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

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.NH(2)) inhibited the growth of the Gram-negative bacteria Acinetobacter baumannii, Klebsiella pneumoniae, and Pseudomonas aeruginosa (MIC≤25μM) suggesting potential for development into an anti-infective agent for use against these emerging antibiotic-resistant pathogens.
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https://hal-normandie-univ.archives-ouvertes.fr/hal-01960943
Contributor : Jérôme Leprince <>
Submitted on : Wednesday, December 19, 2018 - 4:12:11 PM
Last modification on : Tuesday, April 7, 2020 - 3:36:04 PM

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J Michael Conlon, Milena Mechkarska, Eman Ahmed, Jérôme Leprince, Hubert Vaudry, et al.. Purification and properties of antimicrobial peptides from skin secretions of the Eritrea clawed frog Xenopus clivii (Pipidae). Comparative Biochemistry and Physiology - Part C: Toxicology and Pharmacology, Elsevier, 2011, 153 (3), pp.350-354. ⟨10.1016/j.cbpc.2010.12.007⟩. ⟨hal-01960943⟩

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