Citations of this article
101Readers
Mendeley users who have this article in their library.

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)- A nd 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 CCNLR 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.

Cite

CITATION STYLE

APA

Duxbury, Z., Wang, S., MacKenzie, C. I., Tenthorey, J. L., Zhang, X., Huh, S. U., … Jones, J. 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), 18832–18839. https://doi.org/10.1073/pnas.2001185117

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free