A novel bioactive peptide from wasp venom

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 am...

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Detalles Bibliográficos
Autores principales: Chen, Lingling, Chen, Wenlin, Yang, Hailong, Lai, Ren
Formato: Texto
Lenguaje:English
Publicado: Library Publishing Media 2010
Materias:
Research Report
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3086190/
https://www.ncbi.nlm.nih.gov/pubmed/21544181
Descripción
Sumario: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.

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