ArticleScientific reports2015
Identification of a novel cathelicidin antimicrobial peptide from ducks and determination of its functional activity and antibacterial mechanism.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 53 citations in OpenAlex.
- Forensic application of CAMP expression for the determination of wound vitality in human compressed neck skin.International journal of legal medicine · 2026Article
- Cathelicidins: Opportunities and Challenges in Skin Therapeutics and Clinical Translation.Antibiotics (Basel, Switzerland) · 2024Review
- Cathelicidin Antimicrobial Peptide Levels in Atherosclerosis and Myocardial Infarction in Mice and Human.International journal of molecular sciences · 2024Article
- Anticancer peptides as novel immunomodulatory therapeutic candidates for cancer treatment.Exploration of targeted anti-tumor therapy · 2024Review
- Transcriptome analysis of Corvus splendens reveals a repertoire of antimicrobial peptides.Scientific reports · 2023Article
- Regulation of Cathelicidin Antimicrobial Peptide (CAMP) Gene Expression by TNFα and cfDNA in Adipocytes.International journal of molecular sciences · 2023Article
- The Properties of Linezolid, Rifampicin, and Vancomycin, as Well as the Mechanism of Action of Pentamidine, Determine Their Synergy against Gram-Negative Bacteria.International journal of molecular sciences · 2023Article
- Biologically Active Peptides from Venoms: Applications in Antibiotic Resistance, Cancer, and Beyond.International journal of molecular sciences · 2022Review
- Novel Alligator Cathelicidin As-CATH8 Demonstrates Anti-Infective Activity against Clinically Relevant and Crocodylian Bacterial Pathogens.Antibiotics (Basel, Switzerland) · 2022Article
- Antimicrobial Peptides: An Update on Classifications and Databases.International journal of molecular sciences · 2021Review
- CBP22, a Novel Bacteriocin Isolated fromMediators of inflammation · 2021Article
- Avian host defense cathelicidins: structure, expression, biological functions, and potential therapeutic applications.Poultry science · 2020Review
- Lactoferrin Functionalized Biomaterials: Tools for Prevention of Implant-Associated Infections.Antibiotics (Basel, Switzerland) · 2020Review
- Pseudonajide peptide derived from snake venom alters cell envelope integrity interfering on biofilm formation in Staphylococcus epidermidis.BMC microbiology · 2020Article
- Molecular characterization, mRNA gene expression, and antimicrobial activity of 2 new cathelicidin genes in goose.Poultry science · 2020Article
- The Critical Role of Tryptophan in the Antimicrobial Activity and Cell Toxicity of the Duck Antimicrobial Peptide DCATH.Frontiers in microbiology · 2020Article
- Substitution of lysine for isoleucine at the center of the nonpolar face of the antimicrobial peptide, piscidin-1, leads to an increase in the rapidity of bactericidal activity and a reduction in toxicity.Infection and drug resistance · 2019Article
- Snake Venom Cathelicidins as Natural Antimicrobial Peptides.Frontiers in pharmacology · 2019Review
- Identification and Characterization of Novel Antimicrobial Peptide from Hippocampus comes by In Silico and Experimental Studies.Marine biotechnology (New York, N.Y.) · 2018Article
- Identification of novel antimicrobial peptide from Asian sea bass (Lates calcarifer) by in silico and activity characterization.PloS one · 2018Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The family of antimicrobial peptide, cathelicidins, which plays important roles against infections in animals, has been identified from many species. Here, we identified a novel avian cathelicidin ortholog from ducks and named dCATH. The cDNA sequence of dCATH encodes a predicted 146-amino-acid polypeptide composed of a 17-residue signal peptide, a 109-residue conserved cathelin domain and a 20-residue mature peptide. Phylogenetic analysis demonstrated that dCATH is highly divergent from other avian peptides. The α-helical structure of the peptide exerted strong antimicrobial activity against a broad range of bacteria in vitro, with most minimum inhibitory concentrations in the range of 2 to 4 μM. Moreover, dCATH also showed cytotoxicity, lysing 50% of mammalian erythrocytes in the presence or absence of 10% fetal calf serum at concentrations of 32 μM or 20 μM and killing 50% HaCaT cells at a concentration of 10 μM. The effects on bacterial outer and inner membranes, as examined by scanning electron microscope and transmission electron microscopy, indicate that dCATH kills microbial cells by increasing permeability, causing a loss of membrane integrity.
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