ArticleScientific reports2017
A novel bi-domain plant defensin MtDef5 with potent broad-spectrum antifungal activity binds to multiple phospholipids and forms oligomers.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Cysteine-Rich Peptides in Food Systems: Structure, Sources, Functional Properties, Potential Applications, and Future Perspectives.Probiotics and antimicrobial proteins · 2026Review
- Selective α-Amylase Inhibition by Plant Defensins: Structural Determinants, Engineering Strategies, and Translational Prospects.Probiotics and antimicrobial proteins · 2026Review
- Characterization and Biofungicide Potential of a Novel Antifungal defensin, K4CBP6, from Solanum lycopersicum L.Probiotics and antimicrobial proteins · 2026Article
- Harnessing eCISs for precision phytomicrobiome engineering and biocontrol.FEMS microbiology reviews · 2026Review
- Modes of action and potential as a peptide-based biofungicide of a plant defensin MtDef4.Molecular plant pathology · 2024Article
- Transcriptome-Wide Identification and Expression Analysis of Genes Encoding Defense-Related Peptides ofJournal of fungi (Basel, Switzerland) · 2024Article
- Microbial- and Plant-Derived Bioactive Peptides and Their Applications against Foodborne Pathogens: Current Status and Future Prospects.International journal of microbiology · 2024Review
- Small Cationic Cysteine-Rich Defensin-Derived Antifungal Peptide Controls White Mold in Soybean.Journal of fungi (Basel, Switzerland) · 2023Article
- Plant defensin MtDef4-derived antifungal peptide with multiple modes of action and potential as a bio-inspired fungicide.Molecular plant pathology · 2023Article
- The γ-Core Motif Peptides of Plant AMPs as Novel Antimicrobials for Medicine and Agriculture.International journal of molecular sciences · 2022Review
- Article
- Defensin-lipid interactions in membrane targeting: mechanisms of action and opportunities for the development of antimicrobial and anticancer therapeutics.Biochemical Society transactions · 2022Review
- Use of Defensins to Develop Eco-Friendly Alternatives to Synthetic Fungicides to Control Phytopathogenic Fungi and Their Mycotoxins.Journal of fungi (Basel, Switzerland) · 2022Review
- Legume NCRs and nodule-specific defensins of actinorhizal plants-Do they share a common origin?PloS one · 2022Article
- Article
- A Novel Deoxynivalenol-Activated WheatJournal of fungi (Basel, Switzerland) · 2021Article
- Synthetic Oligopeptides Mimicking γ-Core Regions of Cysteine-Rich Peptides ofCurrent issues in molecular biology · 2021Article
- Antimicrobial Peptides and Their Applications in Biomedical Sector.Antibiotics (Basel, Switzerland) · 2021Review
- Plant Defensins from a Structural Perspective.International journal of molecular sciences · 2020Review
- Antifungal symbiotic peptide NCR044 exhibits unique structure and multifaceted mechanisms of action that confer plant protection.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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5 authors.
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Abstract
Defensins are cysteine-rich cationic antimicrobial peptides contributing to the innate immunity in plants. A unique gene encoding a highly cationic bi-domain defensin MtDef5 has been identified in a model legume Medicago truncatula. MtDef5 consists of two defensin domains of 50 amino acids each linked by a 7-amino acid peptide. It exhibits broad-spectrum antifungal activity against filamentous fungi at submicromolar concentrations. It rapidly permeabilizes the plasma membrane of the ascomycete fungi Fusarium graminearum and Neurospora crassa and induces accumulation of reactive oxygen species. It is internalized by these fungi, but uses spatially distinct modes of entry into these fungi. It co-localizes with cellular membranes, travels to nucleus and becomes dispersed in other subcellular locations. It binds to several membrane-resident phospholipids with preference for phosphatidylinositol monophosphates and forms oligomers. Mutations of the cationic amino acids present in the two γ-core motifs of this defensin that eliminate oligomerization also knockout its ability to induce membrane permeabilization and fungal growth arrest. MtDef5 is the first bi-domain plant defensin that exhibits potent broad-spectrum antifungal activity, recruits multiple membrane phospholipids and forms oligomers in their presence. These findings raise the possibility that MtDef5 might be useful as a novel antifungal agent in transgenic crops.
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