High-level expression of human beta-defensin-2 gene with rare codons in E. coli cell-free system.

Abstract:

:Human beta-defensin-2 (hBD2) is A small cationic peptide with A broad range of antimicrobial activity. An E. coli cell-free system was employed to express the hBD2 fusion protein by using the hBD2 gene with 14 rare codons. The results showed that the expression level of trxA-hBD2 fusion protein was 0.35 mg/ml, which is the same as that obtained with A synthetic codon-optimized gene. By using another fusion partner (GFP), similar high-level expression was also achieved in this cell-free system. This meant that human beta-defensin-2 gene could be directly used to express hBD2 fusion protein efficiently in an E. coli cell-free system without the optimization of codons. The expression level of hBD2 fused with thioredoxin could be further improved up to 2.0 mg/ml by adopting A continuous exchange cell-free system. A simple one-stage affinity purification procedure was also developed to recover this fusion protein efficiently.

journal_name

Protein Pept Lett

authors

Chen H,Xu Z,Cen P

doi

10.2174/092986606775101724

subject

Has Abstract

pub_date

2006-01-01 00:00:00

pages

155-62

issue

2

eissn

0929-8665

issn

1875-5305

journal_volume

13

pub_type

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