The changing of the guard: the Pto/Prf receptor complex of tomato and pathogen recognition

Ntoukakis, Vardis; Saur, Isabel M. L.; Conlan, Brendon; Rathjen, John P.

doi:10.1016/j.pbi.2014.04.002

Cited by 56 publications

(49 citation statements)

References 78 publications

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“…A host decoy strategy also fits with the mode of tomato CNL Prf (Pseudomonas resistance and fenthion sensitivity) resistance to several bacterial effectors, including P. syringae AvrPto (103). Prf is held in an inactive form by direct binding of the protein kinase Pto (103,153). A role for Pto in basal immunity has not been established, but its kinase domain resembles that of the PRRs FLS2 (flagellin-sensitive 2) and EFR (elongation factor Tu receptor) and their coreceptor BAK1 (BRI1-associated receptor kinase 1), which are also targeted by AvrPto during infection (118,152).…”

Section: Indirect Nlr Surveillance Of Effector Activitiesmentioning

confidence: 93%

“…One of these, the soluble kinase BIK1 (Botrytis-induced kinase 1), is an important component of PRR signaling in PTI and a key AvrPphB virulence target (68,82,157). A host decoy strategy also fits with the mode of tomato CNL Prf (Pseudomonas resistance and fenthion sensitivity) resistance to several bacterial effectors, including P. syringae AvrPto (103). Prf is held in an inactive form by direct binding of the protein kinase Pto (103,153).…”

Section: Indirect Nlr Surveillance Of Effector Activitiesmentioning

confidence: 99%

See 1 more Smart Citation

Effector-Triggered Immunity: From Pathogen Perception to Robust Defense

Cui

Tsuda

Parker

2015

Annu. Rev. Plant Biol.

1,095

892

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In plant innate immunity, individual cells have the capacity to sense and respond to pathogen attack. Intracellular recognition mechanisms have evolved to intercept perturbations by pathogen virulence factors (effectors) early in host infection and convert it to rapid defense. One key to resistance success is a polymorphic family of intracellular nucleotide-binding/leucine-rich-repeat (NLR) receptors that detect effector interference in different parts of the cell. Effector-activated NLRs connect, in various ways, to a conserved basal resistance network in order to transcriptionally boost defense programs. Effector-triggered immunity displays remarkable robustness against pathogen disturbance, in part by employing compensatory mechanisms within the defense network. Also, the mobility of some NLRs and coordination of resistance pathways across cell compartments provides flexibility to fine-tune immune outputs. Furthermore, a number of NLRs function close to the nuclear chromatin by balancing actions of defense-repressing and defense-activating transcription factors to program cells dynamically for effective disease resistance.

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Section: Indirect Nlr Surveillance Of Effector Activitiesmentioning

confidence: 93%

Section: Indirect Nlr Surveillance Of Effector Activitiesmentioning

confidence: 99%

Effector-Triggered Immunity: From Pathogen Perception to Robust Defense

Cui

Tsuda

Parker

2015

Annu. Rev. Plant Biol.

1,095

892

View full text Add to dashboard Cite

show abstract

“…Previous studies on plant proteins such as the CNL receptor Prf (Gutierrez et al, 2010;Ntoukakis et al, 2014) and RPS5 (Ade et al, 2007) have suggested that oligomerization of plant NLRs plays some type of role in the activation of defense mechanisms. Crystallographic analyses of the structures and functions of the N-terminal domains of MLA10 confirmed that they form homodimers and revealed the nature of the interface for each N-terminal dimer module.…”

Section: The Oligomerization Of Bph14 Is Implicated In Plant Immunitymentioning

confidence: 99%

The Coiled-Coil and Nucleotide Binding Domains of BROWN PLANTHOPPER RESISTANCE14 Function in Signaling and Resistance against Planthopper in Rice

et al. 2017

Plant Cell

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BROWN PLANTHOPPER RESISTANCE14 (BPH14), the first planthopper resistance gene isolated via map-based cloning in rice (Oryza sativa), encodes a coiled-coil, nucleotide binding site, leucine-rich repeat (CC-NB-LRR) protein. Several planthopper and aphid resistance genes encoding proteins with similar structures have recently been identified. Here, we analyzed the functions of the domains of BPH14 to identify molecular mechanisms underpinning BPH14-mediated planthopper resistance. The CC or NB domains alone or in combination (CC-NB [CN]) conferred a similar level of brown planthopper resistance to that of full-length (FL) BPH14. Both domains activated the salicylic acid signaling pathway and defense gene expression. In rice protoplasts and Nicotiana benthamiana leaves, these domains increased reactive oxygen species levels without triggering cell death. Additionally, the resistance domains and FL BPH14 protein formed homocomplexes that interacted with transcription factors WRKY46 and WRKY72. In rice protoplasts, the expression of FL BPH14 or its CC, NB, and CN domains increased the accumulation of WRKY46 and WRKY72 as well as WRKY46-and WRKY72-dependent transactivation activity. WRKY46 and WRKY72 bind to the promoters of the receptor-like cytoplasmic kinase gene RLCK281 and the callose synthase gene LOC_Os01g67364.1, whose transactivation activity is dependent on WRKY46 or WRKY72. These findings shed light on this important insect resistance mechanism.

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“…One well studied example for indirect recognition is the Pto-Prf protein complex of tomato. Studies on this complex have revealed important insights into the modification of accessory proteins by effector molecules (13). The Pto kinase is an accessory of the NB-LRR protein Prf, and interacts directly with the unrelated Pseudomonas syringae pv.…”

mentioning

confidence: 99%

“…Interestingly, the NRP is required to maintain Prf in the inactive configuration prior to effector perception, suggesting that there is molecular competition between the effectors and Prf for this binding surface. However, effector binding does not change the Pto-Prf interaction, and the two kinases are kept in close proximity (13,21). This is mediated by the unique Prf N-terminal domain (previously abbreviated as N-term, here named N, residues 1-546), which is the interaction site for Pto (21) and the contact surface for Prf oligomerization (22).…”

mentioning

confidence: 99%