We found that baculoviral polyhedrin (Polh) used as a fusion partner for recombinant expression in Escherichia coli showed almost the same characteristics (rapid solubilization under alkaline conditions and specific degradation by specific alkaline proteases in insect midgut) as the native baculoviral Polh,and formed easily isolatable inclusion bodies.We investigated the use of the Polh protein as a fusion partner for production of an antimicrobial peptide (AMP) (halocidin 18 subunit; Hall8) in E.coli.The recombinant Hall8 AMP could then be hydroxylamine cleaved fiom the fusion protein and easily recovered by simple dialysis and centrifugation.This was facilitated by the fact that Polh was soluble in the alkaline cleavage reaction but became insoluble during dialysis at a neutral pH.Importantly,recombinant and synthetic Hall 8 peptides showed nearly identical antimicrobial activities against E.coli and Staphylococcus aurcus,which were used as representative Gram-negative and Gram-positive bacteria,respectively.These results demonstrated that baculoviral Polh can provide an efficient and facile platform for production and separation of target AMPs.