Title: Molecular cloning of the precursor polypeptide of mastoparan B and its putative processing enzyme, dipeptidyl peptidase IV, from the black-bellied hornet, Vespa basalis Lee VS, Tu WC, Jinn TR, Peng CC, Lin LJ, Tzen JT Ref: Insect Molecular Biology, 16:231, 2007 : PubMed
Mastoparan B, a cationic toxin, is the major peptide component in the venom of Vespa basalis. Molecular cloning of its cDNA fragment revealed that this toxin was initially synthesized as a precursor polypeptide, containing an N-terminal signal sequence, a prosequence, the mature toxin, and an appendix glycine at C-terminus. Sequence alignment between precursors of mastoparan B and melittin from honeybee venom showed a significant conservation in prosequence. Alternate positions existing in both prosequences were either proline or alanine known as the potential cleaving sites for dipeptidyl peptidase IV. Subsequently, a putative dipeptidyl peptidase IV cDNA fragment was cloned from Vespa basalis venom gland. The prosequence may possibly be removed via sequential liberation of dipeptides during the processing of mastoparan B.
Lee VS, Tu WC, Jinn TR, Peng CC, Lin LJ, Tzen JT (2007) Molecular cloning of the precursor polypeptide of mastoparan B and its putative processing enzyme, dipeptidyl peptidase IV, from the black-bellied hornet, Vespa basalis Insect Molecular Biology16: 231-7
Lee VS, Tu WC, Jinn TR, Peng CC, Lin LJ, Tzen JT (2007) Insect Molecular Biology16: 231-7
