Abstract
To ward off pathogens and pests, plants use a sophisticated immune system. They use pattern-recognition receptors (PRRs), as well as nucleotide-binding and leucine-rich repeat (NB-LRR) domains, for detecting nonindigenous molecular signatures from pathogens. Plant PRRs induce local and systemic immunity. Plasma-membrane-localized PRRs are the main components of multiprotein complexes having additional transmembrane and cytosolic kinases. Topical research involving proteins and their interactive partners, along with transcriptional and posttranscriptional regulation, has extended our understanding of R-gene-mediated plant immunity. The unique LRR domain conformation helps in the best utilization of a surface area and essentially mediates protein–protein interactions. Genome-wide analyses of inter- and intraspecies PRRs and NB-LRRs offer innovative information about their working and evolution. We reviewed plant immune responses with relevance to PRRs and NB-LRRs. This article focuses on the significant functional diversity, pathogen-recognition mechanisms, and subcellular compartmentalization of plant PRRs and NB-LRRs. We highlight the potential biotechnological application of PRRs and NB-LRRs to enhance broad-spectrum disease resistance in crops.
Highlights
Like animals, plant immune responses depend on cellular events, but plants possess a pathogen-recognition system to balance the absence of an adaptive immune system [1,2,3]
We summarize the roles of pattern-recognition receptors (PRRs) and nucleotide-binding leucine-rich repeats (NB-leucine-rich repeats (LRR)) in connection with PAMP-triggered immunity (PTI) and Effector-Triggered Immunity (ETI) for plant defense
Cloned NB-LRR genes can facilitate their use in agriculture as molecular markers or by transgenic means
Summary
Plant immune responses depend on cellular events, but plants possess a pathogen-recognition system to balance the absence of an adaptive immune system [1,2,3]. Previous studies showed that PAMPs are recognized with the help of PRRs (Table 1) [27] This PAMP recognition was well-described in the case of the Arabidopsis receptor kinase FLS2 (Flagellin Sensing 2) that directly binds with bacterial flagellin and forms a signaling complex [28,29,30]. CERK1 (Chitin Elicitor Receptor Kinase 1) has a role in identifying bacterial peptidoglycans (PGNs) for mediating immunity in Arabidopsis thaliana [75] From these facts, we point out that the binding of CERK with chitin or PGNs is, the ability to perceive completely different pathogens, i.e., fungi or bacteria. A similar activation mechanism in Arabidopsis was observed for RLK–LRR–BRI1 (Brassinosteroid Insensitive 1) and BAK1/SERK1 (somatic embryogenesis receptor kinases) [89] This proposes the involvement of many LRR-containing RLKs (and RLPs) in the same heterodimeric complexes with BAK1 or related SERK proteins [90]
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