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Animal NLRs continue to inform plant NLR structure and function.
Hayden Burdett1, Bostjan Kobe1, Peter A Anderson2
1School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD, 4072, Australia.
Plant NLRs, like animal counterparts, possess nucleotide-binding pockets and self-associating TIR domains. This suggests plant NLRs may form higher-order complexes, akin to animal inflammasomes, for innate immunity signaling.
Area of Science:
- Plant molecular biology
- Immunology
- Structural biology
Background:
- Plant NLRs (NLRs) exhibit structural similarities to animal NLRs.
- NLRs play crucial roles in plant innate immunity.
- Animal NLRs, particularly inflammasomes, form higher-order complexes to mediate immune responses.
Purpose of the Study:
- To review structure-function relationships in plant NLRs.
- To explore how animal NLR knowledge informs plant NLR mechanisms.
- To highlight the role of higher-order protein complexes in innate immunity signaling.
Main Methods:
- Literature review of plant and animal NLR research.
- Comparative analysis of structural and functional data.
- Synthesis of evidence for protein complex formation in plant immunity.
Main Results:
- Plant NLRs share functional similarities with animal NLRs, including nucleotide binding and hydrolysis.
- TIR domains of plant NLRs demonstrate self-association.
- Emerging evidence suggests full-length plant NLRs may also form higher-order structures.
Conclusions:
- Plant NLRs may assemble into higher-order complexes analogous to mammalian inflammasomes.
- The formation of higher-order protein complexes is a conserved mechanism in innate immunity across multicellular organisms.
- Further research into plant NLR complex formation is warranted to elucidate immune signaling pathways.
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