title: Cytolytic peptides belonging to the brevinin-1 and brevinin-2 families isolated from the skin of the Japanese brown frog, Rana dybowskii.
abstract: Peptidomic analysis of an extract of the skins of specimens of Dybowski's brown frog Rana dybowskii Gunther, 1876, collected on Tsushima Island, Japan led to the identification of 10 peptides with differential antibacterial and hemolytic activities. The primary structures of these peptides identified them as belonging to the brevinin-1 (5 peptides) and brevinin-2 (5 peptides) families of antimicrobial peptides. A peptide (FIGPIISALASLFG.NH(2)) with structural similarity to members of the temporin family was also isolated but this component lacked cytolytic activity. Phylogenetic relationships among the Japanese brown frogs (R. dybowskii, R. japonica, R. okinavana, R. ornativentris, R. pirica, R. sakuraii, R. tagoi, and R. tsushimensis) are only incompletely understood. Cladograms based upon maximum parsimony analyses of the brevinin-1 and brevinin-2 amino acid sequences provide strong support for a sister-group relationship between R. dybowskii and R. pirica and somewhat weaker support for a sister-group relationship between R. okinavana and R. tsushimensis. These conclusions are consistent with previous analyses based upon allozyme variations and comparisons of the nucleotide sequences of mitochondrial genes.
authors: Department of Biochemistry, Faculty of Medicine and Health Sciences, United Arab Emirates University, 17666 Al-Ain, United Arab Emirates. jmconlon@uaeu.ac.ae
authors: J Michael
authors: JM
authors: Conlon
authors: Jolanta
authors: J
authors: Kolodziejek
authors: Norbert
authors: N
authors: Nowotny
authors: Jérôme
authors: J
authors: Leprince
authors: Hubert
authors: H
authors: Vaudry
authors: Laurent
authors: L
authors: Coquet
authors: Thierry
authors: T
authors: Jouenne
authors: Shawichi
authors: S
authors: Iwamuro
mesh_terms: D000595:Amino Acid Sequence; D029845:Amphibian Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D002851:Chromatography, High Pressure Liquid; D003603:Cytotoxins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D004912:Erythrocytes / Q000187:drug effects; D004926:Escherichia coli / Q000187:drug effects / Q000254:growth & development; D005260:Female; D006461:Hemolysis / Q000187:drug effects; D006801:Humans; D050296:Microbial Viability / Q000187:drug effects; D008969:Molecular Sequence Data; D010802:Phylogeny; D020033:Protein Isoforms; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D011898:Ranidae / Q000145:classification / Q000235:genetics; D012867:Skin / Q000737:chemistry*; D013211:Staphylococcus aureus / Q000187:drug effects / Q000235:genetics; D014020:Tissue Extracts / Q000737:chemistry* / Q000494:pharmacology
chemical_list: D029845:Amphibian Proteins; D023181:Antimicrobial Cationic Peptides; D003603:Cytotoxins; D020033:Protein Isoforms; D011506:Proteins; D014020:Tissue Extracts; C104501:temporin; C078413:brevinin-1 protein, Rana; C078414:brevinin-2, Rana