Animal NLRs continue to inform plant NLR structure and function

Burdett, H.; Kobe, Boštjan; Anderson, Peter

doi:10.1016/j.abb.2019.05.001

Cited by 26 publications

(18 citation statements)

References 139 publications

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“…Although animal and plant NLRs presumably evolved independently (Urbach and Ausubel, 2017), studies on animal systems have cross-informed the mechanisms used by plant systems and vice versa (Burdett et al, 2019). Proteins involved in innate immunity pathways have recruited analogous domains and use conceptually analogous mechanisms of signaling, including SCAF (Vajjhala et al, 2017).…”

Section: Discussionmentioning

confidence: 99%

“…The ATP-Mediated Activation of the ZAR1 Resistosome Transition from an ADP to an ATP-bound state and oligomer formation has been postulated as a requirement for activation (Burdett et al, 2019), and this is now elegantly demonstrated with the structure of the third state (PDB: 6J5T) (Wang et al, 2019a). Interestingly, the authors found dATP, rather than ATP, to be a more efficient activating ligand in vitro.…”

Section: The Structures Of Zar1 Complexesmentioning

confidence: 99%

“…Pathogen effector recognition may occur either directly or indirectly, through detection of effector activities on host proteins. Mechanistic understanding of plant NLR function has relied on structural information from individual NLR domains and inferences from studies on animal NLRs (Burdett et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

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The Plant “Resistosome”: Structural Insights into Immune Signaling

Burdett

Bentham

Williams

et al. 2019

Cell Host & Microbe

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Plant innate immunity is triggered via direct or indirect recognition of pathogen effectors by the NLR family immune receptors. Mechanistic understanding of plant NLR function has relied on structural information from individual NLR domains and inferences from studies on animal NLRs. Recent reports of the cryo-EM structures of the Arabidopsis plant immune receptor ZAR1 in monomeric inactive and transition states, as well as the active oligomeric state or the ''resistosome,'' have afforded a quantum leap in our understanding of how plant NLRs function. In this Review, we outline the recent structural findings and examine their implications for the activation of plant immune receptors more broadly. We also discuss how NLR signaling in plants, as illustrated by the ZAR1 structure, is analogous to innate immune receptor signaling mechanisms across kingdoms, drawing particular attention to the concept of signaling by cooperative assembly formation.

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Section: Discussionmentioning

confidence: 99%

Section: The Structures Of Zar1 Complexesmentioning

confidence: 99%

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The Plant “Resistosome”: Structural Insights into Immune Signaling

Burdett

Bentham

Williams

et al. 2019

Cell Host & Microbe

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“…syringae ( Psy B728a), produce BGAL1‐insensitive glycans to escape the recognition by FLS2 (Yamamoto et al 2011; Chiku et al 2013; Buscaill et al 2019). As peptide MAMPs elf18, nlp24, and pep13 from bacterial, fungal, and oomycete pathogens, respectively, are also buried within the folded protein structures, it will be interesting to determine how these elicitors are released (Brunner et al 2002; Ottmann et al 2009; Reiss et al 2011; Bohm et al 2014).…”

Section: Recent Discoveries Of the Activation Of Immunity Mediated Bymentioning

confidence: 99%

Plant immune signaling: Advancing on two frontiers

Wang

Feng

Zhou

et al. 2020

JIPB

175

144

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Plants have evolved multiple defense strategies to cope with pathogens, among which plant immune signaling that relies on cell-surface localized and intracellular receptors takes fundamental roles. Exciting breakthroughs were made recently on the signaling mechanisms of pattern recognition receptors (PRRs) and intracellular nucleotide-binding site (NBS) and leucine-rich repeat (LRR) domain receptors (NLRs). This review summarizes the current view of PRRs activation, emphasizing the most recent discoveries about PRRs' dynamic regulation and signaling mechanisms directly leading to downstream molecular events including mitogen-activated protein kinase (MAPK) activation and calcium (Ca 2+ ) burst. Plants also have evolved intracellular NLRs to perceive the presence of specific pathogen effectors and trigger more robust immune responses. We also discuss the current understanding of the mechanisms of NLR activation, which has been greatly advanced by recent breakthroughs including structures of the first full-length plant NLR complex, findings of NLR sensor-helper pairs and novel biochemical activity of Toll/interleukin-1 receptor (TIR) domain.

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“…Mutations within the MHD motif frequently lead to constitutive activity (often called auto-activation [22][23][24][25][26]). The C-terminal LRR domain has a role in auto-inhibition [27][28][29], a function shared with animal NLRs [30][31][32], but can also define effector recognition specificity [33].…”

Section: Introductionmentioning

confidence: 99%

The rice NLR pair Pikp-1/Pikp-2 initiates cell death through receptor cooperation rather than negative regulation

Zdrzałek¹,

Kamoun²,

Terauchi³

et al. 2020

PLoS ONE

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Plant NLR immune receptors are multidomain proteins that can function as specialized sensor/helper pairs. Paired NLR immune receptors are generally thought to function via negative regulation, where one NLR represses the activity of the second and detection of pathogen effectors relieves this repression to initiate immunity. However, whether this mechanism is common to all NLR pairs is not known. Here, we show that the rice NLR pair Pikp-1/Pikp-2, which confers resistance to strains of the blast pathogen Magnaporthe oryzae (syn. Pyricularia oryzae) expressing the AVR-PikD effector, functions via receptor cooperation, with effector-triggered activation requiring both NLRs to trigger the immune response. To investigate the mechanism of Pikp-1/Pikp-2 activation, we expressed truncated variants of these proteins, and made mutations in previously identified NLR sequence motifs. We found that any domain truncation, in either Pikp-1 or Pikp-2, prevented cell death in the presence of AVR-PikD, revealing that all domains are required for activity. Further, expression of individual Pikp-1 or Pikp-2 domains did not result in cell death. Mutations in the conserved P-loop and MHD sequence motifs in both Pikp-1 and Pikp-2 prevented cell death activation, demonstrating that these motifs are required for the function of the two partner NLRs. Finally, we showed that Pikp-1 and Pikp-2 associate to form homo-and hetero-complexes in planta in the absence of AVR-PikD; on co-expression the effector binds to Pikp-1 generating a tri-partite complex. Taken together, we provide evidence that Pikp-1 and Pikp-2 form a fine-tuned system that is activated by AVR-PikD via receptor cooperation rather than negative regulation.

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Animal NLRs continue to inform plant NLR structure and function

Cited by 26 publications

References 139 publications

The Plant “Resistosome”: Structural Insights into Immune Signaling

The Plant “Resistosome”: Structural Insights into Immune Signaling

Plant immune signaling: Advancing on two frontiers

The rice NLR pair Pikp-1/Pikp-2 initiates cell death through receptor cooperation rather than negative regulation

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