Enhanced soluble production of cholera toxin B subunit in Escherichia coil by co-expression of SKP chaperones

文献类型： 外文期刊

第一作者： Zhang, Yuanpeng

作者： Zhang, Yuanpeng;Qiao, Xuwen;Yu, Xiaoming;Chen, Jin;Hou, Liting;Bi, Zhixiang;Zheng, Qisheng;Hou, Jibo;Zhang, Yuanpeng;Qiao, Xuwen;Yu, Xiaoming;Chen, Jin;Hou, Liting;Bi, Zhixiang;Zheng, Qisheng;Hou, Jibo

作者机构：

关键词： Recombinant cholera toxin B subunit;SKP;Chaperones;Co-expression

期刊名称：PROTEIN EXPRESSION AND PURIFICATION （ 影响因子：1.65； 五年影响因子：1.548 ）

ISSN： 1046-5928

年卷期： 2017 年 138 卷

页码：

收录情况： SCI

摘要： The cholera toxin B subunit (CTB) is a nontoxic portion of the cholera toxin that retains mucosal adjuvant properties. Expression of CTB in Escherichia coli is difficult as CTB aggregates and accumulates as insoluble inclusion bodies. To remedy this problem, the periplasmic chaperone, SKP, was investigated as possible co-expression partner to increase the solubility of recombinant CTB (rCTB) in E. coil. The result showed co-expression of SKP enhanced the soluble expression of rCTB in E. coli. Moreover, soluble rCTB was successfully expressed and secreted into the periplasmic space through the direction of the LTB leader signal. rCTB in periplasm was purified using an immobilized D-galactose resin; GM1-ELISA ex-periments showed that rCTB retains strong GM1 ganglioside-binding activity. Intranasal administration of ovalbumin (OVA) with rCTB significantly induced both mucosal and humoral immune responses specific to OVA. These data indicate that co-expression of the molecular chaperone SKP with CTB increased the solubility of rCTB while maintaining its function. (c) 2017 Elsevier Inc. All rights reserved.

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