title: Host-defense peptides from skin secretions of the tetraploid frogs Xenopus petersii and Xenopus pygmaeus, and the octoploid frog Xenopus lenduensis (Pipidae).
abstract: Peptidomic analysis of norepinephrine-stimulated skin secretions led to the identification of host-defense peptides belonging to the magainin, peptide glycine-leucine-amide (PGLa), and caerulein precursor fragment (CPF) families from the tetraploid frogs, Xenopus petersii (Peters' clawed frog) and Xenopus pygmaeus (Bouchia clawed frog), and the octoploid frog Xenopus lenduensis (Lendu Plateau clawed frog). Xenopsin-precursor fragment (XPF) peptides were not detected. The primary structures of the antimicrobial peptides from X. petersii demonstrate a close, but not conspecific relationship, with Xenopus laevis whereas the X. pygmaeus peptides show appreciable variation from previously characterized orthologs from other Xenopus species. Polyploidization events within the Xenopodinae (Silurana+Xenopus) are associated with extensive gene silencing (nonfunctionization) but unexpectedly the full complement of four PGLa paralogs were isolated from X. lenduendis secretions. Consistent with previous data, the CPF peptides showed the highest growth-inhibitory activity against bacteria with CPF-PG1 (GFGSLLGKALKIGTNLL.NH(2)) from X. pygmaeus combining high antimicrobial potency against Staphylococcus aureus (MIC=6 μM) with relatively low hemolytic activity (LC(50)=145 μM).
authors: Rare Species Conservatory Foundation, St. Louis, MO 63110, USA.
authors: Jay D
authors: JD
authors: King
authors: Milena
authors: M
authors: Mechkarska
authors: Laurent
authors: L
authors: Coquet
authors: Jérôme
authors: J
authors: Leprince
authors: Thierry
authors: T
authors: Jouenne
authors: Hubert
authors: H
authors: Vaudry
authors: Koji
authors: K
authors: Takada
authors: J Michael
authors: JM
authors: Conlon
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D002108:Ceruletide / Q000737:chemistry; D004912:Erythrocytes / Q000187:drug effects; D053878:Hemolytic Agents / Q000494:pharmacology; D006801:Humans; D054806:Magainins / Q000737:chemistry; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D011123:Polyploidy; D011498:Protein Precursors / Q000737:chemistry; D012867:Skin / Q000378:metabolism*; D013211:Staphylococcus aureus / Q000187:drug effects; D040681:Structural Homology, Protein; D057891:Tetraploidy; D014981:Xenopus / Q000235:genetics*; D029867:Xenopus Proteins / Q000737:chemistry / Q000302:isolation & purification
chemical_list: D023181:Antimicrobial Cationic Peptides; D053878:Hemolytic Agents; D054806:Magainins; D010455:Peptides; D011498:Protein Precursors; D029867:Xenopus Proteins; C016832:xenopsin; D002108:Ceruletide