title: Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides.
abstract: Three cytolytic peptides, termed brevinin-1E, brevinin-2E, and esculentin, were isolated from skin secretions of the European frog Rana esculenta (Simmaco, M., Mignogna, G., Barra, D., and Bossa, F. (1993) FEBS Lett. 324, 159-161). Nucleotide sequence analysis of cDNAs coding for the corresponding precursors revealed that in all of them a single copy of the sequence of the mature peptide is present preceded by a dibasic cleavage site and followed by a stop codon. The signal peptides of these precursors show a clear homology to the corresponding region of the precursor of dermorphin, a neuropeptide occurring in the skin of amphibians of the subfamily Phyllomedusinae. Ten new peptides, ranging in size from 24 to 46 residues, all possessing an intramolecular disulfide bridge located at the carboxyl-terminal end, were isolated from skin secretions of R. esculenta. These peptides can be grouped into four subfamilies on the basis of their distinctive structural and/or functional properties. All of these new peptides have antimicrobial and/or hemolytic activities typical for the respective subfamily. In addition, we demonstrate that esculentin-1 also inhibits the growth of Pseudomonas aeruginosa, Candida albicans, and Saccharomyces cerevisiae.
authors.affiliation: Dipartimento di Scienze Biochimiche A. Rossi Fanelli, Università La Sapienza, Roma, Italy.
authors.forename: M
authors.initials: M
authors.lastname: Simmaco
authors.forename: G
authors.initials: G
authors.lastname: Mignogna
authors.forename: D
authors.initials: D
authors.lastname: Barra
authors.forename: F
authors.initials: F
authors.lastname: Bossa
mesh_terms: D000595:Amino Acid Sequence; D029845:Amphibian Proteins; D000818:Animals; D000900:Anti-Bacterial Agents / Q000096:biosynthesis* / Q000302:isolation & purification / Q000633:toxicity; D000890:Anti-Infective Agents / Q000302:isolation & purification* / Q000378:metabolism / Q000633:toxicity; D023181:Antimicrobial Cationic Peptides; D001483:Base Sequence; D002176:Candida albicans / Q000187:drug effects; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000378:metabolism; D004912:Erythrocytes / Q000187:drug effects; D004926:Escherichia coli / Q000187:drug effects; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides; D010452:Peptide Biosynthesis; D010455:Peptides / Q000302:isolation & purification / Q000633:toxicity; D021382:Protein Sorting Signals / Q000235:genetics / Q000378:metabolism; D011550:Pseudomonas aeruginosa / Q000187:drug effects; D011893:Rana esculenta; D012441:Saccharomyces cerevisiae / Q000187:drug effects; D017386:Sequence Homology, Amino Acid; D012879:Skin Physiological Phenomena; D013211:Staphylococcus aureus / Q000187:drug effects
chemical_list: D029845:Amphibian Proteins; D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D018076:DNA, Complementary; D009838:Oligodeoxyribonucleotides; D010455:Peptides; D021382:Protein Sorting Signals; C092874:esculentin protein, Rana esculenta