1. A novel serine protease inhibitor from the venom of Vespa bicolor Fabricius
Xinbo Yang, Yakun Wang, Zekuan Lu, Lei Zhai, Juguo Jiang, Jingze Liu, Haining Yu Comp Biochem Physiol B Biochem Mol Biol. 2009 May;153(1):116-20. doi: 10.1016/j.cbpb.2009.02.010. Epub 2009 Mar 1.
Hornets possess highly toxic venoms, which are rich in toxin, enzymes and biologically active peptides. Many bioactive substances have been identified from wasp venoms but only a few serine protease inhibitors have been identified from two kinds of wasp venoms. In this work, a serine protease inhibitor named bicolin was purified and characterized from the venom of the wasp, Vespa bicolor Fabricius. The precursor encoding bicolin was cloned from the cDNA library of the venomous glands. It is a cysteine-rich small protein containing 54 amino acid residues including 6 half-cysteines. The peptide is homologous to serine protease inhibitors isolated from venoms of Anoplius samariensis and Pimpla hypochondriaca. Bicolin showed inhibitory ability against trypsin and thrombin.
2. Two families of antimicrobial peptides from wasp (Vespa magnifica) venom
Xueqing Xu, Jianxu Li, Qiuming Lu, Hailong Yang, Yungong Zhang, Ren Lai Toxicon. 2006 Feb;47(2):249-53. doi: 10.1016/j.toxicon.2005.10.015. Epub 2005 Dec 5.
The hornet possesses highly toxic venom, which is rich in toxin, enzymes and biologically active peptides. Many bioactive substances were identified from wasp venom. Two families of antimicrobial peptides were purified and characterized from the venom of the wasp, Vespamagnifica (Smith). The primary structures of these peptides are homologous to those of chemotactic peptides and mastoparans isolated from other vespid venoms. They also share similarity to temporins which are amphibian antimicrobial peptides identified from the skin of the frog, Ranaboylii. These peptides show antimicrobial activities against bacteria and fungi. However, they show little hemolytic activity against human blood red cells.
3. Structural and biological characterization of mastoparans in the venom of Vespa species in Taiwan
Chun-Hsien Lin, Jason T C Tzen, Ching-Lin Shyu, Mars J Yang, Wu-Chun Tu Peptides. 2011 Oct;32(10):2027-36. doi: 10.1016/j.peptides.2011.08.015. Epub 2011 Aug 22.
Mastoparans, a family of small peptides, are isolated from the wasp venom. In this study, six mastoparans were identified in the venom of six Vespa species in Taiwan. The precursors of these mastoparans are composed of N-terminal signal sequence, prosequence, mature mastoparan, and appendix glycine at C-terminus. These mature mastoparans all have characteristic features of linear cationic peptides rich in hydrophobic and basic amino acids without disulfide bond. Therefore, these peptides could be predicted to adopt an amphipathic α-helical secondary structure. In fact, the CD (circular dichroism) spectra of these peptides show a high content α-helical conformation in the presence of 8 mM SDS or 40% 2,2,2-trifluoroethanol (TFE). All mastoparans exhibit mast cell degranulation activity, antimicrobial activity against both Gram-positive and -negative bacteria tested, various degree of hemolytic activity on chicken, human, and sheep erythrocytes as well as membrane permeabilization on Escherichia coli BL21. Our results also show that the hemolytic activity of mastoparans is correlated to mean hydrophobicity and mean hydrophobic moment.
