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High-Yield Recombinant Expression of the Chicken Antimicrobial Peptide Fowlicidin-2 in Escherichia coli

文献类型： 外文期刊

作者： Feng, Xingjun 1 ; Xu, Wenshan 1 ; Qu, Pei 1 ; Li, Xiaochong 1 ; Xing, Liwei 1 ; Liu, Di 1 ; Jiao, Jian 1 ; Wang, Jue 1 ; Li, 1 ;

作者机构： 1.Northeast Agr Univ, Coll Anim Sci & Technol, Harbin 150030, Peoples R China

2.Heilongjiang Acad Agr Sci, Anim Husb Res Ctr, Harbin 150086, Peoples R China

3.Chinese Acad Sci, Northeast Inst Geog & Agr Ecol, Harbin 150081, Peoples R China

4.Collaborat Innovat Ctr Dev & Utilizat Forest Reso, Harbin 150040, Peoples R China

关键词： recombinant expression;antimicrobial peptides;fowlicidin-2;cyanogen bromide;Escherichia coli;antibacterial activity

期刊名称：BIOTECHNOLOGY PROGRESS （ 影响因子：2.681； 五年影响因子：2.691 ）

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收录情况： SCI

摘要： The antimicrobial peptide fowlicidin-2 identified in chicken is a member of the cathelicidins family. The mature fowlicidin-2 possesses high antibacterial efficacy and lipopolysaccharide (LPS) neutralizing activity, and also represents an excellent candidate as an antimicrobial agent. In the present study, the recombinant fowlicidin-2 was successfully produced by Escherichia coli (E. coli) recombinant expression system. The gene encoding fowlicidin-2 with the codon preference of E. coli was designed through codon optimization and synthesized in vitro. The gene was then ligated into the plasmid pET-32a(+), which features fusion protein thioredoxin at the N-terminal. The recombinant plasmid was transformed into E. coli BL21(DE3) and cultured in Luria-Bertani (LB) medium. After isopropyl--D-thiogalactopyranoside (IPTG) induction, the fowlicidin-2 fusion protein was successfully expressed as inclusion bodies. The inclusion bodies were dissolved and successfully released the peptide in 70% formic acid solution containing cyanogen bromide (CNBr) in a single step. After purification by reverse-phase high-performance liquid chromatography (RP-HPLC), approximate to 6.0 mg of fowlicidin-2 with purity more than 97% was obtained from 1 litre of bacteria culture. The recombinant peptide exhibited high antibacterial activity against the Gram-positive and Gram-negative bacteria, and even drug-resistant strains. This system could be used to rapidly and efficiently produce milligram quantities of a battery of recombinant antimicrobial peptides as well as for large-scale production. (c) 2015 American Institute of Chemical Engineers Biotechnol. Prog., 31:369-374, 2015

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[1]Design and high-level expression of a hybrid antimicrobial peptide LF15-CA8 in Escherichia coli. Feng, Xing-Jun,Xing, Li-Wei,Liu, Di,Song, Xue-Ying,Li, Jing,Xu, Wen-Shan,Liu, Chun-Long,Li, Zhong-Qiu. 2014

[2]Recombinant expression, purification, and antimicrobial activity of a novel hybrid antimicrobial peptide LFT33. Feng, Xingjun,Guo, Jiayin,Song, Xueying,Li, Jing,Xu, Wenshan,Liu, Chunlong,Li, Zhongqiu. 2012

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