Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides

• Published in: The Journal of biological chemistry Vol. 269; no. 16; pp. 11956 - 11961
• Main Authors: SIMMACO, M, MIGNOGNA, G, BARRA, D, BOSSA, F
• Format: Journal Article
• Language: English
• Published: Bethesda, MD American Society for Biochemistry and Molecular Biology 22.04.1994
• Subjects: Amino Acid Sequence; Amphibian Proteins; Animals; Anti-Bacterial Agents - biosynthesis; Anti-Bacterial Agents - isolation & purification; Anti-Bacterial Agents - toxicity; Anti-Infective Agents - isolation & purification; Anti-Infective Agents - metabolism; Anti-Infective Agents - toxicity; Antimicrobial Cationic Peptides; Bacteriology; Base Sequence; Biological and medical sciences; Candida albicans - drug effects; Cloning, Molecular; DNA, Complementary - metabolism; Erythrocytes - drug effects; Escherichia coli - drug effects; Fundamental and applied biological sciences. Psychology; Microbial Sensitivity Tests; Microbiology; Molecular Sequence Data; Oligodeoxyribonucleotides; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains; Peptide Biosynthesis; Peptides - isolation & purification; Peptides - toxicity; Protein Sorting Signals - genetics; Protein Sorting Signals - metabolism; Pseudomonas aeruginosa - drug effects; Rana esculenta; Saccharomyces cerevisiae - drug effects; Sequence Homology, Amino Acid; Skin Physiological Phenomena; Staphylococcus aureus - drug effects; Hemolysis; Peptides; Amphibia; Host agent relation; Primary structure; Salientia; Antimicrobial agent; Vertebrata; Structure activity relation; Rana esculenta; Skin; Biosynthesis precursor; Molecular cloning
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/s0021-9258(17)32666-2

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.