Structure and biological activities of a new mastoparan isolated from the venom of the hornet Vespa basalis

C. L. Ho, L. L. Hwang

Research output: Contribution to journalArticle

61 Citations (Scopus)

Abstract

By gel filtration on a Fractogel TSK HW 50 column followed by cation-exchange chromatography on CM-Trisacryl M, a tetradecapeptide amide, designated 'mastoparan B', was purified from the venom of the hornet Vespa basalis. Its amino acid sequence was determined as: Leu-Lys-Leu-Lys-Ser-Ile-Val-Ser-Trp-Ala-Lys-Lys-Val-Leu-NH2 and its molecular mass was measured to be 1611 Da by fast-atom-bombardment mass spectrometry. In addition to having a common structure of vespid mastoparans, the peptide shows a less hydrophobic sequence at positions 1, 2, 5, 8 and 9. The peptide caused liberation of histamine from rat peritoneal mast cells and induced oedema in the rat paw. However, the latter effect was inhibited by 'anti-serotonin' (anti-5-hydroxytryptamine) (cyproheptadine), but not by antihistamine (chlorpheniramine). The peptide also possesses a potent haemolytic activity which acts in synergy with the lethal protein of the venom, suggesting the possible involvement of mastoparan B in the lethal effect of Vespa basalis venom.

Original languageEnglish
Pages (from-to)453-456
Number of pages4
JournalBiochemical Journal
Volume274
Issue number2
Publication statusPublished - 1991
Externally publishedYes

Fingerprint

Wasp Venoms
Wasps
Venoms
Bioactivity
Peptides
Rats
Serotonin
Chlorpheniramine
Fast Atom Bombardment Mass Spectrometry
Cyproheptadine
Histamine Release
Histamine Antagonists
Molecular mass
Chromatography
Mast Cells
Amides
Histamine
Gel Chromatography
Mass spectrometry
Cations

ASJC Scopus subject areas

  • Biochemistry

Cite this

Structure and biological activities of a new mastoparan isolated from the venom of the hornet Vespa basalis. / Ho, C. L.; Hwang, L. L.

In: Biochemical Journal, Vol. 274, No. 2, 1991, p. 453-456.

Research output: Contribution to journalArticle

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