Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae)

J. Michael Conlon, Milena Mechkarska, Eman Ahmed, Jérôme Leprince, Hubert Vaudry, Jay D. King, Koji Takada

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)

Abstract

Five peptides with antimicrobial activity were isolated from norepinephrine-stimulated skin secretions of the tetraploid frog Xenopus clivii Peracca, 1898 (Pipidae). Characterization of the peptides demonstrated that they are structurally similar to magainins (2 peptides), caerulein-precursor fragments, CPF (2 peptides), and xenopsin-precursor fragments, XPF (1 peptide) that have been previously isolated from other species of the genus Xenopus. The magainins and the XPF peptide were active only against the Gram-negative microorganism Escherichia coli whereas the CPF peptides were also active against the Gram-positive Staphylococcus aureus. The most abundant antimicrobial peptide in the secretions, CPF-C1 (GFGSLLGKALRLG ANVL.NH2) inhibited the growth of the Gram-negative bacteria Acinetobacter baumannii, Klebsiella pneumoniae, and Pseudomonas aeruginosa (MIC ≤ 25 μM) suggesting potential for development into an anti-infective agent for use against these emerging antibiotic-resistant pathogens.

Original languageEnglish
Pages (from-to)350-354
Number of pages5
JournalComparative Biochemistry and Physiology - C Toxicology and Pharmacology
Volume153
Issue number3
DOIs
Publication statusPublished - Apr 2011
Externally publishedYes

Keywords

  • Antibiotic resistance
  • Antimicrobial peptide
  • Frog skin
  • Magainin
  • Procaerulein
  • Proxenopsin

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Aquatic Science
  • Animal Science and Zoology
  • Toxicology
  • Cell Biology
  • Health, Toxicology and Mutagenesis

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