Pentadactylin: An antimicrobial peptide from the skin secretions of the South American bullfrog Leptodactylus pentadactylus

Jay D. King; Nadia Al-Ghaferi; Bency Abraham; Agnes Sonnevend; Jerome Leprince; Per F. Nielsen; J. Michael Conlon

doi:10.1016/j.cbpc.2005.09.002

Pentadactylin: An antimicrobial peptide from the skin secretions of the South American bullfrog Leptodactylus pentadactylus

Jay D. King
, Nadia Al-Ghaferi
, Bency Abraham
, Agnes Sonnevend
, Jerome Leprince
, Per F. Nielsen
, J. Michael Conlon

School of Biomedical Sciences

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

34 Citations (Scopus)

Abstract

Norepinephrine-stimulated skin secretions were obtained from male specimens of the South American bullfrog, Leptodactylus pentadactylus and shown to contain two peptides that inhibited the growth of microorganisms. The primary structure of a previously undescribed peptide, termed pentadactylin, was established as Gly-Leu-Leu-Asp-Thr-Leu-Lys-Gly-Ala-Ala-Lys-Asn-Val-Val-Gly-Ser- Leu-Ala-Ser-Lys-Val-Met-Glu-Lys-Leu.NH₂. The second peptide, which differs from pentadactylin by eight amino acid residues, is identical to fallaxin previously isolated from skin secretions of the Caribbean mountain chicken frog L. fallax. Pentadactylin inhibited the growth of reference strains of both Gram-negative bacteria (Escherichia coli, Enterobacter cloacae, Klebsiella pneumoniae, Pseudomonas aeruginosa) and Gram-positive bacteria (Staphylococcus aureus, Staphylococcus epidermidis, Enterococcus faecalis, Streptococcus group B) but potencies were relatively low (MIC values in the range 25-200 μM). The peptide showed very low hemolytic activity against human erythrocytes (LD50 > 400 μM).

Original language	English
Pages (from-to)	393-397
Number of pages	5
Journal	Comparative Biochemistry and Physiology - C Toxicology and Pharmacology
Volume	141
Issue number	4
DOIs	https://doi.org/10.1016/j.cbpc.2005.09.002
Publication status	Published (in print/issue) - Aug 2005

Funding

The authors thank Chad Peeling of Clyde Peeling Reptiland and Dr. Louise Rollins-Smith, Vanderbilt University for help in collection of the skin secretions. This work was supported by an Interdisciplinary Grant (03/12-8-03-01) and a Faculty Support Grant (NP/05/01) from the United Arab Emirates University.

Funders
United Arab Emirates University

Keywords

Antimicrobial peptide
Fallaxin
Frog skin
Leptodactylidae
Pentadactylin

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10.1016/j.cbpc.2005.09.002

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title = "Pentadactylin: An antimicrobial peptide from the skin secretions of the South American bullfrog Leptodactylus pentadactylus",

abstract = "Norepinephrine-stimulated skin secretions were obtained from male specimens of the South American bullfrog, Leptodactylus pentadactylus and shown to contain two peptides that inhibited the growth of microorganisms. The primary structure of a previously undescribed peptide, termed pentadactylin, was established as Gly-Leu-Leu-Asp-Thr-Leu-Lys-Gly-Ala-Ala-Lys-Asn-Val-Val-Gly-Ser- Leu-Ala-Ser-Lys-Val-Met-Glu-Lys-Leu.NH2. The second peptide, which differs from pentadactylin by eight amino acid residues, is identical to fallaxin previously isolated from skin secretions of the Caribbean mountain chicken frog L. fallax. Pentadactylin inhibited the growth of reference strains of both Gram-negative bacteria (Escherichia coli, Enterobacter cloacae, Klebsiella pneumoniae, Pseudomonas aeruginosa) and Gram-positive bacteria (Staphylococcus aureus, Staphylococcus epidermidis, Enterococcus faecalis, Streptococcus group B) but potencies were relatively low (MIC values in the range 25-200 μM). The peptide showed very low hemolytic activity against human erythrocytes (LD50 > 400 μM).",

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author = "King, \{Jay D.\} and Nadia Al-Ghaferi and Bency Abraham and Agnes Sonnevend and Jerome Leprince and Nielsen, \{Per F.\} and Conlon, \{J. Michael\}",

year = "2005",

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doi = "10.1016/j.cbpc.2005.09.002",

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AU - Al-Ghaferi, Nadia

AU - Abraham, Bency

AU - Sonnevend, Agnes

AU - Leprince, Jerome

AU - Nielsen, Per F.

AU - Conlon, J. Michael

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N2 - Norepinephrine-stimulated skin secretions were obtained from male specimens of the South American bullfrog, Leptodactylus pentadactylus and shown to contain two peptides that inhibited the growth of microorganisms. The primary structure of a previously undescribed peptide, termed pentadactylin, was established as Gly-Leu-Leu-Asp-Thr-Leu-Lys-Gly-Ala-Ala-Lys-Asn-Val-Val-Gly-Ser- Leu-Ala-Ser-Lys-Val-Met-Glu-Lys-Leu.NH2. The second peptide, which differs from pentadactylin by eight amino acid residues, is identical to fallaxin previously isolated from skin secretions of the Caribbean mountain chicken frog L. fallax. Pentadactylin inhibited the growth of reference strains of both Gram-negative bacteria (Escherichia coli, Enterobacter cloacae, Klebsiella pneumoniae, Pseudomonas aeruginosa) and Gram-positive bacteria (Staphylococcus aureus, Staphylococcus epidermidis, Enterococcus faecalis, Streptococcus group B) but potencies were relatively low (MIC values in the range 25-200 μM). The peptide showed very low hemolytic activity against human erythrocytes (LD50 > 400 μM).

AB - Norepinephrine-stimulated skin secretions were obtained from male specimens of the South American bullfrog, Leptodactylus pentadactylus and shown to contain two peptides that inhibited the growth of microorganisms. The primary structure of a previously undescribed peptide, termed pentadactylin, was established as Gly-Leu-Leu-Asp-Thr-Leu-Lys-Gly-Ala-Ala-Lys-Asn-Val-Val-Gly-Ser- Leu-Ala-Ser-Lys-Val-Met-Glu-Lys-Leu.NH2. The second peptide, which differs from pentadactylin by eight amino acid residues, is identical to fallaxin previously isolated from skin secretions of the Caribbean mountain chicken frog L. fallax. Pentadactylin inhibited the growth of reference strains of both Gram-negative bacteria (Escherichia coli, Enterobacter cloacae, Klebsiella pneumoniae, Pseudomonas aeruginosa) and Gram-positive bacteria (Staphylococcus aureus, Staphylococcus epidermidis, Enterococcus faecalis, Streptococcus group B) but potencies were relatively low (MIC values in the range 25-200 μM). The peptide showed very low hemolytic activity against human erythrocytes (LD50 > 400 μM).

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KW - Leptodactylidae

KW - Pentadactylin

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JO - Comparative Biochemistry and Physiology - C Toxicology and Pharmacology

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IS - 4

ER -

Pentadactylin: An antimicrobial peptide from the skin secretions of the South American bullfrog Leptodactylus pentadactylus

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