ArticleMolecular plant2015
A Host KH RNA-Binding Protein Is a Susceptibility Factor Targeted by an RXLR Effector to Promote Late Blight Disease.
Article in Molecular plant, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 77 citations in OpenAlex.
- Potato StRWA2 recruits the E3 ligase StSNIPER2 to destabilize NLRs and promoteHorticulture research · 2026Article
- Mutations in the signal peptide of effector gene Pi04314 contribute to the adaptive evolution of the Phytophthora infestans.BMC ecology and evolution · 2025Article
- Nucleic acid-binding KH domain proteins influence a spectrum of biological pathways including as part of membrane-localized complexes.Journal of structural biology: X · 2024Article
- Potato: from functional genomics to genetic improvement.Molecular horticulture · 2024Review
- Chloroplast protein StFC-II was manipulated by aHorticulture research · 2024Article
- Fine mapping a QTL for BYDV-PAV resistance in maize.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2024Article
- Phytophthora infestans RXLR effector Pi23014 targets host RNA-binding protein NbRBP3a to suppress plant immunity.Molecular plant pathology · 2024Article
- HemibiotrophicPlants (Basel, Switzerland) · 2023Article
- Nuclear effectors of plant pathogens: Distinct strategies to be one step ahead.Molecular plant pathology · 2023Review
- Exploiting breakdown in nonhost effector-target interactions to boost host disease resistance.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The First Whole Genome Sequence Discovery of the Devastating FungusJournal of fungi (Basel, Switzerland) · 2022Article
- Phytophthora infestans RXLR effector Pi04089 perturbs diverse defense-related genes to suppress host immunity.BMC plant biology · 2021Article
- Multiple Mechanisms Drive the Evolutionary Adaptation ofJournal of fungi (Basel, Switzerland) · 2021Article
- Host-interactor screens of Phytophthora infestans RXLR proteins reveal vesicle trafficking as a major effector-targeted process.The Plant cell · 2021Article
- Review
- Article
- Importin-αs are required for the nuclear localization and function of the Plasmopara viticola effector PvAVH53.Horticulture research · 2021Article
- Fungal effectors, the double edge sword of phytopathogens.Current genetics · 2021Review
- Comparative transcriptome analysis reveals resistant and susceptible genes in tobacco cultivars in response to infection by Phytophthora nicotianae.Scientific reports · 2021Article
- Comparative transcriptome analysis ofPeerJ · 2021Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Plant pathogens deliver effector proteins that alter host processes to create an environment conducive to colonization. Attention has focused on identifying the targets of effectors and how their manipulation facilitates disease. RXLR effector Pi04089 from the potato blight pathogen Phytophthora infestans accumulates in the host nucleus and enhances colonization when transiently expressed in planta. Its nuclear localization is required for enhanced P. infestans colonization. Pi04089 interacts in yeast and in planta with a putative potato K-homology (KH) RNA-binding protein, StKRBP1. Co-localization of Pi04089 and StKRBP1, and bimolecular fluorescence complementation between them, indicate they associate at nuclear speckles. StKRBP1 protein levels increased when it was co-expressed with Pi04089. Indeed, such accumulation of StKRBP1 was observed also on the first day of leaf colonization by the pathogen. Remarkably, overexpression of StKRBP1 significantly enhances P. infestans infection. Mutation of the nucleotide-binding motif GxxG to GDDG in all three KH domains of StKRBP1 abolishes its interaction with Pi04089, its localization to nuclear speckles, and its increased accumulation when co-expressed with the effector. Moreover, the mutant StKRBP1 protein no longer enhances leaf colonization by P. infestans, implying that nucleotide binding is likely required for this activity. We thus argue that StKRBP1 can be regarded as a susceptibility factor, as its activity is beneficial to the pathogen.
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