ArticleThe Journal of biological chemistry2010
Insight into invertebrate defensin mechanism of action: oyster defensins inhibit peptidoglycan biosynthesis by binding to lipid II.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 139 citations in OpenAlex.
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- Hijacking the Electron Train: Menaquinone-Binding Antimicrobial Peptides.Chembiochem : a European journal of chemical biology · 2025Review
- Article
- Cross-talk and mutual shaping between the immune system and the microbiota during an oyster's life.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024Review
- Peptide Dendrimer-Based Antibacterial Agents: Synthesis and Applications.ACS infectious diseases · 2024Review
- Specific Cationic Antimicrobial Peptides Enhance the Recovery of Low-Load QuiescentInternational journal of molecular sciences · 2023Article
- Marine Invertebrate Antimicrobial Peptides and Their Potential as Novel Peptide Antibiotics.Marine drugs · 2023Review
- Mechanisms and regulation of defensins in host defense.Signal transduction and targeted therapy · 2023Review
- Insect Antimicrobial Peptides: Advancements, Enhancements and New Challenges.Antibiotics (Basel, Switzerland) · 2023Review
- Immunostimulation ofPeerJ · 2023Article
- Functional Diversification of Oyster Big Defensins Generates Antimicrobial Specificity and Synergy against Members of the Microbiota.Marine drugs · 2022Article
- Antimicrobial peptides from freshwater invertebrate species: potential for future applications.Molecular biology reports · 2022Review
- The cecropin-prophenoloxidase regulatory mechanism is a cross-species physiological function in mosquitoes.iScience · 2022Article
- Defensin-lipid interactions in membrane targeting: mechanisms of action and opportunities for the development of antimicrobial and anticancer therapeutics.Biochemical Society transactions · 2022Review
- Real-Time Fluorescence Microscopy on LivingInternational journal of molecular sciences · 2022Article
- Potent bactericidal activity of reduced cryptdin-4 derived from its hydrophobicity and mediated by bacterial membrane disruption.Amino acids · 2022Article
- Large-Scale Plasma Peptidomic Profiling Reveals a Novel, Nontoxic,Marine drugs · 2021Article
- Comparison of a Short Linear Antimicrobial Peptide with Its Disulfide-Cyclized and Cyclotide-Grafted Variants against Clinically Relevant Pathogens.Microorganisms · 2021Article
10 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Three oyster defensin variants (Cg-Defh1, Cg-Defh2, and Cg-Defm) were produced as recombinant peptides and characterized in terms of activities and mechanism of action. In agreement with their spectrum of activity almost specifically directed against Gram-positive bacteria, oyster defensins were shown here to be specific inhibitors of a bacterial biosynthesis pathway rather than mere membrane-active agents. Indeed, at lethal concentrations, the three defensins did not compromise Staphylococcus aureus membrane integrity but inhibited the cell wall biosynthesis as indicated by the accumulation of the UDP-N-acetylmuramyl-pentapeptide cell wall precursor. In addition, a combination of antagonization assays, thin layer chromatography, and surface plasmon resonance measurements showed that oyster defensins bind almost irreversibly to the lipid II peptidoglycan precursor, thereby inhibiting the cell wall biosynthesis. To our knowledge, this is the first detailed analysis of the mechanism of action of antibacterial defensins produced by invertebrates. Interestingly, the three defensins, which were chosen as representative of the oyster defensin molecular diversity, bound differentially to lipid II. This correlated with their differential antibacterial activities. From our experimental data and the analysis of oyster defensin sequence diversity, we propose that oyster defensin activity results from selective forces that have conserved residues involved in lipid II binding and diversified residues at the surface of oyster defensins that could improve electrostatic interactions with the bacterial membranes.
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