A Novel Thioredoxin-Dependent Peroxiredoxin (TPx-Q) Plays an Important Role in Defense Against Oxidative Stress and Is a Possible Drug Target in Babesia microti
Identifieur interne : 000234 ( an2020/Analysis ); précédent : 000233; suivant : 000235A Novel Thioredoxin-Dependent Peroxiredoxin (TPx-Q) Plays an Important Role in Defense Against Oxidative Stress and Is a Possible Drug Target in Babesia microti
Auteurs : Houshuang Zhang ; Zhonghua Wang ; Jingwei Huang ; Jie Cao ; Yongzhi Zhou ; Jinlin ZhouSource :
- Frontiers in Veterinary Science [ 2297-1769 ] ; 2020.
Abstract
Thioredoxin peroxidases (TPxs) are ubiquitous cysteine-based peroxidases that reduce peroxides as part of antioxidant defenses and redox signaling and are essential for
Url:
DOI: 10.3389/fvets.2020.00076
PubMed: 32133382
PubMed Central: 7040034
Affiliations:
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<author><name sortKey="Wang, Zhonghua" sort="Wang, Zhonghua" uniqKey="Wang Z" first="Zhonghua" last="Wang">Zhonghua Wang</name>
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<author><name sortKey="Huang, Jingwei" sort="Huang, Jingwei" uniqKey="Huang J" first="Jingwei" last="Huang">Jingwei Huang</name>
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<author><name sortKey="Cao, Jie" sort="Cao, Jie" uniqKey="Cao J" first="Jie" last="Cao">Jie Cao</name>
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<author><name sortKey="Zhou, Yongzhi" sort="Zhou, Yongzhi" uniqKey="Zhou Y" first="Yongzhi" last="Zhou">Yongzhi Zhou</name>
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<author><name sortKey="Zhou, Jinlin" sort="Zhou, Jinlin" uniqKey="Zhou J" first="Jinlin" last="Zhou">Jinlin Zhou</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">A Novel Thioredoxin-Dependent Peroxiredoxin (TPx-Q) Plays an Important Role in Defense Against Oxidative Stress and Is a Possible Drug Target in <italic>Babesia microti</italic>
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<author><name sortKey="Zhang, Houshuang" sort="Zhang, Houshuang" uniqKey="Zhang H" first="Houshuang" last="Zhang">Houshuang Zhang</name>
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<author><name sortKey="Wang, Zhonghua" sort="Wang, Zhonghua" uniqKey="Wang Z" first="Zhonghua" last="Wang">Zhonghua Wang</name>
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<author><name sortKey="Huang, Jingwei" sort="Huang, Jingwei" uniqKey="Huang J" first="Jingwei" last="Huang">Jingwei Huang</name>
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<author><name sortKey="Cao, Jie" sort="Cao, Jie" uniqKey="Cao J" first="Jie" last="Cao">Jie Cao</name>
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<author><name sortKey="Zhou, Yongzhi" sort="Zhou, Yongzhi" uniqKey="Zhou Y" first="Yongzhi" last="Zhou">Yongzhi Zhou</name>
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<author><name sortKey="Zhou, Jinlin" sort="Zhou, Jinlin" uniqKey="Zhou J" first="Jinlin" last="Zhou">Jinlin Zhou</name>
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<series><title level="j">Frontiers in Veterinary Science</title>
<idno type="eISSN">2297-1769</idno>
<imprint><date when="2020">2020</date>
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<front><div type="abstract" xml:lang="en"><p>Thioredoxin peroxidases (TPxs) are ubiquitous cysteine-based peroxidases that reduce peroxides as part of antioxidant defenses and redox signaling and are essential for <italic>Babesia microti</italic>
protection against adverse environment agents like reactive oxygen species (ROS) and reactive nitrogen species (RNS). To better systematically understand TPxs, we identified a novel 2-Cys peroxiredoxin-Q (BmTPx-Q) of <italic>B. microti</italic>
. The full-length BmTPx-Q gene is 653 bp that consists of an intact open reading frame of 594 bp that encodes a 197-amino acid protein. The predicted protein has a molecular weight of 22.3 kDa and an isoelectric point of 9.18. Moreover, BmTPx-Q showed low identity at the amino acid level to other peroxiredoxins (Prxs) among the currently known subfamilies. The recombinant BmTPx-Q protein (rBmTPx-Q) was expressed in <italic>Escherichia coli</italic>
and purified with beads. The native protein BmTPx-Q was detected using mouse anti-BmTPx-Q polyclonal serum with western blotting and indirect immunofluorescence assay (IFA). In addition, enzyme activity was observed using nicotinamide adenine dinucleotide phosphate (NADPH) as substrate and triggered the NADPH-dependent reduction of the Trx/TrxR system. It was also discovered that BmTPx-Q mainly exists as a monomer whether under its native or functional states. In addition, when incubated with Chloroquine diphosphate salt for 24 h <italic>in vitro</italic>
, the expression of BmTPx-Q showed a marked downward trend with the increase of drug concentration. These results suggest that <italic>B. microti</italic>
uses BmTPx-Q to reduce and detoxify hydrogen peroxides to survive and proliferate inside the host. Furthermore, BmTPx-Q showed the lowest identity with host enzymes and could be a potential drug target for the development of novel strategies to control <italic>B. microti</italic>
infection.</p>
</div>
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<tree><noCountry><name sortKey="Cao, Jie" sort="Cao, Jie" uniqKey="Cao J" first="Jie" last="Cao">Jie Cao</name>
<name sortKey="Huang, Jingwei" sort="Huang, Jingwei" uniqKey="Huang J" first="Jingwei" last="Huang">Jingwei Huang</name>
<name sortKey="Wang, Zhonghua" sort="Wang, Zhonghua" uniqKey="Wang Z" first="Zhonghua" last="Wang">Zhonghua Wang</name>
<name sortKey="Zhang, Houshuang" sort="Zhang, Houshuang" uniqKey="Zhang H" first="Houshuang" last="Zhang">Houshuang Zhang</name>
<name sortKey="Zhou, Jinlin" sort="Zhou, Jinlin" uniqKey="Zhou J" first="Jinlin" last="Zhou">Jinlin Zhou</name>
<name sortKey="Zhou, Yongzhi" sort="Zhou, Yongzhi" uniqKey="Zhou Y" first="Yongzhi" last="Zhou">Yongzhi Zhou</name>
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