Structural and biological characterization of mastoparans in the venom of Vespa species in Taiwan

• Published in: Peptides (New York, N.Y. : 1980) Vol. 32; no. 10; pp. 2027 - 2036
• Main Authors: Lin, Chun-Hsien, Tzen, Jason T.C., Shyu, Ching-Lin, Yang, Mars J., Tu, Wu-Chun
• Format: Journal Article
• Language: English
• Published: New York, NY Elsevier Inc 01.10.2011; Elsevier
• Subjects: Amino Acid Sequence; amino acids; Animals; Anti-Bacterial Agents - chemistry; Anti-Bacterial Agents - metabolism; Anti-Bacterial Agents - pharmacology; anti-infective properties; Antimicrobial activity; bacteria; Base Sequence; Biological and medical sciences; Cell Degranulation - drug effects; Chickens; disulfide bonds; erythrocytes; Escherichia coli; Fundamental and applied biological sciences. Psychology; hemolysis; Hemolysis - drug effects; Hemolytic activity; Humans; hydrophobicity; Hymenoptera; Mast cell degranulation; mast cells; Mast Cells - drug effects; Mast Cells - physiology; Mastoparans; Membrane permeabilization; Microbial Sensitivity Tests; Molecular Sequence Data; peptides; Peptides - chemistry; Peptides - genetics; Peptides - metabolism; Peptides - pharmacology; Protein Structure, Secondary; Rats; Rats, Sprague-Dawley; Sequence Alignment; Sheep; signal peptide; Taiwan; venoms; Vertebrates: endocrinology; Vespa; Vespa species; Wasp Venoms - chemistry; Wasp Venoms - genetics; Wasp Venoms - metabolism; Wasp Venoms - pharmacology; Wasps - chemistry; Taiwan; Membrane permeabilization; Antimicrobial activity; Hemolytic activity; Vespa species; Mastoparans; Mast cell degranulation; Characterization; Venom; Degranulation; Mast cell; Antibacterial agent; Antimicrobial agent
• DOI: 10.1016/j.peptides.2011.08.015
• ISSN: 0196-9781; 1873-5169

► Five cDNAs of precursor polypeptide of MPs were first identified. ► MPs adopt α-helical conformation in the presence of 40% TFE or 8mM SDS. ► All MPs exhibit multifunctional activity, i.e., mast cell degranulation activity; antimicrobial activity against Gram-positive and Gram-negative bacteria; hemolytic activity on chicken, human, and sheep erythrocytes; membrane permeabilization on E. coli BL21. 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 8mM 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.