Anoplin, a novel antimicrobial peptide from the venom of the solitary wasp Anoplius samariensis

• Published in: Biochimica et biophysica acta Vol. 1550; no. 1; pp. 70 - 80
• Main Authors: Konno, Katsuhiro, Hisada, Miki, Fontana, Renato, Lorenzi, Carla C.B., Naoki, Hideo, Itagaki, Yasuhiro, Miwa, Akiko, Kawai, Nobufumi, Nakata, Yoshihiro, Yasuhara, Tadashi, Ruggiero Neto, João, de Azevedo, Walter F., Palma, Mario S., Nakajima, Terumi
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 26.11.2001
• Subjects: Amino Acid Sequence; Amphipathic α-helical structure; Animals; Anoplin; Anti-Bacterial Agents - chemistry; Anti-Bacterial Agents - isolation & purification; Anti-Bacterial Agents - pharmacology; Antimicrobial Cationic Peptides; Antimicrobial peptide; Cell Degranulation; Chromatography, High Pressure Liquid; Circular Dichroism; Female; Mast Cells - drug effects; Mast Cells - physiology; Microbial Sensitivity Tests; Models, Molecular; Oligopeptides - chemistry; Oligopeptides - isolation & purification; Oligopeptides - pharmacology; Rats; Sequence Alignment; Solitary wasp venom; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Wasp Venoms - chemistry; Wasp Venoms - isolation & purification; Wasp Venoms - pharmacology; Wasps; PG, L-α-phosphatidyl- DL-glycerol; CPY, carboxypeptidase Y; TFE, trifluoroethanol; Solitary wasp venom; PC, L-α-phosphatidylcholine; CID, collision-induced dissociation; Amphipathic α-helical structure; MALDI-TOF MS, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry; EMP-AF, eumenine mastoparan-AF; PMTX, pompilidotoxin; PSD, post-source decay; APM, aminopeptidase M; Anoplin; Antimicrobial peptide; CD, circular dichroism
• ISSN: 0167-4838; 0006-3002; 1879-2588; 1878-2434
• DOI: 10.1016/S0167-4838(01)00271-0

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-NH 2, 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 α-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 α-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 α-helical antimicrobial peptides hitherto found in nature, which is advantageous for chemical manipulation and medical application.