title: Discovery and characterization of two isoforms of moronecidin, a novel antimicrobial peptide from hybrid striped bass.
abstract: We isolated a novel 22-residue, C-terminally amidated antimicrobial peptide, moronecidin, from the skin and gill of hybrid striped bass. Two isoforms, differing by only one amino acid, are derived from each parental species, white bass (Morone chrysops) and striped bass (Morone saxatilis). Molecular masses (2543 and 2571 Da), amino acid sequences (FFHHIFRGIVHVGKTIH(K/R)LVTGT), cDNA, and genomic DNA sequences were determined for each isoform. A predicted 79-residue moronecidin prepropeptide consists of three domains: a signal peptide (22 amino acids), a mature peptide (22 amino acids), and a C-terminal prodomain (35 amino acids). The synthetic, amidated white bass moronecidin exhibited broad spectrum antimicrobial activity that was retained at high salt concentration. An alpha-helical structure was confirmed by circular dichroism spectroscopy. The moronecidin gene consists of three introns and four exons. Peptide sequence and gene organization were similar to pleurocidin, an antimicrobial peptide from winter flounder. A TATA box and several consensus-binding motifs for transcription factors were found in the region 5' to the transcriptional start site. Moronecidin gene expression was detected in gill, skin, intestine, spleen, anterior kidney, and blood cells by kinetic reverse transcription (RT)-PCR. Thus, moronecidin is a new alpha-helical, broad spectrum antimicrobial peptide isolated from the skin and gills of hybrid striped bass.
authors.affiliation: Department of Pediatrics, University of California, San Diego School of Medicine, La Jolla, California 92093-0830, USA.
authors.forename: Xavier
authors.initials: X
authors.lastname: Lauth
authors.forename: Hiroko
authors.initials: H
authors.lastname: Shike
authors.forename: Jane C
authors.initials: JC
authors.lastname: Burns
authors.forename: Mark E
authors.initials: ME
authors.lastname: Westerman
authors.forename: Vaughn E
authors.initials: VE
authors.lastname: Ostland
authors.forename: James M
authors.initials: JM
authors.lastname: Carlberg
authors.forename: Jon C
authors.initials: JC
authors.lastname: Van Olst
authors.forename: Victor
authors.initials: V
authors.lastname: Nizet
authors.forename: Steven W
authors.initials: SW
authors.lastname: Taylor
authors.forename: Chisato
authors.initials: C
authors.lastname: Shimizu
authors.forename: Philippe
authors.initials: P
authors.lastname: Bulet
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides; D001483:Base Sequence; D001492:Bass; D002942:Circular Dichroism; D018076:DNA, Complementary / Q000378:metabolism; D005091:Exons; D029941:Fish Proteins; D006461:Hemolysis; D007438:Introns; D007700:Kinetics; D008957:Models, Genetic; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D010452:Peptide Biosynthesis; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D020033:Protein Isoforms; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000494:pharmacology*; D012333:RNA, Messenger / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013997:Time Factors; D014018:Tissue Distribution; D014158:Transcription, Genetic
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D018076:DNA, Complementary; D029941:Fish Proteins; D010455:Peptides; D020033:Protein Isoforms; D011506:Proteins; D012333:RNA, Messenger; C449802:moronecidin protein, Morone saxatilis