ArticleMolecular plant pathology2014
A dimeric PR-1-type pathogenesis-related protein interacts with ToxA and potentially mediates ToxA-induced necrosis in sensitive wheat.
Article in Molecular plant pathology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.
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Who cites it
37 citing papers in PubMed, 1 synthesis or guideline pooled it, 101 citations in OpenAlex.
- Pathogenesis-related protein 10 in resistance to biotic stress: progress in elucidating functions, regulation and modes of action.Frontiers in plant science · 2023Pooled it
- A PR1-Like Protein Stabilizes a Barwin-Like Protein to Enhance Wheat Resistance to Leaf Rust.Plant, cell & environment · 2026Article
- Functional evaluation of pathogenesis-related protein-1 (PR1) genes in mung bean (Vigna radiata) response to Pythium myriotylum.BMC genomics · 2025Article
- Omic characterisation of multi-component defences against the necrotrophic pathogen Pyrenophora tritici-repentis in wheat.Plant biology (Stuttgart, Germany) · 2025Article
- Analysis and comparison of the bacterial σ54 regulon: Evidence of phylogenetic trends in gene regulation.PloS one · 2025Article
- Unveiling the dynamic expression of PR-1 during Musa spp. infection by Fusarium oxysporum fsp. Cubense: a cloning and characterization study.Molecular biology reports · 2024Article
- Enhancement of broad-spectrum disease resistance in wheat through key genes involved in systemic acquired resistance.Frontiers in plant science · 2024Review
- Dual functionality of pathogenesis-related proteins: defensive role in plants versus immunosuppressive role in pathogens.Frontiers in plant science · 2024Article
- The function of plant PR1 and other members of the CAP protein superfamily in plant-pathogen interactions.Molecular plant pathology · 2023Review
- QTL detection and candidate gene analysis of grape white rot resistance by interspecific grape (Horticulture research · 2023Article
- Article
- Pathogenesis-related protein 1 suppresses oomycete pathogen by targeting against AMPK kinase complex.Journal of advanced research · 2023Article
- Molecular, Histological and Histochemical Responses of Banana Cultivars Challenged withPlants (Basel, Switzerland) · 2022Article
- Isolation and Characterization of a Novel Pathogenesis-Related Protein-1 Gene (Plants (Basel, Switzerland) · 2022Article
- Genome-Wide Characterization and Expression Analysis of Pathogenesis-Related 1 (International journal of molecular sciences · 2022Article
- The Parastagonospora nodorum necrotrophic effector SnTox5 targets the wheat gene Snn5 and facilitates entry into the leaf mesophyll.The New phytologist · 2022Article
- Pathogens pulling the strings: Effectors manipulating salicylic acid and phenylpropanoid biosynthesis in plants.Molecular plant pathology · 2021Review
- Short Peptides Make a Big Difference: The Role of Botany-Derived AMPs in Disease Control and Protection of Human Health.International journal of molecular sciences · 2021Review
- Remote homology clustering identifies lowly conserved families of effector proteins in plant-pathogenic fungi.Microbial genomics · 2021Article
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A dimeric PR-1-type pathogenesis-related protein (PR-1-5), recently identified in wheat, was found to interact with Stagonospora nodorum ToxA in both yeast two-hybrid and co-immunoprecipitation assays. Site-specific mutational analyses revealed that the RGD motif of ToxA is not targeted by PR-1-5, whereas two surface-exposed asparagine residues are essential for the interaction: the N102 residue of the turning loop between β2 and β3 in ToxA and the N141 residue of the turning loop between βC and βD in PR-1-5. Recombinant PR-1-5 and ToxA mutant proteins carrying alanine substitutions at the interacting sites were expressed in Pichia pastoris, together with the wild-type proteins. Native polyacrylamide gel electrophoresis (PAGE) confirmed that the PR-1-5-N141A mutant retains the ability to form dimers. Plant assays indicated that the ToxA-N102A mutant fails to induce necrosis, whereas the PR-1-5-N141A mutant is impaired in the 'necrosis-promoting' activity shown by the wild-type PR-1-5 when co-infiltrated with ToxA in sensitive wheat. Reverse transcriptase-polymerase chain reaction and Western blot analyses revealed that the native PR-1-5 protein is differentially expressed between ToxA-sensitive and ToxA-insensitive wheat lines in response to ToxA treatment. These results suggest that PR-1-5 is a potential target of ToxA and the site-specific interaction between PR-1-5 and ToxA may mediate ToxA-induced necrosis in sensitive wheat.
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