GAP-initiated constitutive expression of a novel plectasin-derived peptide MP1106 by Pichia pastoris and its activity against Streptococcus suis

文献类型： 外文期刊

第一作者： Jiao, Jian

作者： Jiao, Jian;Feng, Xingjun;Jiao, Jian;Mao, Ruoyu;Wang, Xiumin;Zhang, Yong;Teng, Da;Wang, Jianhua;Jiao, Jian;Mao, Ruoyu;Wang, Xiumin;Zhang, Yong;Teng, Da;Wang, Jianhua

作者机构：

关键词： Antimicrobial peptide;MP1106;GAP promoter;Streptococcus suis;Pichia pastoris

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： 2015 年 50 卷 2 期

页码：

收录情况： SCI

摘要： MP1106 is a novel variant of plectasin with potent activity against some Gram-positive pathogenic bacteria, especially for Streptococcus suis and Staphylococcus aureus. MP1106 was successfully expressed in Pichia pastoris X-33 using the glyceraldehyde-3-phosphate dehydrogenase (GAP) promoter. The total protein concentration and antimicrobial activity were 998.3 mg/L and 51,200 AU/mL, respectively. After purification by cation exchange chromatography, recombinant MP1106 (rMP1106) with a concentration of 100.13 mg/L and a purity of 95.2% was obtained from fermentation culture. Its antimicrobial spectrum was similar to that of plectasin, and the antibacterial activity against S. suis CVCC3309 was enhanced up to 29-fold over that of plectasin. In addition, 97.9% of the S. suis CVCC606 bacteria were killed by 16x minimal inhibitory concentration (MIC) rMP1106 within 6 h. The percentage hemolysis by rMP1106 against mouse erythrocytes was 3.8% at a concentration of 512 mu g/mL. Exposure of porcine intestinal epithelial cells to 16-128 mu g/mL rMP1106 caused a 9.5% decrease in cell viability. The rMP1106 was stable over broad ranges of temperature, pH and NaCl concentration. In addition, rMP1106 was highly resistant to papain, proteinase K and snailase digestion but susceptible to trypsin and slightly susceptible to pepsin. These results suggested that rMP1106 has potential as a promising therapeutic drug against S. suis infections. (C) 2014 Elsevier Ltd. All rights reserved.

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