A Novel Bioactive Peptide with Myotropic Activity from Wasp Venoms

• Published in: Chinese journal of natural medicines Vol. 9; no. 4; pp. 317 - 320
• Main Authors: YAN, Hong-Li, CHEN, Wen-Lin, CHEN, Ling-Ling, LAI, Ren, LIU, Jing-Ze
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 2011
• Subjects: amino acids; bioactive properties; bioassays; cDNA libraries; chemical composition; complementary DNA; Contraction; gel chromatography; high performance liquid chromatography; ileum; mass spectrometry; signal peptide; Smooth muscle; venoms; Vespa; Vespa bicolor; Wasp venoms; China; Smooth muscle; Vespa bicolor; Wasp venoms; Contraction
• ISSN: 1875-5364; 1875-5364
• DOI: 10.1016/S1875-5364(11)60069-1

To study the chemical constituents of the venom of Vespa bicolor Fabricius collected from Shanxi Province, China. Gel chromatography and HPLC were applied to isolate a peptide from the venom. Mass spectrometry and Edman degradation were used for its structural characterization. The cDNA encoding vespin-BF precursor was cloned from the cDNA library of the venomous glands. The synthetic peptide was used for its bioassay. A novel bioactive peptide (vespin-BF) with unique primary structure was purified and characterized. Its amino acid sequence was determined as TYQRKMAITAGAVKHRLMSTTIIIILVRIE YLRDNMVISLESSF. Vespin-BF induced contraction of isolated ileum smooth muscle. The precursor is composed of 67 amino acid residues including the predicted signal peptide and mature vespin-BF. A di-basic enzymatic processing site (-KR-) was located between the signal and the mature peptide. BLAST search indicated that vespin-BF shows obvious similarity to vespin identified from the venoms of Vespa magnifica. A novel bioactive peptide from the wasp venoms was characterized.