Identification and functional study of a novel 2-cys peroxiredoxin (BmTPx-1) of Babesia microti

文献类型： 外文期刊

第一作者： Zhang, Houshuang

作者： Zhang, Houshuang;Wang, Zhonghua;Gong, Haiyan;Cao, Jie;Zhou, Yongzhi;Zhou, Jinlin;Zhou, Jinlin

作者机构：

关键词： Babesia microti;Peroxiredoxin;Antioxidant enzyme

期刊名称：EXPERIMENTAL PARASITOLOGY （ 影响因子：2.011； 五年影响因子：2.132 ）

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收录情况： SCI

摘要： Babesia microti is an emerging human pathogen and the primary causative agent of human babesiosis in many regions of the world. Although the peroxiredoxins (Prxs) or thioredoxin peroxidases (TPx) enzymes of this parasite have been sequenced and annotated, their biological properties remain largely unknown. Prxs are a family of antioxidant enzymes that protect biological molecules against metabolically produced reactive oxygen species (ROS) and reduce hydrogen peroxide (H2O2) to water in both eukaryotes and prokaryotes. In this study, TPx-1 cDNA was cloned from B. microti (designated BmTPx-1). Recombinant BmTPx-1 (rBmTPx-1) was expressed in Escherichia coli as a histidine fusion protein and purified using Ni-NTA His bind resin. To test the defense capacity of enzymatic antioxidants against the effect of ROS, a mixed-function oxidation system was utilized with the recombinant BmTPx-1 protein. A decreased ability of rBmTPx-1 to donate electrons to the thioredoxin (Trx)/TrxR reductase system was clarified by reaction with H2O2. These results suggest that BmTPx-1 has a great impact on protecting parasites from oxidative stress in the erythrocytic stage. (C) 2016 Elsevier Inc. All rights reserved.

分类号： Q958.9

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