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An RLP23-SOBIR1-BAK1 complex mediates NLP-triggered immunity.

Identifieur interne : 000F30 ( Main/Exploration ); précédent : 000F29; suivant : 000F31

An RLP23-SOBIR1-BAK1 complex mediates NLP-triggered immunity.

Auteurs : Isabell Albert [Allemagne] ; Hannah Böhm [Allemagne] ; Markus Albert [Allemagne] ; Christina E. Feiler [Allemagne] ; Julia Imkampe [Allemagne] ; Niklas Wallmeroth [Allemagne] ; Caterina Brancato [Allemagne] ; Tom M. Raaymakers [Pays-Bas] ; Stan Oome [Pays-Bas] ; Heqiao Zhang [République populaire de Chine] ; Elzbieta Krol [Allemagne] ; Christopher Grefen [Allemagne] ; Andrea A. Gust [Allemagne] ; Jijie Chai [République populaire de Chine] ; Rainer Hedrich [Allemagne] ; Guido Van Den Ackerveken [Pays-Bas] ; Thorsten Nürnberger [Allemagne]

Source :

RBID : pubmed:27251392

Abstract

Plants and animals employ innate immune systems to cope with microbial infection. Pattern-triggered immunity relies on the recognition of microbe-derived patterns by pattern recognition receptors (PRRs). Necrosis and ethylene-inducing peptide 1-like proteins (NLPs) constitute plant immunogenic patterns that are unique, as these proteins are produced by multiple prokaryotic (bacterial) and eukaryotic (fungal, oomycete) species. Here we show that the leucine-rich repeat receptor protein (LRR-RP) RLP23 binds in vivo to a conserved 20-amino-acid fragment found in most NLPs (nlp20), thereby mediating immune activation in Arabidopsis thaliana. RLP23 forms a constitutive, ligand-independent complex with the LRR receptor kinase (LRR-RK) SOBIR1 (Suppressor of Brassinosteroid insensitive 1 (BRI1)-associated kinase (BAK1)-interacting receptor kinase 1), and recruits a second LRR-RK, BAK1, into a tripartite complex upon ligand binding. Stable, ectopic expression of RLP23 in potato (Solanum tuberosum) confers nlp20 pattern recognition and enhanced immunity to destructive oomycete and fungal plant pathogens, such as Phytophthora infestans and Sclerotinia sclerotiorum. PRRs that recognize widespread microbial patterns might be particularly suited for engineering immunity in crop plants.

DOI: 10.1038/nplants.2015.140
PubMed: 27251392


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<div type="abstract" xml:lang="en">Plants and animals employ innate immune systems to cope with microbial infection. Pattern-triggered immunity relies on the recognition of microbe-derived patterns by pattern recognition receptors (PRRs). Necrosis and ethylene-inducing peptide 1-like proteins (NLPs) constitute plant immunogenic patterns that are unique, as these proteins are produced by multiple prokaryotic (bacterial) and eukaryotic (fungal, oomycete) species. Here we show that the leucine-rich repeat receptor protein (LRR-RP) RLP23 binds in vivo to a conserved 20-amino-acid fragment found in most NLPs (nlp20), thereby mediating immune activation in Arabidopsis thaliana. RLP23 forms a constitutive, ligand-independent complex with the LRR receptor kinase (LRR-RK) SOBIR1 (Suppressor of Brassinosteroid insensitive 1 (BRI1)-associated kinase (BAK1)-interacting receptor kinase 1), and recruits a second LRR-RK, BAK1, into a tripartite complex upon ligand binding. Stable, ectopic expression of RLP23 in potato (Solanum tuberosum) confers nlp20 pattern recognition and enhanced immunity to destructive oomycete and fungal plant pathogens, such as Phytophthora infestans and Sclerotinia sclerotiorum. PRRs that recognize widespread microbial patterns might be particularly suited for engineering immunity in crop plants. </div>
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