Antimicrobial peptides from the venom gland of the social wasp Vespa tropica.

Peptide agents are regarded as potential candidates for overcoming the life-threatening resistance of pathogenic microorganisms to classic antibiotics. Accordingly, a peptidomic and genomic investigation of natural antimicrobial peptides (AMPs) can provide structure-functional information for designing peptide antibiotics with therapeutic potential. In the present study, we identified nine AMPs from the venom gland of the wasp Vespa tropica using combined methods of peptidomics and genomics. These AMPs were classified into two different families based on sequence similarity, mastoparan and vespid chemotactic peptides (VCPs), and thus named mastoparan-VT1 to -VT7, VCP-VT1 and -VT2. Among these nine AMPs, mastoparan-VT1 and VCP-VT1 are identical to peptides from other wasps. These AMPs exerted broad-spectrum antimicrobial activity against standard and clinically isolated strains of bacteria. In addition, they showed weak hemolytic activity toward human erythrocytes. Our results reveal that identical AMPs are widely distributed in different wasp venoms and might provide templates for the development of novel peptide antibiotics.