Plants use receptor
kinases (RKs) and receptor-like
proteins (RLPs) as
pattern recognition receptors (
PRRs) to sense
pathogen-associated molecular patterns (
PAMPs) that are typical of whole classes of microbes. After
ligand perception, many
leucine-rich repeat (LRR)-containing
PRRs interact with the LRR-RK BRI1-ASSOCIATED
KINASE 1 (BAK1). BAK1 is thus expected to interact with unknown
PRRs. Here, we used BAK1 as molecular bait to identify a previously unknown LRR-RLP required for the recognition of the csp22
peptide derived from bacterial
cold shock protein. We established a method to identify
proteins that interact with BAK1 only after csp22 treatment. BAK1 was expressed transiently in Nicotiana benthamiana and immunopurified
after treatment with csp22. BAK1-associated
proteins were identified by mass spectrometry. We identified several
proteins including known BAK1 interactors and a previously uncharacterized LRR-RLP that we termed RECEPTOR-LIKE
PROTEIN REQUIRED FOR CSP22 RESPONSIVENESS (NbCSPR). This RLP associates with BAK1 upon csp22 treatment, and NbCSPR-silenced plants are impaired in csp22-induced defense responses. NbCSPR confers resistance to bacteria in an age-dependent and
flagellin-induced manner. As such, it limits bacterial growth and Agrobacterium-mediated transformation of flowering N. benthamiana plants. Transgenic expression of NbCSPR into Arabidopsis thaliana conferred responsiveness to csp22 and antibacterial resistance. Our method may be used to identify LRR-type RKs and RLPs required for
PAMP perception/responsiveness, even when the active purified
PAMP has not been defined.