cDNA Encoding Precursors of the Bee-Venom Peptides Melittin and Secapin

  • R. Vlasak
  • I. Malec
  • G. Kreil
Part of the Molecular Biology and Biophysics book series (MBB)


The venom gland of honeybees is a Y-shaped, tubular structure that contains highly polyploid cells. The secretion produced by the gland cells is collected in a central duct and stored in the venom sac. Whereas the large venom gland of queen bees operates at maximal capacity in newly emerged animals, venom production in worker bees starts slowly after emergence and then increases gradually over a period of about 2 wk (1). Worker bee venom is available in large quantities and its constituents have been studied in great detail (2,3,). In addition to small amounts of biogenic amines, the enzymes and peptides listed in Table 1 have been isolated from this venom. Even though worker and queen bees are genetically identical, their venoms differ markedly. Phospholipase A2, which is barely detectable in queen bee venom (4), is one of the differences noted (5). However, in both cases, melittin is the main venom constituent. This peptide was discovered through it lytic action on cells and liposomes. The primary structure of melittin, which is composed of 26 amino acids, was established by Habermann and Jentsch (6). The interaction of this peptide with natural and artificial phospholipid bilayers was studied extensively by various biophysical and biochemical methods (see ref. 7 for a brief summary), and the crystal structure of the melittin tetramer was elucidated (8).


Codon Amide Carboxyl Polypeptide Arginine 


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© The Humana Press Inc. 1987

Authors and Affiliations

  • R. Vlasak
  • I. Malec
  • G. Kreil

There are no affiliations available

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