Abstract
We identified two antimicrobial peptides (AMPs) with similarity to moronecidin in Antarctic fishes. The characteristics of both AMPs were determined using moronecidin as a control. Moronecidin, which was first isolated from hybrid striped bass, is highly salt-resistant, and possesses broad-spectrum activity against various microbes. The moronecidin-like peptide from Notothenia coriiceps exhibited a narrower spectrum of activity and a higher salt sensitivity than moronecidin. The AMP from Parachaenichthys charcoti exhibited similar antimicrobial activity to moronecidin, and similar salt sensitivity. In an experiment to identify toxic effects, both of the moronecidin-like peptides from the Antarctic fishes exhibited lower hemolytic activity than moronecidin. In spite of its low toxicity, the AMP from N. coriiceps is unlikely to be considered as a candidate for antibiotic development, owing to its narrow spectrum of activity and high salt sensitivity. In contrast, the high salt resistance and broad-spectrum activity of the AMP from P. charcoti could be more advantageous for clinical use than moronecidin, since it could kill bacteria under physiological conditions with low toxicity. A further comparison of these two AMPs from Antarctic fishes with other AMPs could help to reduce the toxicity of AMPs for clinical use.
Highlights
Antimicrobial agents have defeated many infectious diseases and have improved public health significantly
Genes encoding moronecidin-like peptides in antarctic fishes
To detect piscidin homologs in Antarctic fishes, we investigated the genome of N. coriiceps using the BlastP tool, and we identified a gene encoding a moronecidin-like peptide with NCBI accession number XP_010768425.1
Summary
Antimicrobial agents have defeated many infectious diseases and have improved public health significantly. AMPs have drawbacks; these include instability, hemolytic activity, salt sensitivity, toxicity toward eukaryotic cells, susceptibility to proteolysis, and a higher cost of production compared with conventional antibiotics [2, 9, 10]. In spite of their drawbacks, some AMPs from the pool of thousands of natural peptides have been developed and validated as therapeutic agents [9,10,11]. Moronecidin is a 22-residue amphipathic alpha-helical peptide, which is C-terminally amidated It exhibits broad-spectrum antimicrobial activity with low toxicity and high salt tolerance [24]. To investigate whether these AMPs had distinct characteristics arising from their origin in fish that live in a cold environment, we tested the effect of temperature on their activity
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