title: Anoplin, a novel antimicrobial peptide from the venom of the solitary wasp Anoplius samariensis.
abstract: A novel antimicrobial peptide, anoplin, was purified from the venom of the solitary wasp Anoplius samariensis. The sequence was mostly analyzed by mass spectrometry, which was corroborated by solid-phase synthesis. Anoplin, composed of 10 amino acid residues, Gly-Leu-Leu-Lys-Arg-Ile-Lys-Thr-Leu-Leu-NH2, has a high homology to crabrolin and mastoparan-X, the mast cell degranulating peptides from social wasp venoms, and, therefore, can be predicted to adopt an amphipathic alpha-helix secondary structure. In fact, the circular dichroism (CD) spectra of anoplin in the presence of trifluoroethanol or sodium dodecyl sulfate showed a high content, up to 55%, of the alpha-helical conformation. A modeling study of anoplin based on its homology to mastoparan-X supported the CD results. Biological evaluation using the synthetic peptide revealed that this peptide exhibited potent activity in stimulating degranulation from rat peritoneal mast cells and broad-spectrum antimicrobial activity against both Gram-positive and Gram-negative bacteria. Therefore, this is the first antimicrobial component to be found in the solitary wasp venom and it may play a key role in preventing potential infection by microorganisms during prey consumption by their larvae. Moreover, this peptide is the smallest among the linear alpha-helical antimicrobial peptides hitherto found in nature, which is advantageous for chemical manipulation and medical application.
authors.affiliation: Center of Study of Social Insects, Department of Biology, Intitute of Biosciences of Rio Claro, São Paulo State University, Rio Claro, SP, Brazil. kk-gon@rc.unesp.br
authors.forename: K
authors.initials: K
authors.lastname: Konno
authors.forename: M
authors.initials: M
authors.lastname: Hisada
authors.forename: R
authors.initials: R
authors.lastname: Fontana
authors.forename: C C
authors.initials: CC
authors.lastname: Lorenzi
authors.forename: H
authors.initials: H
authors.lastname: Naoki
authors.forename: Y
authors.initials: Y
authors.lastname: Itagaki
authors.forename: A
authors.initials: A
authors.lastname: Miwa
authors.forename: N
authors.initials: N
authors.lastname: Kawai
authors.forename: Y
authors.initials: Y
authors.lastname: Nakata
authors.forename: T
authors.initials: T
authors.lastname: Yasuhara
authors.forename: J
authors.initials: J
authors.lastname: Ruggiero Neto
authors.forename: W F
authors.initials: WF
authors.lastname: de Azevedo
authors.forename: M S
authors.initials: MS
authors.lastname: Palma
authors.forename: T
authors.initials: T
authors.lastname: Nakajima
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides; D015550:Cell Degranulation; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D005260:Female; D008407:Mast Cells / Q000187:drug effects / Q000502:physiology; D008826:Microbial Sensitivity Tests; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry* / Q000302:isolation & purification* / Q000494:pharmacology; D051381:Rats; D016415:Sequence Alignment; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014862:Wasp Venoms / Q000737:chemistry* / Q000302:isolation & purification* / Q000494:pharmacology; D014863:Wasps
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D009842:Oligopeptides; D014862:Wasp Venoms; C443041:anoplin