Multimeric expression of the antimicrobial peptide buforin II in Escherichia coli by fusion to a cysteine-rich acidic peptide

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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 TI 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 mg of pure buforin II was obtained per 1 l 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.
Publisher
SPRINGER-VERLAG SINGAPORE PTE LTD
Issue Date
1999-06
Language
English
Article Type
Article
Keywords

XENOPUS-LAEVIS; ANTIBACTERIAL PEPTIDE; INNATE IMMUNITY; LIPID BILAYERS; DEFENSINS; SYSTEM; SKIN; MAGAININ; DNA; INHIBITOR

Citation

JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.9, no.3, pp.303 - 310

ISSN
1017-7825
URI
http://hdl.handle.net/10203/77673
Appears in Collection
BS-Journal Papers(저널논문)
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