ArticleMolecular plant pathology2022
Decoy engineering of the receptor-like cytoplasmic kinase StPBS1 to defend against virus infection in potato.
Article in Molecular plant pathology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Harnessing Natural Diversity and Rational Design for Enhanced Plant Immunity.Plant, cell & environment · 2026Review
- All Roads Lead to Rome: Pathways to Engineering Disease Resistance in Plants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Bioengineering secreted proteases converts divergent Rcr3 orthologs and paralogs into extracellular immune co-receptors.The Plant cell · 2024Article
- Soybean-Phakopsora pachyrhizi interactions: towards the development of next-generation disease-resistant plants.Plant biotechnology journal · 2024Review
- Engineering plant immune circuit: walking to the bright future with a novel toolbox.Plant biotechnology journal · 2023Review
- Decoy engineering of the receptor-like cytoplasmic kinase StPBS1 to defend against virus infection in potato.Molecular plant pathology · 2022Article
Corrections and comments
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Authors and funding
14 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Potato virus Y (PVY) is an important pathogen of potato (Solanum tuberosum). Although the PBS1-RPS5 immune system is well documented in Arabidopsis thaliana, it has not been reported in potato. In Arabidopsis, the bacterial effector AvrPphB cleaves AtPBS1 to trigger an immune response. Here, we show that the AvrPphB-triggered immune response is mediated by StPBS1, a close homologue of AtPBS1 in potato. However, downstream signalling of StPBS1 was mediated by unknown resistance (R) proteins other than potato orthologues of AtRPS5 and HvPBR1, which is important for HvPBS1 signalling in barley. Immune signalling of StPBS1 is mediated by the AvrPphB C-terminal cleavage domain and an STKPQ motif, in contrast to AtPBS1-mediated immunity in which both AvrPphB cleavage fragments and an SEMPH motif are essential. The cleavage sequence of AvrPphB in StPBS1 was replaced with that of the PVY NIa-Pro protease to obtain StPBS1
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