Leptodactylus ocellatus (Amphibia): mechanism of defense in the skin and molecular phylogenetic relationships

Amphibian antimicrobial peptides have been known for many decades and several of them have already been isolated. However, the number of species investigated is still small. Herein, we report on the skin secretions of Leptodactylus ocellatus, which were extracted by mild electrical stimulation and i...

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Published in:	Journal of experimental zoology. Part A, Ecological genetics and physiology Vol. 313A; no. 1; pp. 1 - 8
Main Authors:	Leite Jr, João Manoel Almeida, Silva, Luciano Paulino, Silva-Leite, Roberta Rocha, Ferrari, Ana Stella, Noronha, Sergio Eustáquio, Silva, Helio Ricardo, Bloch Jr, Carlos, Leite, José Roberto de Souza de Almeida
Format:	Journal Article
Language:	English
Published:	Hoboken Wiley Subscription Services, Inc., A Wiley Company 01-01-2010
Subjects:	Amino Acid Sequence Amphibia Animals Antimicrobial Cationic Peptides - genetics Antimicrobial Cationic Peptides - isolation & purification Antimicrobial Cationic Peptides - secretion Anura Brazil Ecosystem Escherichia coli Leptodactylus ocellatus Mass Spectrometry Microbial Sensitivity Tests Phylogeny Ranidae - genetics Ranidae - physiology Sequence Analysis, Protein Skin - secretion Staphylococcus aureus Brazil
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Summary:	Amphibian antimicrobial peptides have been known for many decades and several of them have already been isolated. However, the number of species investigated is still small. Herein, we report on the skin secretions of Leptodactylus ocellatus, which were extracted by mild electrical stimulation and its semi‐preparative reverse‐phase chromatography was resolved in more than 30 fractions. Among these fractions, two novel antimicrobial peptides were isolated and their amino acid sequences determined by de novo sequencing. The ocellatins‐5 and ‐6 (21 and 22 amino acid residues, respectively) are amidated at the C‐terminus. Ocellatins inhibited the growth of reference strains of both Gram‐negative bacteria (Escherichia coli) and Gram‐positive bacteria (Staphylococcus aureus) with minimal inhibition concentration values in the range of 32–128 µg/mL. The amino acid sequence of the peptides shows structural similarity with members of the antimicrobial peptides found in the skin secretion of other leptodactylid frogs. 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 species. J. Exp. Zool. 313A:1–8, 2010. © 2009 Wiley‐Liss, Inc.
Bibliography:	istex:365DCA0A29D5E7A77EFAC8A847E9ABBC12379869 ark:/67375/WNG-RKR6HWRZ-0 CNPq (Universal) Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA) ArticleID:JEZ551 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1932-5223 1932-5231 1932-5231
DOI:	10.1002/jez.551