ArticlePloS one2013
Structural and functional studies of a phosphatidic acid-binding antifungal plant defensin MtDef4: identification of an RGFRRR motif governing fungal cell entry.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers, 1 of them a synthesis that pooled it.
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Who cites it
71 citing papers in PubMed, 1 synthesis or guideline pooled it, 131 citations in OpenAlex.
- Defensins of Grasses: A Systematic Review.Biomolecules · 2020Pooled it
- Coumarin-Based Antifungal Leads: Design, Synthesis, Mechanistic Insights, and Synergistic Activity.Chemistry & biodiversity · 2026Article
- Article
- Brilacidin's Antifungal Mechanism: Insights from Lipid Membrane Models.Antibiotics (Basel, Switzerland) · 2026Article
- Antifungal peptides: From modes of action to synergistic and immunologic potential.Cell stress · 2026Article
- Molecular mechanisms and genetic regulation of self-incompatibility in flowering plants: implications for crop improvement and evolutionary biology.Plant molecular biology · 2025Review
- Antifungal Peptides SmAPAntibiotics (Basel, Switzerland) · 2025Article
- Peptides from plants and microorganisms: a defense strategy for biotic and abiotic stresses.Frontiers in plant science · 2025Review
- Discovery of Five Classes of Bacterial Defensins: Ancestral Precursors of Defensins from Eukarya?ACS omega · 2024Article
- Plant peptides - redefining an area of ribosomally synthesized and post-translationally modified peptides.Natural product reports · 2024Review
- Modes of action and potential as a peptide-based biofungicide of a plant defensin MtDef4.Molecular plant pathology · 2024Article
- Fighting pathogenic yeasts with plant defensins and anti-fungal proteins from fungi.Applied microbiology and biotechnology · 2024Review
- Nature-inspired peptide of MtDef4 C-terminus tail enables protein delivery in mammalian cells.Scientific reports · 2024Article
- Hyperpolarisation of Mitochondrial Membranes Is a Critical Component of the Antifungal Mechanism of the Plant Defensin, Ppdef1.Journal of fungi (Basel, Switzerland) · 2024Article
- Production of Plant Proteins and Peptides with Pharmacological Potential.Advances in biochemical engineering/biotechnology · 2024Review
- The Plant Defensin Ppdef1 Is a Novel Topical Treatment for Onychomycosis.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
- Novel insights into plant defensin ingestion induced metabolic responses in the polyphagous insect pest Helicoverpa armigera.Scientific reports · 2023Article
- Article
- The γ-Core Motif Peptides of Plant AMPs as Novel Antimicrobials for Medicine and Agriculture.International journal of molecular sciences · 2022Review
11 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MtDef4 is a 47-amino acid cysteine-rich evolutionary conserved defensin from a model legume Medicago truncatula. It is an apoplast-localized plant defense protein that inhibits the growth of the ascomycetous fungal pathogen Fusarium graminearum in vitro at micromolar concentrations. Little is known about the mechanisms by which MtDef4 mediates its antifungal activity. In this study, we show that MtDef4 rapidly permeabilizes fungal plasma membrane and is internalized by the fungal cells where it accumulates in the cytoplasm. Furthermore, analysis of the structure of MtDef4 reveals the presence of a positively charged γ-core motif composed of β2 and β3 strands connected by a positively charged RGFRRR loop. Replacement of the RGFRRR sequence with AAAARR or RGFRAA abolishes the ability of MtDef4 to enter fungal cells, suggesting that the RGFRRR loop is a translocation signal required for the internalization of the protein. MtDef4 binds to phosphatidic acid (PA), a precursor for the biosynthesis of membrane phospholipids and a signaling lipid known to recruit cytosolic proteins to membranes. Amino acid substitutions in the RGFRRR sequence which abolish the ability of MtDef4 to enter fungal cells also impair its ability to bind PA. These findings suggest that MtDef4 is a novel antifungal plant defensin capable of entering into fungal cells and affecting intracellular targets and that these processes are mediated by the highly conserved cationic RGFRRR loop via its interaction with PA.
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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.