New Mastoparan Peptides in the Venom of the Solitary Eumenine Wasp Eumenes micado
Katsuhiro Konno,
Kohei Kazuma,
Marisa Rangel,
Joacir Stolarz-de-Oliveira,
Renato Fontana,
Marii Kawano,
Hiroyuki Fuchino,
Izumi Hide,
Tadashi Yasuhara,
Yoshihiro Nakata
Affiliations
Katsuhiro Konno
Institute of Natural Medicine, University of Toyama, Toyama, Toyama 930-0194, Japan
Kohei Kazuma
Institute of Natural Medicine, University of Toyama, Toyama, Toyama 930-0194, Japan
Marisa Rangel
Immunopathology Laboratory, Butantan Institute, Sao Paulo SP 05503-900, Brazil
Joacir Stolarz-de-Oliveira
Laboratory of Physiology and Animal Toxins, Federal University of West Pará, Santarém PA 68040-070, Brazil
Renato Fontana
Department of Biological Sciences, State University of Santa Cruz, Ilhéus BA 45662-900, Brazil
Marii Kawano
Research Center for Medicinal Plant Resources, National Institutes of Biomedical Innovation, Health and Nutrition, Tsukuba, Ibaraki 305-0843, Japan
Hiroyuki Fuchino
Research Center for Medicinal Plant Resources, National Institutes of Biomedical Innovation, Health and Nutrition, Tsukuba, Ibaraki 305-0843, Japan
Izumi Hide
Department of Molecular and Pharmacological Neuroscience, Graduate School of Biomedical and Health Sciences, Hiroshima University, Hiroshima, Hiroshima 734-8551, Japan
Tadashi Yasuhara
Laboratory of Microbial Chemistry, School of Pharmacy, Kitasato University, Minato-ku, Tokyo 108-8641, Japan
Yoshihiro Nakata
Department of Pharmacology, Hiroshima University Graduate School of Biomedical & Health Sciences, Hiroshima 734-8553, Japan
Comprehensive LC-MS and MS/MS analysis of the crude venom extract from the solitary eumenine wasp Eumenes micado revealed the component profile of this venom mostly consisted of small peptides. The major peptide components, eumenine mastoparan-EM1 (EMP-EM1: LKLMGIVKKVLGAL-NH2) and eumenine mastoparan-EM2 (EMP-EM2: LKLLGIVKKVLGAI-NH2), were purified and characterized by the conventional method. The sequences of these new peptides are homologous to mastoparans, the mast cell degranulating peptides from social wasp venoms; they are 14 amino acid residues in length, rich in hydrophobic and basic amino acids, and C-terminal amidated. Accordingly, these new peptides can belong to mastoparan peptides (in other words, linear cationic α-helical peptides). Indeed, the CD spectra of these new peptides showed predominantly α-helix conformation in TFE and SDS. In biological evaluation, both peptides exhibited potent antibacterial activity, moderate degranulation activity from rat peritoneal mast cells, and significant leishmanicidal activity, while they showed virtually no hemolytic activity on human or mouse erythrocytes. These results indicated that EMP-EM peptides rather strongly associated with bacterial cell membranes rather than mammalian cell membranes.
