Design, expression and characterization of the hybrid antimicrobial peptide LHP7, connected by a flexible linker, against Staphylococcus and Streptococcus

文献类型： 外文期刊

第一作者： Xi, Di

作者： Xi, Di;Xiang, Wensheng;Xi, Di;Teng, Da;Wang, Xiumin;Mao, Ruoyu;Yang, Yalin;Wang, Jianhua;Xi, Di;Teng, Da;Wang, Xiumin;Mao, Ruoyu;Yang, Yalin;Wang, Jianhua

作者机构：

关键词： Hybrid antimicrobial peptide;Expression;Pichia pastoris;Staphylococcus aureus;Hemolysis;Stability

期刊名称：PROCESS BIOCHEMISTRY （ 影响因子：3.757； 五年影响因子：3.665 ）

ISSN： 1359-5113

年卷期： 2013 年 48 卷 3 期

页码：

收录情况： SCI

摘要： The emergence of bacterial resistance to common antibiotics poses a threat to human health and has rekindled an interest in antimicrobial peptides (AMPs). LHP7, a novel hybrid AMP containing 83 amino acid residues was designed on the basis of the LH28 and plectasin. LHP7 was expressed in Pichia pastoris, the total concentration of secreted protein reached 0.906 g/L after 108 h of methanol induction. Its antimicrobial activity was higher than that of the parent AMPs; the minimal inhibitory concentrations (MICs) of LHP7 against Staphylococcus aureus, Streptococcus pneumoniae and Streptococcus suis were 0.091, 0.023 and 0.18 mu M, respectively. The antibacterial activity of LHP7 against clinical MRSA isolates (MICs = 0.73-2.91 mu M) was enhanced over that of plectasin. The fractional inhibitory concentration (FIC) indicated a synergistic effect between LHP7 and ampicillin against MRSA (FIC = 0.375), and combinations of LHP7 with gentamicin, rifampin or tetracycline provided evidence of additive effects (FIC = 0.625-1.0). LHP7 exhibited a broad range of pH stability and thermostability, and a hemolytic activity of less than 5% below a concentration of 500 mu g/mL. It was resistant to pepsin and papain digestion, but sensitive to trypsin digestion. These results suggest that LHP7 might have potential as a broadly applied and clinically useful antimicrobial agent. (C) 2013 Elsevier Ltd. All rights reserved.

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