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

2001; Elsevier BV; Volume: 1550; Issue: 1 Linguagem: Inglês

10.1016/s0167-4838(01)00271-0

1878-1454

Katsuhiro Konno, Miki Hisada, Renato Fontana, Carla C. B. Lorenzi, Hideo Naoki, Yasuhiro Itagaki, Akiko Miwa, Nobufumi Kawai, Yoshihiro Nakata, Tadashi Yasuhara, João Ruggiero Neto, Walter Filgueira de Azevedo, Mário Sérgio Palma, Terumi Nakajima,

Insect and Arachnid Ecology and Behavior

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 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.