ArticlePLoS pathogens2013
The tomato Prf complex is a molecular trap for bacterial effectors based on Pto transphosphorylation.
Article in PLoS pathogens, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 62 citations in OpenAlex.
- Harnessing Natural Diversity and Rational Design for Enhanced Plant Immunity.Plant, cell & environment · 2026Review
- Role of Plasmodesmata During Plant-Pathogen Interactions.The plant pathology journal · 2026Review
- A dominant-negative avirulence effector of the barley powdery mildew fungus provides mechanistic insight into barley MLA immune receptor activation.Journal of experimental botany · 2023Article
- Dynamic changes of the Prf/Pto tomato resistance complex following effector recognition.Nature communications · 2023Article
- Distinct Phyllosphere Microbiome of Wild Tomato Species in Central Peru upon Dysbiosis.Microbial ecology · 2023Article
- Effector-Dependent and -Independent Molecular Mechanisms of Soybean-Microbe Interaction.International journal of molecular sciences · 2022Review
- Thirty years of resistance: Zig-zag through the plant immune system.The Plant cell · 2022Review
- Pseudomonas syringae effector HopZ3 suppresses the bacterial AvrPto1-tomato PTO immune complex via acetylation.PLoS pathogens · 2021Article
- What the Wild Things Do: Mechanisms of Plant Host Manipulation by Bacterial Type III-Secreted Effector Proteins.Microorganisms · 2021Review
- Diversity, Function and Regulation of Cell Surface and Intracellular Immune Receptors inPlants (Basel, Switzerland) · 2020Review
- Plant STAND P-loop NTPases: a current perspective of genome distribution, evolution, and function : Plant STAND P-loop NTPases: genomic organization, evolution, and molecular mechanism models contribute broadly to plant pathogen defense.Molecular genetics and genomics : MGG · 2018Review
- Behind the lines-actions of bacterial type III effector proteins in plant cells.FEMS microbiology reviews · 2016Review
- Comparative analysis of plant immune receptor architectures uncovers host proteins likely targeted by pathogens.BMC biology · 2016Article
- PBL13 Is a Serine/Threonine Protein Kinase That Negatively Regulates Arabidopsis Immune Responses.Plant physiology · 2015Article
- Nuclear processes associated with plant immunity and pathogen susceptibility.Briefings in functional genomics · 2015Review
- The N-terminal domain of the tomato immune protein Prf contains multiple homotypic and Pto kinase interaction sites.The Journal of biological chemistry · 2015Article
- Pto kinase binds two domains of AvrPtoB and its proximity to the effector E3 ligase determines if it evades degradation and activates plant immunity.PLoS pathogens · 2014Article
- Identification of post-translational modifications of plant protein complexes.Journal of visualized experiments : JoVE · 2014Article
- Improving crop disease resistance: lessons from research on Arabidopsis and tomato.Frontiers in plant science · 2014Review
- Proteomics of effector-triggered immunity (ETI) in plants.Virulence · 2014Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The major virulence strategy of phytopathogenic bacteria is to secrete effector proteins into the host cell to target the immune machinery. AvrPto and AvrPtoB are two such effectors from Pseudomonas syringae, which disable an overlapping range of kinases in Arabidopsis and Tomato. Both effectors target surface-localized receptor-kinases to avoid bacterial recognition. In turn, tomato has evolved an intracellular effector-recognition complex composed of the NB-LRR protein Prf and the Pto kinase. Structural analyses have shown that the most important interaction surface for AvrPto and AvrPtoB is the Pto P+1 loop. AvrPto is an inhibitor of Pto kinase activity, but paradoxically, this kinase activity is a prerequisite for defense activation by AvrPto. Here using biochemical approaches we show that disruption of Pto P+1 loop stimulates phosphorylation in trans, which is possible because the Pto/Prf complex is oligomeric. Both P+1 loop disruption and transphosphorylation are necessary for signalling. Thus, effector perturbation of one kinase molecule in the complex activates another. Hence, the Pto/Prf complex is a sophisticated molecular trap for effectors that target protein kinases, an essential aspect of the pathogen's virulence strategy. The data presented here give a clear view of why bacterial virulence and host recognition mechanisms are so often related and how the slowly evolving host is able to keep pace with the faster-evolving pathogen.
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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.