Direct Expression of Antimicrobial Peptides in an Intact Form by a Translationally Coupled Two-Cistron Expression System

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We describe a novel prokaryotic expression system for the production of cationic antimicrobial peptides (AMPs). The method relies on a translationally coupled two-cistron system, in which the termination codon for the first cistron (which encodes the anionic polypeptide mIFc2, a derivative of human gamma interferon) overlaps with the initiation codon for the second cistron (which encodes a cationic AMP) in the sequence of 5'-TAATG-3'. By forming an insoluble complex with the AMP upon translation, the mIFc2 protein efficiently neutralized the toxicity of the coexpressed cationic AMP and minimized the sensitivity of AMP to proteolytic degradation in a host. The AMPs were retrieved from the insoluble inclusion bodies without any chemical or enzymatic cleavage step by simple cation-exchange chromatography. With our system, similar to 100 mg of various AMPs (buforin IIb, parasin I, and pexiganan) were obtained from 1 liter of Escherichia coli culture. Our expression system may represent a universal cost-effective solution for the mass production of intact AMPs in their natural forms.
Publisher
AMER SOC MICROBIOLOGY
Issue Date
2009-06
Language
English
Article Type
Article
Keywords

HOST-DEFENSE PEPTIDES; HIGH-LEVEL EXPRESSION; ESCHERICHIA-COLI; MESSENGER-RNA; ANTIBACTERIAL; INITIATION; PURIFICATION; GENERATION; EFFICIENT; PROTEIN

Citation

APPLIED AND ENVIRONMENTAL MICROBIOLOGY, v.75, no.12, pp.3980 - 3986

ISSN
0099-2240
DOI
10.1128/AEM.02753-08
URI
http://hdl.handle.net/10203/96894
Appears in Collection
BS-Journal Papers(저널논문)
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