ArticleThe Plant journal : for cell and molecular biology2012
A tomato LysM receptor-like kinase promotes immunity and its kinase activity is inhibited by AvrPtoB.
Article in The Plant journal : for cell and molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 142 citations in OpenAlex.
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- Chitin Soil Amendment Triggers Systemic Plant Disease Resistance Through Enhanced Pattern-Triggered Immunity.Plant biotechnology journal · 2025Article
- Transcriptome analysis provides new insights into the resistance of pepper to Phytophthora capsici infection.BMC genomics · 2025Article
- Plant Immunity: At the Crossroads of Pathogen Perception and Defense Response.Plants (Basel, Switzerland) · 2024Review
- Transmembrane proteins in grape immunity: current knowledge and methodological advances.Frontiers in plant science · 2024Review
- The Imperative Use of Bacillus Consortium and Quercetin Contributes to Suppress Fusarium Wilt Disease by Direct Antagonism and Induced Resistance.Microorganisms · 2023Article
- Multiple host targets ofbioRxiv : the preprint server for biology · 2023Article
- Tomato LysM receptor kinase 4 mediates chitin-elicited fungal resistance in both leaves and fruit.Horticulture research · 2023Article
- Loss of function of the bHLH transcription factor Nrd1 in tomato enhances resistance to Pseudomonas syringae.Plant physiology · 2022Article
- In silico integration of disease resistance QTL, genes and markers with theMolecular breeding : new strategies in plant improvement · 2022Article
- Comparative Transcriptome and Metabolome Analysis of Resistant and SusceptibleFrontiers in plant science · 2022Article
- LysM receptors in Coffea arabica: Identification, characterization, and gene expression in response to Hemileia vastatrix.PloS one · 2022Article
- Toward Understanding the Molecular Recognition of Fungal Chitin and Activation of the Plant Defense Mechanism in Horticultural Crops.Molecules (Basel, Switzerland) · 2021Review
- Transcriptome analysis of Clavibacter michiganensis subsp. michiganensis-infected tomatoes: a role of salicylic acid in the host response.BMC plant biology · 2021Article
- Regulation of theMicroorganisms · 2021Review
- Crosstalk between Ubiquitination and Other Post-translational Protein Modifications in Plant Immunity.Plant communications · 2020Review
- Receptor-Like Kinases Sustain Symbiotic Scrutiny.Plant physiology · 2020Review
- Diversity, Function and Regulation of Cell Surface and Intracellular Immune Receptors inPlants (Basel, Switzerland) · 2020Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Resistance in tomato (Solanum lycopersicum) to infection by Pseudomonas syringae involves both detection of pathogen-associated molecular patterns (PAMPs) and recognition by the host Pto kinase of pathogen effector AvrPtoB which is translocated into the host cell and interferes with PAMP-triggered immunity (PTI). The N-terminal portion of AvrPtoB is sufficient for its virulence activity and for recognition by Pto. An amino acid substitution in AvrPtoB, F173A, abolishes these activities. To investigate the mechanisms of AvrPtoB virulence, we screened for tomato proteins that interact with AvrPtoB and identified Bti9, a LysM receptor-like kinase. Bti9 has the highest amino acid similarity to Arabidopsis CERK1 among the tomato LysM receptor-like kinases (RLKs) and belongs to a clade containing three other tomato proteins, SlLyk11, SlLyk12, and SlLyk13, all of which interact with AvrPtoB. The F173A substitution disrupts the interaction of AvrPtoB with Bti9 and SlLyk13, suggesting that these LysM-RLKs are its virulence targets. Two independent tomato lines with RNAi-mediated reduced expression of Bti9 and SlLyk13 were more susceptible to P. syringae. Bti9 kinase activity was inhibited in vitro by the N-terminal domain of AvrPtoB in an F173-dependent manner. These results indicate Bti9 and/or SlLyk13 play a role in plant immunity and the N-terminal domain of AvrPtoB may have evolved to interfere with their kinase activity. Finally, we found that Bti9 and Pto interact with AvrPtoB in a structurally similar although not identical fashion, suggesting that Pto may have evolved as a molecular mimic of LysM-RLK kinase domains.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.