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KMID : 0545119990090030303
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Journal of Microbiology and Biotechnology
1999 Volume.9 No. 3 p.303 ~ p.310
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Multimeric Expression of the Antimicrobial Peptide Buforin 2 in Escherichia coli by Fusion to a Cysteine-Rich Acidic Peptide
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Lee, Jae Hyun
Kim, Jeong Hyun/Hong, Seung Suh/Lee, Hyun Soo/Kim, Sun Chang
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Abstract
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A cost-effective mass production method for a strong antimicrobial peptide, buforin Ⅱ, which was isolated from the stomach of Bufo bufo gargarizans, has been developed. This method is based on the neutralization of the positive charge of buforin Ⅱ by fusion with a cysteine-rich acidic peptide (CAP) to avoid any lethal effect on the host. The neutralized fusion peptide was multimerized and expressed in Escherichia coli as tandem repeats to increase the production yield. Multimers of the CAP-buforin Ⅱ fusion peptide were successfully expressed at high levels in E. coli as inclusion bodies. More than 100 ㎎ of pure buforin Ⅱ was obtained per 1 1 of E. coli culture after cleaving the multimeric polypeptide with CNBr. The buforin Ⅱ obtained from the recombinant E. coli had antimicrobial activity identical to that of natural buforin Ⅱ. The proposed expression system can provide a cost-effective mass production method for both antimicrobial peptides and other host-lethal basic proteins.
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