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A cecropin-A gene was isolated from the immunized larvae of the Japanese oak silkworm, Antheraea yamamai anddesigned Ay-CecA. The complete Ay-CecA cDNA consists of 419 nucleotides with 195 bp open reading frame encod-ing a 64 amino acid precursor that contains a putative 22-residue signal peptide, a 4-residue propetide and a 37-residuemature peptide with a theoretical mass of 4046.81. The deduced amino acid sequence of the peptide evidenced a sig-nificant degree of identity (62 ~ 78% identity) with other lepidopteran cecropins. Like many insect cecropin, Ay-CecAalso harbored a glycine residue for C-terminal amidation at the C-end, which suggests potential amidation. To under-stand this peptide better, we successfully expressed bioactive recombinant Ay-CecA in Escherichia coli that are highlysensitive to the mature peptide. For this, we fused mature Ay-CecA gene with insoluble protein ketosteroid isomerase(KSI) gene to avoid the cell death during induction. The fusion KSI-CecA protein was expressed as inclusion body. Theexpressed fusion protein was purified by Ni-NTA immobilized metal affinity chromatography (IMAC), and cleaved bycyanogen bromide (CNBr) to release recombinant Ay-CecA. The purified recombinant Ay-CecA showed considerablyantibacterial activity against Gram-negative bacteria, E. cori ML 35, Klebsiella pneumonia and Pseudomonas aerug-inosa. Our results proved that this peptide with a potent antibacterial activity may play a role in the immune responseof Japanese oak silkworm.Key words : Antheraea yamamai, Cecropin, KSI-CecA, Antibacterial activity

Cloning and functional expression of a cecropin-A gene from the Japanese oak silkworm, Antheraea yamamai