Structure–function analysis of ZAR1 immune receptor reveals key molecular interactions for activity

Baudin, Maël; Schreiber, Karl J.; Martin, Eliza C.; Petrescu, Andrei‐Jose; Lewis, Jennifer D.

doi:10.1111/tpj.14547

Cited by 26 publications

(28 citation statements)

References 105 publications

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“…To validate the ZAR1 constructs we generated, we first used agroinfiltration to transiently express wild-type ZAR1 and the MHD mutants AtZAR1 D489V and NbZAR1 D481V in N. benthamiana leaves ( Figure 2A). As recently reported by Baudin et al (2019), AtZAR1 did not trigger macroscopic cell death in N. benthamiana leaves even when the full-length protein carries the D489V mutation in the MHD motif ( Figure 2B and 2C). In contrast, NbZAR1 caused macroscopic cell death when the MHD mutant NbZAR1 D481V was expressed in N. benthamiana leaves ( Figure 2D and 2E).…”

Section: Unlike Arabidopsis Zar1 Nbzar1 Triggers Autoimmune Cell Deasupporting

confidence: 84%

A vector system for fast-forwardin vivostudies of the ZAR1 resistosome in the model plantNicotiana benthamiana

Harant

Sakai

Kamoun

et al. 2020

Preprint

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Nicotiana benthamiana has emerged as a complementary experimental system to Arabidopsis. It enables fast-forward in vivo analyses primarily through transient gene expression and is particularly popular in the study of plant immunity. Recently, our understanding of NLR plant immune receptors has greatly advanced following the discovery of Arabidopsis ZAR1 resistosome. Here, we describe a novel vector system of 52 plasmids that enables functional studies of the ZAR1 resistosome in N. benthamiana. We showed that ZAR1 stands out among the coiled coil class of NLRs for being highly conserved across distantly related dicot plant species and confirmed NbZAR1 as the N. benthamiana ortholog of Arabidopsis ZAR1. NbZAR1 triggers autoimmune cell death in N. benthamiana and this activity is dependent on a functional N-terminal a1 helix. C-terminally tagged NbZAR1 remains functional in N. benthamiana thus enabling cell biology and biochemical studies in this plant system. We conclude that the NbZAR1 open source plasmids form an additional experimental system to Arabidopsis for in planta resistosome studies.

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Section: Unlike Arabidopsis Zar1 Nbzar1 Triggers Autoimmune Cell Deasupporting

confidence: 84%

A vector system for fast-forwardin vivostudies of the ZAR1 resistosome in the model plantNicotiana benthamiana

Harant

Sakai

Kamoun

et al. 2020

Preprint

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“…Similar to TIR domains, the hetero‐ and homo‐dimerization of CC domains of CNLs have also been shown (El Kasmi et al 2017; Bentham et al 2018; Zou et al 2018a; Baudin et al 2019), yet the role of dimerization is not clear. A recent interactome analysis demonstrated that the heterodimerization of CC domains is more frequent than homodimerization, indicating that CNLs may form a network to mediate immune responses after the perception of effectors.…”

Section: Recent Discoveries Of the Activation Of Intracellular Nlrsmentioning

confidence: 99%

Plant immune signaling: Advancing on two frontiers

Wang

Feng

Zhou

et al. 2020

JIPB

188

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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“…Effector detection often occurs (directly or indirectly) at the C‐terminal LRR domain, and results in the exchange of ADP for ATP in the NBARC domain due to deep conformational reorganization of NLR domains. In many cases, oligomerization of the N‐terminal domain (CC or TIR) is associated with the activation of the NLR and the induction of downstream signalling (Baudin, Hassan, Schreiber, & Lewis, 2017; Baudin, Schreiber, Martin, Petrescu, & Lewis, 2019; Bernoux et al, 2011; Maekawa et al, 2011). The mechanisms by which activated NLRs induce defence responses remain elusive as very few signalling pathways have been identified so far.…”

Section: Introductionmentioning

confidence: 99%

“…We previously showed that protein domains of ZAR1 are involved in specific intra‐ and inter‐molecular interactions that are critical for ZAR1 activity and prevent inappropriate activation of the NLR (Baudin et al, 2017, 2019; Liu et al, 2019). The LRR domain of ZAR1 is important for interactions with ZED1, RKS1/ZRK1 and ZRK3 (Baudin et al, 2017; G. Wang, Roux, et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

A natural diversity screen in Arabidopsis thaliana reveals determinants for HopZ1a recognition in the ZAR1‐ZED1 immune complex

Baudin

Martin

Sass

et al. 2020

Plant Cell & Environment

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Pathogen pressure on hosts can lead to the evolution of genes regulating the innate immune response. By characterizing naturally occurring polymorphisms in immune receptors, we can better understand the molecular determinants of pathogen recognition. ZAR1 is an ancient Arabidopsis thaliana NLR (Nucleotide‐binding [NB] Leucine‐rich‐repeat [LRR] Receptor) that recognizes multiple secreted effector proteins from the pathogenic bacteria Pseudomonas syringae and Xanthomonas campestris through its interaction with receptor‐like cytoplasmic kinases (RLCKs). ZAR1 was first identified for its role in recognizing P. syringae effector HopZ1a, through its interaction with the RLCK ZED1. To identify additional determinants of HopZ1a recognition, we performed a computational screen for ecotypes from the 1001 Genomes project that were likely to lack HopZ1a recognition, and tested ~300 ecotypes. We identified ecotypes containing polymorphisms in ZAR1 and ZED1. Using our previously established Nicotiana benthamiana transient assay and Arabidopsis ecotypes, we tested for the effect of naturally occurring polymorphisms on ZAR1 interactions and the immune response. We identified key residues in the NB or LRR domain of ZAR1 that impact the interaction with ZED1. We demonstrate that natural diversity combined with functional assays can help define the molecular determinants and interactions necessary to regulate immune induction in response to pathogens.

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Structure–function analysis of ZAR1 immune receptor reveals key molecular interactions for activity

Cited by 26 publications

References 105 publications

A vector system for fast-forwardin vivostudies of the ZAR1 resistosome in the model plantNicotiana benthamiana

A vector system for fast-forwardin vivostudies of the ZAR1 resistosome in the model plantNicotiana benthamiana

Plant immune signaling: Advancing on two frontiers

A natural diversity screen in Arabidopsis thaliana reveals determinants for HopZ1a recognition in the ZAR1‐ZED1 immune complex

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