Molecular cloning and characterization of a diapause-specific peptide in the beet armyworm, Spodoptera exigua

Abstract

The leaf beetle, Gastrophysa atrocyanea, diapause-specific peptide (DSP), which plays a role in diapause, inhibits Ca2+ channels and has antifungal activity. Here, we show the molecular cloning and characterization of a diapause-specific peptide in the beet armyworm Spodoptera exigua. The S. exigua diapause-specific peptide (SeDSP) gene consists of only one exon encoding 63 amino acid residues. A comparative analysis showed that mature SeDSP consists of 40 amino acid residues including six cysteines, which are similar to those of S. littoralis Spodomicin and G. atrocyanea DSP. The SeDSP was expressed as a 4.5kDa peptide in baculovirus-infected insect cells. SeDSP was constitutively expressed in the epidermis of S. exigua larvae and pupae after molting and metamorphosis. In addition, recombinant SeDSP showed antibacterial activity against Bacillus megaterium.