ArticlePlant physiology2004
Differential antifungal and calcium channel-blocking activity among structurally related plant defensins.
Article in Plant physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers, 1 of them a synthesis that pooled it.
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Who cites it
91 citing papers in PubMed, 1 synthesis or guideline pooled it, 220 citations in OpenAlex.
- Defensins of Grasses: A Systematic Review.Biomolecules · 2020Pooled it
- Phage Display Derived Antibodies Against Antimicrobial Peptide FsPDF2 Reveal Stress Response in European Beech.Plant biotechnology journal · 2026Article
- Identification of the Plant Defensin (MsPDF) Gene Family inPlants (Basel, Switzerland) · 2025Article
- Article
- Antimicrobial Plant Peptides: Structure, Classification, Mechanism and Therapeutic Potential.Current topics in medicinal chemistry · 2025Review
- Plant Antimicrobial Peptides and Their Main Families and Roles: A Review of the Literature.Current issues in molecular biology · 2024Review
- Complex of Defense Polypeptides of Wheatgrass (Plants (Basel, Switzerland) · 2024Article
- Characterization and functional analysis of gerberaaBIOTECH · 2024Article
- 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
- Hyperpolarisation of Mitochondrial Membranes Is a Critical Component of the Antifungal Mechanism of the Plant Defensin, Ppdef1.Journal of fungi (Basel, Switzerland) · 2024Article
- Genome-wide identification and analysis of a cotton secretome reveals its role in resistance against Verticillium dahliae.BMC biology · 2023Article
- Plant defensin MtDef4-derived antifungal peptide with multiple modes of action and potential as a bio-inspired fungicide.Molecular plant pathology · 2023Article
- In silico characterization of cysteine-stabilized αβ defensins from neglected unicellular microeukaryotes.BMC microbiology · 2023Article
- Article
- The potential of plant proteins as antifungal agents for agricultural applications.Synthetic and systems biotechnology · 2022Review
- Novel Polyhydroquinoline-Hydrazide-Linked Schiff's Base Derivatives: Multistep Synthesis, Antimicrobial, and Calcium-Channel-Blocking Activities.Antibiotics (Basel, Switzerland) · 2022Article
- 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
- Calcium nutrition nanoagent rescues tomatoes from mosaic virus disease by accelerating calcium transport and activating antiviral immunity.Frontiers in plant science · 2022Article
31 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Plant defensins are a family of small Cys-rich antifungal proteins that play important roles in plant defense against invading fungi. Structures of several plant defensins share a Cys-stabilized alpha/beta-motif. Structural determinants in plant defensins that govern their antifungal activity and the mechanisms by which they inhibit fungal growth remain unclear. Alfalfa (Medicago sativa) seed defensin, MsDef1, strongly inhibits the growth of Fusarium graminearum in vitro, and its antifungal activity is markedly reduced in the presence of Ca(2+). By contrast, MtDef2 from Medicago truncatula, which shares 65% amino acid sequence identity with MsDef1, lacks antifungal activity against F. graminearum. Characterization of the in vitro antifungal activity of the chimeras containing portions of the MsDef1 and MtDef2 proteins shows that the major determinants of antifungal activity reside in the carboxy-terminal region (amino acids 31-45) of MsDef1. We further define the active site by demonstrating that the Arg at position 38 of MsDef1 is critical for its antifungal activity. Furthermore, we have found for the first time, to our knowledge, that MsDef1 blocks the mammalian L-type Ca(2+) channel in a manner akin to a virally encoded and structurally unrelated antifungal toxin KP4 from Ustilago maydis, whereas structurally similar MtDef2 and the radish (Raphanus sativus) seed defensin Rs-AFP2 fail to block the L-type Ca(2+) channel. From these results, we speculate that the two unrelated antifungal proteins, KP4 and MsDef1, have evolutionarily converged upon the same molecular target, whereas the two structurally related antifungal plant defensins, MtDef2 and Rs-AFP2, have diverged to attack different targets in fungi.
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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.