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Molecular cloning of the precursor polypeptide of mastoparan B and its putative processing enzyme, dipeptidyl peptidase IV, from the black‐bellied hornet, Vespa basalis
Author(s) -
Lee V. S. Y.,
Tu W.C.,
Jinn T.R.,
Peng C.C.,
Lin L.J.,
Tzen J. T. C.
Publication year - 2007
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1111/j.1365-2583.2006.00718.x
Subject(s) - biology , enzyme , dipeptidyl peptidase , cloning (programming) , dipeptidyl peptidase 4 , biochemistry , microbiology and biotechnology , endocrinology , type 2 diabetes , diabetes mellitus , computer science , programming language
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.