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Comparative analysis of plant immune receptor architectures uncovers host proteins likely targeted by pathogens.

Sarris PF, Cevik V, Dagdas G, Jones JD, Krasileva KV - BMC Biol. (2016)

Bottom Line: These composite immune receptors are thought to arise from fusions between NLRs and additional domains that serve as "baits" for the pathogen-derived effector proteins, thus enabling pathogen recognition.Domains fused to NLRs overlap with previously identified pathogen targets confirming that they act as baits for the pathogen.We hypothesize that NLR-IDs that we revealed provide clues to the host proteins targeted by pathogens, and that this information can be deployed to discover new sources of disease resistance.

View Article: PubMed Central - PubMed

Affiliation: The Sainsbury Laboratory, Norwich Research Park, Norwich, UK.

ABSTRACT

Background: Plants deploy immune receptors to detect pathogen-derived molecules and initiate defense responses. Intracellular plant immune receptors called nucleotide-binding leucine-rich repeat (NLR) proteins contain a central nucleotide-binding (NB) domain followed by a series of leucine-rich repeats (LRRs), and are key initiators of plant defense responses. However, recent studies demonstrated that NLRs with non-canonical domain architectures play an important role in plant immunity. These composite immune receptors are thought to arise from fusions between NLRs and additional domains that serve as "baits" for the pathogen-derived effector proteins, thus enabling pathogen recognition. Several names have been proposed to describe these proteins, including "integrated decoys" and "integrated sensors". We adopt and argue for "integrated domains" or NLR-IDs, which describes the product of the fusion without assigning a universal mode of action.

Results: We have scanned available plant genome sequences for the full spectrum of NLR-IDs to evaluate the diversity of integrations of potential sensor/decoy domains across flowering plants, including 19 crop species. We manually curated wheat and brassicas and experimentally validated a subset of NLR-IDs in wild and cultivated wheat varieties. We have examined NLR fusions that occur in multiple plant families and identified that some domains show re-occurring integration across lineages. Domains fused to NLRs overlap with previously identified pathogen targets confirming that they act as baits for the pathogen. While some of the integrated domains have been previously implicated in disease resistance, others provide new targets for engineering durable resistance to plant pathogens.

Conclusions: We have built a robust reproducible pipeline for detecting variable domain architectures in plant immune receptors across species. We hypothesize that NLR-IDs that we revealed provide clues to the host proteins targeted by pathogens, and that this information can be deployed to discover new sources of disease resistance.

No MeSH data available.


Related in: MedlinePlus

Summary of the information encoded in the discovered NLRs that possess “integrated domains”
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Fig6: Summary of the information encoded in the discovered NLRs that possess “integrated domains”

Mentions: Overlap between fusions and effector targets point to the multiple levels of information encoded in NLR-IDs (Fig. 6). Presented NLR-IDs are likely to be molecular sensors of the effectors, so they can also be exploited to identify and validate pathogen-derived virulence factors. For many pathogens, researchers have now accumulated long lists of predicted effector molecules that are likely to be secreted or translocated inside plant cells. Systematic analyses of these effectors against the NLR-IDs in either proteomic or yeast two-hybrid assays would allow for prioritization and validation of pathogen effectors. These validation tools represent an important milestone for deciphering pathogen arsenals and identifying new sources of disease resistance.Fig. 6


Comparative analysis of plant immune receptor architectures uncovers host proteins likely targeted by pathogens.

Sarris PF, Cevik V, Dagdas G, Jones JD, Krasileva KV - BMC Biol. (2016)

Summary of the information encoded in the discovered NLRs that possess “integrated domains”
© Copyright Policy - OpenAccess
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4759884&req=5

Fig6: Summary of the information encoded in the discovered NLRs that possess “integrated domains”
Mentions: Overlap between fusions and effector targets point to the multiple levels of information encoded in NLR-IDs (Fig. 6). Presented NLR-IDs are likely to be molecular sensors of the effectors, so they can also be exploited to identify and validate pathogen-derived virulence factors. For many pathogens, researchers have now accumulated long lists of predicted effector molecules that are likely to be secreted or translocated inside plant cells. Systematic analyses of these effectors against the NLR-IDs in either proteomic or yeast two-hybrid assays would allow for prioritization and validation of pathogen effectors. These validation tools represent an important milestone for deciphering pathogen arsenals and identifying new sources of disease resistance.Fig. 6

Bottom Line: These composite immune receptors are thought to arise from fusions between NLRs and additional domains that serve as "baits" for the pathogen-derived effector proteins, thus enabling pathogen recognition.Domains fused to NLRs overlap with previously identified pathogen targets confirming that they act as baits for the pathogen.We hypothesize that NLR-IDs that we revealed provide clues to the host proteins targeted by pathogens, and that this information can be deployed to discover new sources of disease resistance.

View Article: PubMed Central - PubMed

Affiliation: The Sainsbury Laboratory, Norwich Research Park, Norwich, UK.

ABSTRACT

Background: Plants deploy immune receptors to detect pathogen-derived molecules and initiate defense responses. Intracellular plant immune receptors called nucleotide-binding leucine-rich repeat (NLR) proteins contain a central nucleotide-binding (NB) domain followed by a series of leucine-rich repeats (LRRs), and are key initiators of plant defense responses. However, recent studies demonstrated that NLRs with non-canonical domain architectures play an important role in plant immunity. These composite immune receptors are thought to arise from fusions between NLRs and additional domains that serve as "baits" for the pathogen-derived effector proteins, thus enabling pathogen recognition. Several names have been proposed to describe these proteins, including "integrated decoys" and "integrated sensors". We adopt and argue for "integrated domains" or NLR-IDs, which describes the product of the fusion without assigning a universal mode of action.

Results: We have scanned available plant genome sequences for the full spectrum of NLR-IDs to evaluate the diversity of integrations of potential sensor/decoy domains across flowering plants, including 19 crop species. We manually curated wheat and brassicas and experimentally validated a subset of NLR-IDs in wild and cultivated wheat varieties. We have examined NLR fusions that occur in multiple plant families and identified that some domains show re-occurring integration across lineages. Domains fused to NLRs overlap with previously identified pathogen targets confirming that they act as baits for the pathogen. While some of the integrated domains have been previously implicated in disease resistance, others provide new targets for engineering durable resistance to plant pathogens.

Conclusions: We have built a robust reproducible pipeline for detecting variable domain architectures in plant immune receptors across species. We hypothesize that NLR-IDs that we revealed provide clues to the host proteins targeted by pathogens, and that this information can be deployed to discover new sources of disease resistance.

No MeSH data available.


Related in: MedlinePlus