ArticlePloS one2014
Cathelicidins from the bullfrog Rana catesbeiana provides novel template for peptide antibiotic design.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 54 citations in OpenAlex.
- Functional characterization of HR-CATH2, a novel cathelicidin fromZoological research · 2026Article
- Genome Mining and Structural Study of Cathelicidins Across Chiroptera Species.Biochemistry research international · 2025Article
- Cathelicidins: Opportunities and Challenges in Skin Therapeutics and Clinical Translation.Antibiotics (Basel, Switzerland) · 2024Review
- Synergistic collaboration between AMPs and non-direct antimicrobial cationic peptides.Nature communications · 2024Article
- Discovery of Ll-CATH: a novel cathelicidin from the Chong'an Moustache Toad (Leptobrachium liui) with antibacterial and immunomodulatory activity.BMC veterinary research · 2024Article
- Multi-omics resources for the Australian southern stuttering frog (Mixophyes australis) reveal assorted antimicrobial peptides.Scientific reports · 2024Article
- Cathelicidin-HG Alleviates Sepsis-Induced Platelet Dysfunction by Inhibiting GPVI-Mediated Platelet Activation.Research (Washington, D.C.) · 2024Article
- Flow-Based Fmoc-SPPS Preparation and SAR Study of Cathelicidin-PY Reveals Selective Antimicrobial Activity.Molecules (Basel, Switzerland) · 2023Article
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- FM-CATH, A Novel Cathelicidin FromFrontiers in pharmacology · 2021Article
- Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing Peptides.Antibiotics (Basel, Switzerland) · 2020Article
- Cathelicidin-DM is an Antimicrobial Peptide fromACS omega · 2020Article
- Identification and characterization of two novel cathelicidins from the frogZoological research · 2019Article
- Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing.Scientific reports · 2018Article
- The first identified cathelicidin from tree frogs possesses anti-inflammatory and partial LPS neutralization activities.Amino acids · 2017Article
- Cathelicidin-trypsin inhibitor loop conjugate represents a promising antibiotic candidate with protease stability.Scientific reports · 2017Article
- Identification and Characterization of the First Cathelicidin from Sea Snakes with Potent Antimicrobial and Anti-inflammatory Activity and Special Mechanism.The Journal of biological chemistry · 2015Article
- Antimicrobial peptides in 2014.Pharmaceuticals (Basel, Switzerland) · 2015Review
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cathelicidins, a class of gene-encoded effector molecules of vertebrate innate immunity, provide a first line of defense against microbial invasions. Although cathelicidins from mammals, birds, reptiles and fishes have been extensively studied, little is known about cathelicidins from amphibians. Here we report the identification and characterization of two cathelicidins (cathelicidin-RC1 and cathelicidin-RC2) from the bullfrog Rana catesbeiana. The cDNA sequences (677 and 700 bp, respectively) encoding the two peptides were successfully cloned from the constructed lung cDNA library of R. catesbeiana. And the deduced mature peptides are composed of 28 and 33 residues, respectively. Structural analysis indicated that cathelicidin-RC1 mainly assumes an amphipathic alpha-helical conformation, while cathelicidin-RC2 could not form stable amphipathic structure. Antimicrobial and bacterial killing kinetic analysis indicated that the synthetic cathelicidin-RC1 possesses potent, broad-spectrum and rapid antimicrobial potency, while cathelicidin-RC2 exhibited very weak antimicrobial activity. Besides, the antimicrobial activity of cathelicidin-RC1 is salt-independent and highly stable. Scanning electron microscopy (SEM) analysis indicated that cathelicidin-RC1 kills microorganisms through the disruption of microbial membrane. Moreover, cathelicidin-RC1 exhibited low cytotoxic activity against mammalian normal or tumor cell lines, and low hemolytic activity against human erythrocytes. The potent, broad-spectrum and rapid antimicrobial activity combined with the salt-independence, high stability, low cytotoxic and hemolytic activities make cathelicidin-RC1 an ideal template for the development of novel peptide antibiotics.
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