How to build a pathogen detector: structural basis of NB-LRR function

Takken, Frank L. W.; Goverse, A.

doi:10.1016/j.pbi.2012.05.001

Cited by 257 publications

(234 citation statements)

References 63 publications

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“…CC-NB) dysfunctional, while binding to the sensor (i.e. LRR) domain is still intact (Takken and Goverse, 2012). We tried to make SW5F, along with SW5B, constitutively active by introducing mutations at positions that switch several other CC-NB-LRR resistance proteins into a permanent "on" state.…”

Section: Discussionmentioning

confidence: 99%

The Effector SPRYSEC-19 ofGlobodera rostochiensisSuppresses CC-NB-LRR-Mediated Disease Resistance in Plants

et al. 2012

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The potato cyst nematode Globodera rostochiensis invades roots of host plants where it transforms cells near the vascular cylinder into a permanent feeding site. The host cell modifications are most likely induced by a complex mixture of proteins in the stylet secretions of the nematodes. Resistance to nematodes conferred by nucleotide-binding-leucine-rich repeat (NB-LRR) proteins usually results in a programmed cell death in and around the feeding site, and is most likely triggered by the recognition of effectors in stylet secretions. However, the actual role of these secretions in the activation and suppression of effector-triggered immunity is largely unknown. Here we demonstrate that the effector SPRYSEC-19 of G. rostochiensis physically associates in planta with the LRR domain of a member of the SW5 resistance gene cluster in tomato (Lycopersicon esculentum).

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Section: Discussionmentioning

confidence: 99%

The Effector SPRYSEC-19 ofGlobodera rostochiensisSuppresses CC-NB-LRR-Mediated Disease Resistance in Plants

et al. 2012

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“…Indeed, the majority of cloned dominant resistance ( R ) genes broadly used by breeders code for NLR proteins. NLRs constitute huge and highly diverse gene families in plant genomes that can be further subdivided into coil‐coil NBS‐LRRs (CNLs), which contain an N‐terminal coil‐coil (CC) domain, and TIR‐NBS‐LRRs (TNLs), which have a Toll/interleukin‐1 (TIR) domain and are absent from monocot genomes (Takken & Goverse, 2012). NLR proteins act as immune receptors that recognize pathogen effectors in the cytosol.…”

Section: Introductionmentioning

confidence: 99%

Integration of decoy domains derived from protein targets of pathogen effectors into plant immune receptors is widespread

et al. 2016

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Summary Plant immune receptors of the class of nucleotide‐binding and leucine‐rich repeat domain (NLR) proteins can contain additional domains besides canonical NB‐ARC (nucleotide‐binding adaptor shared by APAF‐1, R proteins, and CED‐4 (NB‐ARC)) and leucine‐rich repeat (LRR) domains. Recent research suggests that these additional domains act as integrated decoys recognizing effectors from pathogens. Proteins homologous to integrated decoys are suspected to be effector targets and involved in disease or resistance.Here, we scrutinized 31 entire plant genomes to identify putative integrated decoy domains in NLR proteins using the Interpro search. The involvement of the Zinc Finger–BED type (ZBED) protein containing a putative decoy domain, called BED, in rice (Oryza sativa) resistance was investigated by evaluating susceptibility to the blast fungus Magnaporthe oryzae in rice over‐expression and knock‐out mutants.This analysis showed that all plants tested had integrated various atypical protein domains into their NLR proteins (on average 3.5% of all NLR proteins). We also demonstrated that modifying the expression of the ZBED gene modified disease susceptibility.This study suggests that integration of decoy domains in NLR immune receptors is widespread and frequent in plants. The integrated decoy model is therefore a powerful concept to identify new proteins involved in disease resistance. Further in‐depth examination of additional domains in NLR proteins promises to unravel many new proteins of the plant immune system.

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“…Current models of disease resistance protein activation suggest that in the absence of pathogen, NB-LRRs fold into a signaling-competent state that retains the whole protein in an autoinhibited form through intramolecular interactions (Collier and Moffett, 2009;Takken and Goverse, 2012). Recently, random mutagenesis screening of the full-length R3a protein revealed that autoactivation of this I2-like can be achieved through a single amino-acid change within the N-terminal CC domain (I148F; Segretin et al, 2014).…”

Section: Discussion Activation Of Cell Death By the CC Domains Of I2-mentioning

confidence: 99%

“…One such mechanism is based on disease resistance (R) proteins belonging to the nucleotide-binding/ Leu-rich repeat (NB-LRR) family. These proteins display a conserved protein structure, with a central NB domain and LRRs at the C terminus (Collier and Moffett, 2009;Takken and Goverse, 2012). NB-LRR proteins fall into three major clades, which correlate with the domains present at their N termini (Shao et al, 2014).…”

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The Chloroplastic Protein THF1 Interacts with the Coiled-Coil Domain of the Disease Resistance Protein N′ and Regulates Light-Dependent Cell Death

et al. 2016

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One branch of plant immunity is mediated through nucleotide-binding/Leu-rich repeat (NB-LRR) family proteins that recognize specific effectors encoded by pathogens. Members of the I2-like family constitute a well-conserved subgroup of NB-LRRs from Solanaceae possessing a coiled-coil (CC) domain at their N termini. We show here that the CC domains of several I2-like proteins are able to induce a hypersensitive response (HR), a form of programmed cell death associated with disease resistance. Using yeast two-hybrid screens, we identified the chloroplastic protein Thylakoid Formation1 (THF1) as an interacting partner for several I2-like CC domains. Co-immunoprecipitations and bimolecular fluorescence complementation assays confirmed that THF1 and I2-like CC domains interact in planta and that these interactions take place in the cytosol. Several HR-inducing I2-like CC domains have a negative effect on the accumulation of THF1, suggesting that the latter is destabilized by active CC domains. To confirm this model, we investigated N9, which recognizes the coat protein of most Tobamoviruses, as a prototypical member of the I2-like family. Transient expression and gene silencing data indicated that THF1 functions as a negative regulator of cell death and that activation of full-length N9 results in the destabilization of THF1. Consistent with the known function of THF1 in maintaining chloroplast homeostasis, we show that the HR induced by N9 is light-dependent. Together, our results define, to our knowledge, novel molecular mechanisms linking light and chloroplasts to the induction of cell death by a subgroup of NB-LRR proteins.

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How to build a pathogen detector: structural basis of NB-LRR function

Cited by 257 publications

References 63 publications

The Effector SPRYSEC-19 ofGlobodera rostochiensisSuppresses CC-NB-LRR-Mediated Disease Resistance in Plants

The Effector SPRYSEC-19 ofGlobodera rostochiensisSuppresses CC-NB-LRR-Mediated Disease Resistance in Plants

Integration of decoy domains derived from protein targets of pathogen effectors into plant immune receptors is widespread

The Chloroplastic Protein THF1 Interacts with the Coiled-Coil Domain of the Disease Resistance Protein N′ and Regulates Light-Dependent Cell Death

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