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Published on: January 14, 2016
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Animal NLRs provide structural insights into plant NLR function.
Adam Bentham1,2, Hayden Burdett1, Peter A Anderson1
1School of Biological Sciences, Flinders University, Adelaide, SA 5001, Australia.
Annals of Botany
|August 27, 2016
Summary
Plant and animal NLRs (nucleotide binding [NB], leucine-rich repeat [LRR]/nucleotide-binding oligomerization domain [NOD]-like receptors) share immune pathway similarities. A new model proposes plant NLR activation via auto-inhibition release, elicitor binding, and resistosome assembly.
Area of Science:
- Plant and animal immunology
- Molecular biology
- Structural biology
Background:
- Plant intracellular NLRs detect pathogen effectors, triggering hypersensitive response (HR) and cell death.
- Plant NLRs share structural and functional similarities with animal NLRs involved in innate immunity.
- Understanding animal NLRs aids plant NLR mechanism elucidation, and vice versa.
Purpose of the Study:
- To review plant and animal innate immune pathways, focusing on NLR structural and biochemical data.
- To identify knowledge gaps, particularly the limited structural information for plant NLRs compared to animal NLRs.
- To propose a plausible model for plant NLR activation based on animal NLR structural data.
Main Methods:
- Comparative review of plant and animal NLR structural and biochemical information.
- Analysis of existing crystal structures of plant NLR N-terminal domains and integrated decoy domains.
- Extrapolation of activation mechanisms from the animal NLR pair NAIP/NLRC4 to plant NLRs.
Main Results:
- Significant gaps exist in structural data for plant NLRs compared to more complete animal NLR structures.
- Similarities and differences between plant and animal NLRs were assessed.
- A plausible model for plant NLR activation was derived using animal NLR structural insights.
Conclusions:
- Signalling by cooperative assembly formation (SCAF) is likely conserved across plant and animal NLR pathways.
- A three-step model for plant NLR activation is proposed: auto-inhibition release, elicitor/ATP binding-induced rearrangement, and resistosome assembly.
- Further structural and biochemical studies are needed to validate the model and explore variations in NLR function.
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