Animal NLRs provide structural insights into plant NLR function

Bentham, Adam, Burdett, Hayden, Anderson, Peter A., Williams, Simon J. and Kobe, Bostjan (2016) Animal NLRs provide structural insights into plant NLR function. Annals of Botany, 119 5: 689-702. doi:10.1093/aob/mcw171


Author Bentham, Adam
Burdett, Hayden
Anderson, Peter A.
Williams, Simon J.
Kobe, Bostjan
Title Animal NLRs provide structural insights into plant NLR function
Journal name Annals of Botany   Check publisher's open access policy
ISSN 1095-8290
0305-7364
Publication date 2016-08-25
Sub-type Article (original research)
DOI 10.1093/aob/mcw171
Open Access Status Not yet assessed
Volume 119
Issue 5
Start page 689
End page 702
Total pages 14
Place of publication Oxford, United Kingdom
Publisher Oxford University Press
Language eng
Formatted abstract
Background The plant immune system employs intracellular NLRs (nucleotide binding [NB], leucine-rich repeat [LRR]/nucleotide-binding oligomerization domain [NOD]-like receptors) to detect effector proteins secreted into the plant cell by potential pathogens. Activated plant NLRs trigger a range of immune responses, collectively known as the hypersensitive response (HR), which culminates in death of the infected cell. Plant NLRs show structural and functional resemblance to animal NLRs involved in inflammatory and innate immune responses. Therefore, knowledge of the activation and regulation of animal NLRs can help us understand the mechanism of action of plant NLRs, and vice versa.

Scope This review provides an overview of the innate immune pathways in plants and animals, focusing on the available structural and biochemical information available for both plant and animal NLRs. We highlight the gap in knowledge between the animal and plant systems, in particular the lack of structural information for plant NLRs, with crystal structures only available for the N-terminal domains of plant NLRs and an integrated decoy domain, in contrast to the more complete structures available for animal NLRs. We assess the similarities and differences between plant and animal NLRs, and use the structural information on the animal NLR pair NAIP/NLRC4 to derive a plausible model for plant NLR activation.

Conclusions Signalling by cooperative assembly formation (SCAF) appears to operate in most innate immunity pathways, including plant and animal NLRs. Our proposed model of plant NLR activation includes three key steps: (1) initially, the NLR exists in an inactive auto-inhibited state; (2) a combination of binding by activating elicitor and ATP leads to a structural rearrangement of the NLR; and (3) signalling occurs through cooperative assembly of the resistosome. Further studies, structural and biochemical in particular, will be required to provide additional evidence for the different features of this model and shed light on the many existing variations, e.g. helper NLRs and NLRs containing integrated decoys.
Keyword Avirulence protein
Crystal structure
Cryo-electron microscopy
Effector-triggered immunity (ETI)
Nucleotide binding (NB)
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ
Additional Notes Published online 25 August 2016

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
School of Chemistry and Molecular Biosciences
 
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Created: Tue, 27 Sep 2016, 21:39:35 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences