An antimicrobial peptide from the skin secretions of the mountain chicken frog Leptodactylus fallax (Anura:Leptodactylidae)

Louise A. Rollins-Smith; Jay D. King; Per F. Nielsen; Agnes Sonnevend; J. Michael Conlon

doi:10.1016/j.regpep.2004.07.013

An antimicrobial peptide from the skin secretions of the mountain chicken frog Leptodactylus fallax (Anura:Leptodactylidae)

Louise A. Rollins-Smith, Jay D. King, Per F. Nielsen, Agnes Sonnevend, J. Michael Conlon

School of Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

52 Citations (Scopus)

Abstract

A 25 amino-acid-residue, C-terminally α-amidated peptide with antimicrobial activity, which has been termed fallaxin, was isolated in high yield from the norepinephrine-stimulated skin secretions of the mountain chicken frog Leptodactylus fallax (Anura:Leptodactylidae). The amino acid sequence of the peptide (Gly-Val-Val-Asp-Ile-Leu-Lys-Gly-Ala-Ala-Lys-Asp-Ile-Ala-Gly-His- Leu-Ala-Ser-Lys-Val-Met-Asn-Lys-Leu•NH ₂) shows structural similarity with members of the ranatuerin-2 family previously isolated from the skins of frogs of the genus Rana that are only distantly related to the Leptodactylidae. This observation is consistent with the hypothesis that many frog skin antimicrobial peptides are related evolutionarily, having arisen from multiple duplications of an ancestral gene that existed before the radiation of the different families. Fallaxin inhibited the growth of reference strains of Gram-negative bacteria (Escherichia coli, Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella pneumoniae) but with relatively low potency (MIC≥20 μM) and was inactive against the Gram-positive bacterium (Staphylococcus aureus) and the yeast Candida albicans. The hemolytic activity of fallaxin was very low (HC ₅₀>200 μM). A second peptide, comprising residues (1-22) of fallaxin, was also isolated from the skin secretions but this component was inactive against the microorganisms tested.

Original language	English
Pages (from-to)	173-178
Number of pages	6
Journal	Regulatory Peptides
Volume	124
Issue number	1-3
DOIs	https://doi.org/10.1016/j.regpep.2004.07.013
Publication status	Published (in print/issue) - 15 Jan 2005

Funding

This work was supported by an Interdisciplinary Grant (03/12-8-03-01) and a Faculty Support Grant (NP/04/02) from the United Arab Emirates University to JMC and by an NSF Integrated Research Challenges in Enviromental Biology grant (DEB-0213851) and NSF grant (IBN-0131184) to L R-S. The authors thank Laura K. Reinert and Douglas C. Woodhams, Vanderbilt University for technical assistance and Laurey Steinke and Michele Fontaine (University of Nebraska Medical Center, Omaha, NE) for amino acid composition analysis. The support of the Forestry, Wildlife, and Parks Division of the Commonwealth of Dominica is gratefully acknowledged.

Funders	Funder number
National Science Foundation	IBN-0131184, DEB-0213851
United Arab Emirates University

Keywords

Fallaxin
Gram-negative bacteria
HPLC
Ranatuerin-2

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10.1016/j.regpep.2004.07.013

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title = "An antimicrobial peptide from the skin secretions of the mountain chicken frog Leptodactylus fallax (Anura:Leptodactylidae)",

abstract = "A 25 amino-acid-residue, C-terminally α-amidated peptide with antimicrobial activity, which has been termed fallaxin, was isolated in high yield from the norepinephrine-stimulated skin secretions of the mountain chicken frog Leptodactylus fallax (Anura:Leptodactylidae). The amino acid sequence of the peptide (Gly-Val-Val-Asp-Ile-Leu-Lys-Gly-Ala-Ala-Lys-Asp-Ile-Ala-Gly-His- Leu-Ala-Ser-Lys-Val-Met-Asn-Lys-Leu•NH 2) shows structural similarity with members of the ranatuerin-2 family previously isolated from the skins of frogs of the genus Rana that are only distantly related to the Leptodactylidae. This observation is consistent with the hypothesis that many frog skin antimicrobial peptides are related evolutionarily, having arisen from multiple duplications of an ancestral gene that existed before the radiation of the different families. Fallaxin inhibited the growth of reference strains of Gram-negative bacteria (Escherichia coli, Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella pneumoniae) but with relatively low potency (MIC≥20 μM) and was inactive against the Gram-positive bacterium (Staphylococcus aureus) and the yeast Candida albicans. The hemolytic activity of fallaxin was very low (HC 50>200 μM). A second peptide, comprising residues (1-22) of fallaxin, was also isolated from the skin secretions but this component was inactive against the microorganisms tested.",

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AU - Rollins-Smith, Louise A.

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AU - Conlon, J. Michael

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N2 - A 25 amino-acid-residue, C-terminally α-amidated peptide with antimicrobial activity, which has been termed fallaxin, was isolated in high yield from the norepinephrine-stimulated skin secretions of the mountain chicken frog Leptodactylus fallax (Anura:Leptodactylidae). The amino acid sequence of the peptide (Gly-Val-Val-Asp-Ile-Leu-Lys-Gly-Ala-Ala-Lys-Asp-Ile-Ala-Gly-His- Leu-Ala-Ser-Lys-Val-Met-Asn-Lys-Leu•NH 2) shows structural similarity with members of the ranatuerin-2 family previously isolated from the skins of frogs of the genus Rana that are only distantly related to the Leptodactylidae. This observation is consistent with the hypothesis that many frog skin antimicrobial peptides are related evolutionarily, having arisen from multiple duplications of an ancestral gene that existed before the radiation of the different families. Fallaxin inhibited the growth of reference strains of Gram-negative bacteria (Escherichia coli, Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella pneumoniae) but with relatively low potency (MIC≥20 μM) and was inactive against the Gram-positive bacterium (Staphylococcus aureus) and the yeast Candida albicans. The hemolytic activity of fallaxin was very low (HC 50>200 μM). A second peptide, comprising residues (1-22) of fallaxin, was also isolated from the skin secretions but this component was inactive against the microorganisms tested.

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An antimicrobial peptide from the skin secretions of the mountain chicken frog Leptodactylus fallax (Anura:Leptodactylidae)

Abstract

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Keywords

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