Antimicrobial peptides from the venoms of Vespa bicolor Fabricius

• Published in: Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2008-11, Vol.29 (11), p.1887-1892
• Main Authors: Chen, Wenhu, Yang, Xinbo, Yang, Xiaolong, Zhai, Lei, Lu, Zekuan, Liu, Jingze, Yu, Haining
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Antimicrobial peptide; Bacteria - drug effects; Base Sequence; Biological and medical sciences; Chemotactic peptide; Cloning, Molecular; Fundamental and applied biological sciences. Psychology; Fungi - drug effects; Hemolysis - drug effects; Humans; Hymenoptera; Mastoparan; Microbial Sensitivity Tests; Molecular Sequence Data; Peptides - chemistry; Peptides - isolation & purification; Peptides - pharmacology; Rabbits; Vertebrates: endocrinology; Vespa; Vespa bicolor; Wasp venom; Wasp Venoms - chemistry; Wasp Venoms - pharmacology; Wasps - chemistry
• ISSN: 0196-9781; 1873-5169
• DOI: 10.1016/j.peptides.2008.07.018

Hornets possess highly toxic venoms, which are rich in toxins, enzymes and biologically active peptides. Many bioactive substances have been identified from wasp venoms. Vespa mastoparan (MP-VBs) and Vespa chemotatic peptide presenting antimicrobial action (VESP-VBs) were purified and characterized from the venom of the wasp, Vespa bicolor Fabricius. The precursors encoding VESP-VBs and MP-VBs were cloned from the cDNA library of the venomous glands. Analyzed by FAB-MS, the amino acid sequence and molecular mass for VESP-VB1 were FMPIIGRLMSGSL and 1420.6, for MP-VB1 were INMKASAAVAKKLL and 1456.5, respectively. The primary structures of these peptides are homologous to those of chemotactic peptides and mastoparans isolated from other vespid venoms. These peptides showed strong antimicrobial activities against bacteria and fungi and induced mast cell degranulation, but displayed almost no hemolytic activity towards human blood red cells.