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Production of a cytotoxic cationic antibacterial peptide in Escherichia coli using SUMO fusion partner.

Authors
Type
Published Article
Journal
Applied Microbiology and Biotechnology
1432-0614
Publisher
Springer-Verlag
Publication Date
Volume
84
Issue
2
Pages
383–388
Identifiers
DOI: 10.1007/s00253-009-2109-2
PMID: 19582446
Source
Medline
License
Unknown

Abstract

Antibacterial peptide CM4 (ABP-CM4) is a small cationic peptide with broad-spectrum activities against bacteria, fungi, and tumor cells, which may possibly be used as an antimicrobial agent. We report here the application of small ubiquitin-related modifier (SUMO) fusion technology to the expression and purification of cationic antibacterial peptide ABP-CM4. The fusion protein expressed in a soluble form was purified to a purity of 90% by Ni-IDA chromatography and 112 mg protein of interest was obtained per liter of fermentation culture. After the SUMO-CM4 fusion protein was cleaved by the SUMO protease at 30 degrees C for 1 h, the cleaved sample was re-applied to a Ni-IDA. Finally, about 24 mg recombinant CM4 was obtained from 1 l fermentation culture with no less than 96% purity and the recombinant CM4 had similar antimicrobial properties to the synthetic CM4. Thus, the SUMO-mediated peptide expression and purification system potentially could be employed for the production of recombinant cytotoxic peptides.

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