title: Structure, synthesis, and molecular cloning of dermaseptins B, a family of skin peptide antibiotics.
abstract: Analysis of antimicrobial activities that are present in the skin secretions of the South American frog Phyllomedusa bicolor revealed six polycationic (lysine-rich) and amphipathic alpha-helical peptides, 24-33 residues long, termed dermaseptins B1 to B6, respectively. Prepro-dermaseptins B all contain an almost identical signal peptide, which is followed by a conserved acidic propiece, a processing signal Lys-Arg, and a dermaseptin progenitor sequence. The 22-residue signal peptide plus the first 3 residues of the acidic propiece are encoded by conserved nucleotides encompassed by the first coding exon of the dermaseptin genes. The 25-residue amino-terminal region of prepro-dermaseptins B shares 50% identity with the corresponding region of precursors for D-amino acid containing opioid peptides or for antimicrobial peptides originating from the skin of distantly related frog species. The remarkable similarity found between prepro-proteins that encode end products with strikingly different sequences, conformations, biological activities and modes of action suggests that the corresponding genes have evolved through dissemination of a conserved "secretory cassette" exon.
authors.affiliation: Laboratoire de Bioactivation des Peptides, Institut Jacques Monod, 2 Place Jussieu, 75251 Paris Cedex 05, France.
authors.forename: S
authors.initials: S
authors.lastname: Charpentier
authors.forename: M
authors.initials: M
authors.lastname: Amiche
authors.forename: J
authors.initials: J
authors.lastname: Mester
authors.forename: V
authors.initials: V
authors.lastname: Vouille
authors.forename: J P
authors.initials: JP
authors.lastname: Le Caer
authors.forename: P
authors.initials: P
authors.lastname: Nicolas
authors.forename: A
authors.initials: A
authors.lastname: Delfour
mesh_terms: D000595:Amino Acid Sequence; D029845:Amphibian Proteins; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D023181:Antimicrobial Cationic Peptides; D001001:Anura; D001483:Base Sequence; D002455:Cell Division / Q000187:drug effects; D003001:Cloning, Molecular; D019143:Evolution, Molecular; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D010455:Peptides / Q000737:chemistry* / Q000633:toxicity; D011498:Protein Precursors / Q000737:chemistry; D021382:Protein Sorting Signals / Q000737:chemistry; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D012867:Skin / Q000737:chemistry*
chemical_list: D029845:Amphibian Proteins; D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D010446:Peptide Fragments; D010455:Peptides; D011498:Protein Precursors; D021382:Protein Sorting Signals; C087616:dermaseptin b protein, Phyllomedusa