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- Title
High-Level Production of a Novel Antimicrobial Peptide Perinerin in Escherichia coli by Fusion Expression.
- Authors
Qing-Feng Zhou; Xue-Gang Luo; Liang Ye; Tao Xi
- Abstract
Perinerin is a small antimicrobial peptide (AMP) isolated from an Asian marine clamworm, Perinereis aibuhitensis Grube. It shows marked activity in vitro against both Gram-negative and Gram-positive bacteria. To obtain it in large amounts, the coding sequence of perinerin was cloned into pET32a(+) vector and expression as a Trx fusion protein in Escherichia coli. The soluble fusion protein collected from the supernatant of the cell lyste was separated by Ni2+-chelating chromatography. The purified protein was then cleaved by Factor Xa protease to release mature perinerin. Final purification was achieved by ion-exchange chromatography. Recombinant perinerin exhibited a similar antimicrobial activity to the native perinerin. These works might provide a significant foundation for the following research on the action of mechanism of marine AMPs.
- Subjects
ESCHERICHIA; ENTEROBACTERIACEAE; ESCHERICHIA coli; GRAM-positive bacteria; PHYSICAL &; theoretical chemistry; CHROMATOGRAPHIC analysis; FUNGUS-bacterium relationships; ANTIMICROBIAL peptides
- Publication
Current Microbiology, 2007, Vol 54, Issue 5, p366
- ISSN
0343-8651
- Publication type
Article
- DOI
10.1007/s00284-006-0466-y