Expression, purification and antimicrobial activity of puroindoline A protein and its mutants

文献类型： 外文期刊

第一作者： Miao, Yingjie

作者： Miao, Yingjie;Chen, Ling;Wang, Cheng;Wang, Yajuan;Zheng, Qian;Yang, Guangxiao;He, Guangyuan;Chen, Ling;Gao, Chunbao

作者机构：

关键词： Puroindoline A;Artificial mutants;Tryptophan-rich domain;Antimicrobial activity;Circular dichroism;Minimum inhibitory concentration

期刊名称：AMINO ACIDS （ 影响因子：3.52； 五年影响因子：3.6 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： Wheat puroindoline proteins, PINA and PINB, play key roles in determining wheat grain hardness as well as in defending the plant against pathogens. PINA has much greater membrane-binding property and antimicrobial activity because it contains more tryptophan residues in the unique tryptophan-rich domain (TRD). In order to obtain proteins with higher antimicrobial activity, mutants of PINA containing two or three copies of TRD, designated ABBC and ABBBC, respectively, were constructed and expressed in E. coli Rosetta-gami (DE3). Metal affinity chromatography was used to purify the soluble affinity-tagged recombinant proteins. The secondary structures of the recombinant proteins were predicted by the online program Protein Homology/analog Y Recognition Engine v2.0 and experimentally assessed using circular dichroism. Minimum inhibition concentration tests and fluorescence microscope analyses were employed to evaluate the antimicrobial activities of the mutants. The results showed that the purified recombinant ABBC was correctly folded and presented significantly higher antimicrobial activities against E. coli and S. aureus than wild-type PINA, suggesting its potential use as an antimicrobial agent. The results also confirmed that TRD is a determinant of the antimicrobial activity of PINA and demonstrated that it is feasible to enhance the antimicrobial activity of PINA by adding one copy of TRD.

分类号： Q5

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