Expression of an antimicrobial peptide magainin by a promoter inversion system

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A method was developed for the controlled expression of an antimicrobial peptide magainin in Escherichia coli. A series of concatemeric magainin genes was constructed with a gene amplification vector, and fused to the 3' end of malE gene encoding the affinity ligand, E. coil maltose-binding protein (MBP). The construct directed the synthesis of the fusion protein with the magainin polypeptide fused to the C-terminus of MBP. The fusion protein was expressed in a tightly regulatable expression system which was under the control of an invertible promoter. The MBP-fused magainin monomer was expressed efficiently. However, the expression level of the MBP-fused magainin in E. coli decreased with the increasing size of multimers possibly because of the transcription and translation inhibition by the multimeric peptides. After purification using an amylose affinity column, the fusion protein was digested by factor Xa at a specific cleavage site between the monomers. The recombinant magainin had an antimicrobial activity identical to that of synthetic magainin. This experiment shows that a biologically active, antimicrobial peptide magainin can be produced by fusing to MBP, along with a promoter inversion vector system.
Publisher
SPRINGER-VERLAG SINGAPORE PTE LTD
Issue Date
1998-02
Language
English
Article Type
Article
Keywords

CLONED GENE-EXPRESSION; ANTIBACTERIAL PEPTIDE; ESCHERICHIA-COLI; INNATE IMMUNITY; LIPID BILAYERS; DEFENSINS; CONSTRUCTION; CECROPIN; BACTERIA; PROTEINS

Citation

JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.8, no.1, pp.34 - 41

ISSN
1017-7825
URI
http://hdl.handle.net/10203/77706
Appears in Collection
BS-Journal Papers(저널논문)
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