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Design and high-level expression of a hybrid antimicrobial peptide LF15-CA8 in Escherichia coli

文献类型： 外文期刊

作者： Feng, Xing-Jun 1 ; Xing, Li-Wei 1 ; Liu, Di 1 ; Song, Xue-Ying 1 ; Liu, Chun-Long 2 ; Li, Jing 1 ; Xu, Wen-Shan 1 ; Li, Z 1 ;

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

2.Chinese Acad Sci, Key Lab Mollisols Agroecol, Northeast Inst Geog & Agroecol, Harbin 150081, Peoples R China

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

关键词： Antimicrobial peptides;LfcinB;Cecropin;Recombinant expression;Antibacterial activity

期刊名称：JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY （ 影响因子：3.346； 五年影响因子：3.426 ）

ISSN： 1367-5435

年卷期： 2014 年 41 卷 3 期

页码：

收录情况： SCI

摘要： Antimicrobial peptides (AMPs) have been paid considerable attention owing to their broad-spectrum antimicrobial activity and have great potential as novel antimicrobials. In this study, a novel hybrid peptide LF15-CA8 was designed on the basis of bovine lactoferricin (LfcinB) and cecropin A. The gene segment encoding LF15-CA8 was synthesized and cloned into pGEX-4T-BH to form pGEX-4T-LC1 containing one copy of the LF15-CA8 coding region. A series of recombinant vectors containing up to six multiple-copy LF15-CA8 coding regions, i.e., pGEX-4T-LCn (n = 1-6), were subsequently constructed, and used for transformation in Escherichia coli BL21(DE3). After induction with IPTG, pGEX-4T-LC1 and pGEX-4T-LC2 transformants successfully expressed fusion proteins GST-LF15-CA8 and GST-(LF15-CA8)(2) in the form of inclusion bodies, respectively. The inclusion bodies were dissolved and the peptide was successfully released in 70 % formic acid in a single step. After purification, about 10.0 mg of the recombinant peptide LF15-CA8 with purity more than 97 % was obtained from 1 l of bacteria culture of pGEX-4T-LC2 transformants. LF15-CA8 caused an increase in antibacterial activity against Gram-positive bacterium (Staphylococcus aureus ATCC 25923) compared with the parent peptides and did not show obvious hemolytic activity against human erythrocytes in the range of effective antibacterial concentration. These results suggest that the peptide LF15-CA8 could be a promising candidate for therapeutic applications, and may lead to a cost-effective solution for the large-scale production of AMPs.

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[1]High-Yield Recombinant Expression of the Chicken Antimicrobial Peptide Fowlicidin-2 in Escherichia coli. Feng, Xingjun,Xu, Wenshan,Qu, Pei,Li, Xiaochong,Xing, Liwei,Liu, Di,Jiao, Jian,Wang, Jue,Li, Zhongqiu,Liu, Chunlong,Liu, Chunlong.

[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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