Research Report

J Venom Res (2010), Vol 1, 43-47

Published online: 30 September 2010

Full Text: (PDF ~146kb) | (PubMed Central Record HTML)

Lingling Chen †‡, Wenlin Chen ‡§, Hailong Yang †, Ren Lai †*

† Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, Yunnan, China

‡ Clinical Laboratory, the First Affiliated Hospital of Kunming Medical College, Kunming 650032, Yunnan, Chin

§ Yunnan Clinical Research Center of Breast Cancer, the Third Affiliated Hospital of Kunming Medical College, Kunming 650032 , Yunnan, China

*Correspondence to: Ren Lai, Email:, Tel: +86 871 5196202, Fax: +86 871 5199086

Received: 09 August 2010, Revised: 01 September 2010, Accepted: 03 September 2010

© Copyright The Authors


Wasp venoms contain a number of pharmacologically active biomolecules, undertaking a wide range of functions necessary for the wasp’s survival. We purified and characterized a novel bioactive peptide (vespin) from the venoms of Vespa magnifica (Smith) wasps with unique primary structure. Its amino acid sequence was determined to be CYQRRVAITAGGLKHRLMSSLIIIIIIRINYLRDNSVIILESSY. It has 44 residues including 15 leucines or isoleucines (32%) in the sequence. Vespin showed contractile activity on isolated ileum smooth muscle. The cDNA encoding vespin precursor was cloned from the cDNA library of the venomous glands. The precursor consists of 67 amino acid residues including the predicted signal peptide and mature vespin. A di-basic enzymatic processing site (-KR-) is located between the signal peptide and the mature peptide. Vespin did not show similarity with any known proteins or peptides by BLAST search, suggesting it is a novel bioactive peptide from wasp venoms.

KEYWORDS: Wasp venom, Vespa magnifica, smooth muscle, contraction, novel peptide