Eumenitin, a novel antimicrobial peptide from the venom of the solitary eumenine wasp Eumenes rubronotatus

  • Peptides. 2006 Nov;27(11):2624-31. doi: 10.1016/j.peptides.2006.04.013.
Katsuhiro Konno  1 ,  Miki Hisada ,  Hideo Naoki ,  Yasuhiro Itagaki ,  Renato Fontana ,  Marisa Rangel ,  Joacir Stolarz Oliveira ,  Marcia Perez Dos Santos Cabrera ,  João Ruggiero Neto ,  Izumi Hide ,  Yoshihiro Nakata ,  Tadashi Yasuhara ,  Terumi Nakajima
Affiliations
  • 1. Center for Applied Toxinology, Butantan Institute, São Paulo, SP 05503-900, Brazil. [email protected]
PMID: 16762455 DOI: 10.1016/j.peptides.2006.04.013
Abstract

A novel antimicrobial peptide, eumenitin, was isolated from the venom of the solitary eumenine wasp Eumenes rubronotatus. The sequence of eumenitin, Leu-Asn-Leu-Lys-Gly-Ile-Phe-Lys-Lys-Val-Ala-Ser-Leu-Leu-Thr, was mostly analyzed by mass spectrometry together with Edman degradation, and corroborated by solid-phase synthesis. This peptide has characteristic features of cationic linear alpha-helical antimicrobial peptides, and therefore, can be predicted to adopt an amphipathic alpha-helix secondary structure. In fact, the CD spectra of eumenitin in the presence of TFE or SDS showed a high content of alpha-helical conformation. Eumenitin exhibited inhibitory activity against both Gram-positive and Gram-negative bacteria, and moderately stimulated degranulation from the rat peritoneal mast cells and the RBL-2H3 cells, but showed no hemolytic activity against human erythrocytes. This antimicrobial peptide in the eumenine wasp venom may play a role in preventing potential Infection by Microorganisms during prey consumption by their larvae.

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