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 : 000583 ( Pmc/Curation ); précédent : 000582; suivant : 000584A 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
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">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></title><author><name sortKey="Zhang, Houshuang" sort="Zhang, Houshuang" uniqKey="Zhang H" first="Houshuang" last="Zhang">Houshuang Zhang</name></author><author><name sortKey="Wang, Zhonghua" sort="Wang, Zhonghua" uniqKey="Wang Z" first="Zhonghua" last="Wang">Zhonghua Wang</name></author><author><name sortKey="Huang, Jingwei" sort="Huang, Jingwei" uniqKey="Huang J" first="Jingwei" last="Huang">Jingwei Huang</name></author><author><name sortKey="Cao, Jie" sort="Cao, Jie" uniqKey="Cao J" first="Jie" last="Cao">Jie Cao</name></author><author><name sortKey="Zhou, Yongzhi" sort="Zhou, Yongzhi" uniqKey="Zhou Y" first="Yongzhi" last="Zhou">Yongzhi Zhou</name></author><author><name sortKey="Zhou, Jinlin" sort="Zhou, Jinlin" uniqKey="Zhou J" first="Jinlin" last="Zhou">Jinlin Zhou</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">32133382</idno><idno type="pmc">7040034</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7040034</idno><idno type="RBID">PMC:7040034</idno><idno type="doi">10.3389/fvets.2020.00076</idno><date when="2020">2020</date><idno type="wicri:Area/Pmc/Corpus">000583</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000583</idno><idno type="wicri:Area/Pmc/Curation">000583</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000583</idno></publicationStmt><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></title><author><name sortKey="Zhang, Houshuang" sort="Zhang, Houshuang" uniqKey="Zhang H" first="Houshuang" last="Zhang">Houshuang Zhang</name></author><author><name sortKey="Wang, Zhonghua" sort="Wang, Zhonghua" uniqKey="Wang Z" first="Zhonghua" last="Wang">Zhonghua Wang</name></author><author><name sortKey="Huang, Jingwei" sort="Huang, Jingwei" uniqKey="Huang J" first="Jingwei" last="Huang">Jingwei Huang</name></author><author><name sortKey="Cao, Jie" sort="Cao, Jie" uniqKey="Cao J" first="Jie" last="Cao">Jie Cao</name></author><author><name sortKey="Zhou, Yongzhi" sort="Zhou, Yongzhi" uniqKey="Zhou Y" first="Yongzhi" last="Zhou">Yongzhi Zhou</name></author><author><name sortKey="Zhou, Jinlin" sort="Zhou, Jinlin" uniqKey="Zhou J" first="Jinlin" last="Zhou">Jinlin Zhou</name></author></analytic><series><title level="j">Frontiers in Veterinary Science</title><idno type="eISSN">2297-1769</idno><imprint><date when="2020">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><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></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Herwaldt, Bl" uniqKey="Herwaldt B">BL Herwaldt</name></author><author><name sortKey="Caccio, S" uniqKey="Caccio S">S Caccio</name></author><author><name sortKey="Gherlinzoni, F" uniqKey="Gherlinzoni F">F Gherlinzoni</name></author><author><name sortKey="Aspock, H" uniqKey="Aspock H">H Aspöck</name></author><author><name sortKey="Slemenda, Sb" uniqKey="Slemenda S">SB Slemenda</name></author><author><name sortKey="Piccaluga, P" uniqKey="Piccaluga P">P Piccaluga</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Obiegala, A" uniqKey="Obiegala A">A Obiegala</name></author><author><name sortKey="Pfeffer, M" uniqKey="Pfeffer M">M Pfeffer</name></author><author><name 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Front Vet Sci</journal-id><journal-id journal-id-type="iso-abbrev">Front Vet Sci</journal-id><journal-id journal-id-type="publisher-id">Front. Vet. Sci.</journal-id><journal-title-group><journal-title>Frontiers in Veterinary Science</journal-title></journal-title-group><issn pub-type="epub">2297-1769</issn><publisher><publisher-name>Frontiers Media S.A.</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">32133382</article-id><article-id pub-id-type="pmc">7040034</article-id><article-id pub-id-type="doi">10.3389/fvets.2020.00076</article-id><article-categories><subj-group subj-group-type="heading"><subject>Veterinary Science</subject><subj-group><subject>Original Research</subject></subj-group></subj-group></article-categories><title-group><article-title>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></article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Zhang</surname><given-names>Houshuang</given-names></name><xref ref-type="author-notes" rid="fn002"><sup>†</sup></xref><uri xlink:type="simple" xlink:href="http://loop.frontiersin.org/people/482372/overview"></uri></contrib><contrib contrib-type="author"><name><surname>Wang</surname><given-names>Zhonghua</given-names></name><xref ref-type="author-notes" rid="fn002"><sup>†</sup></xref><uri xlink:type="simple" xlink:href="http://loop.frontiersin.org/people/482773/overview"></uri></contrib><contrib contrib-type="author"><name><surname>Huang</surname><given-names>Jingwei</given-names></name><uri xlink:type="simple" xlink:href="http://loop.frontiersin.org/people/386280/overview"></uri></contrib><contrib contrib-type="author"><name><surname>Cao</surname><given-names>Jie</given-names></name><uri xlink:type="simple" xlink:href="http://loop.frontiersin.org/people/482777/overview"></uri></contrib><contrib contrib-type="author"><name><surname>Zhou</surname><given-names>Yongzhi</given-names></name></contrib><contrib contrib-type="author"><name><surname>Zhou</surname><given-names>Jinlin</given-names></name><xref ref-type="corresp" rid="c001"><sup>*</sup></xref><uri xlink:type="simple" xlink:href="http://loop.frontiersin.org/people/422736/overview"></uri></contrib></contrib-group><aff><institution>Key Laboratory of Animal Parasitology of Ministry of Agriculture, Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences</institution>,<addr-line>Shanghai</addr-line>,<country>China</country></aff><author-notes><fn fn-type="edited-by"><p>Edited by: Lise Roy, Paul Valéry University, Montpellier III, France</p></fn><fn fn-type="edited-by"><p>Reviewed by: Xiangye Liu, Xuzhou Medical University, China; Xiaokai Song, Nanjing Agricultural University, China</p></fn><corresp id="c001">*Correspondence: Jinlin Zhou <email>jinlinzhou@shvri.ac.cn</email></corresp><fn fn-type="other" id="fn001"><p>This article was submitted to Parasitology, a section of the journal Frontiers in Veterinary Science</p></fn><fn fn-type="other" id="fn002"><p>†These authors have contributed equally to this work</p></fn></author-notes><pub-date pub-type="epub"><day>18</day><month>2</month><year>2020</year></pub-date><pub-date pub-type="collection"><year>2020</year></pub-date><volume>7</volume><elocation-id>76</elocation-id><history><date date-type="received"><day>19</day><month>11</month><year>2019</year></date><date date-type="accepted"><day>29</day><month>1</month><year>2020</year></date></history><permissions><copyright-statement>Copyright © 2020 Zhang, Wang, Huang, Cao, Zhou and Zhou.</copyright-statement><copyright-year>2020</copyright-year><copyright-holder>Zhang, Wang, Huang, Cao, Zhou and Zhou</copyright-holder><license xlink:href="http://creativecommons.org/licenses/by/4.0/"><license-p>This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.</license-p></license></permissions><abstract><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></abstract><kwd-group><kwd><italic>Babesia microti</italic></kwd><kwd>thioredoxin</kwd><kwd>peroxidase-Q</kwd><kwd>antioxidant activity</kwd><kwd>drug target</kwd></kwd-group><counts><fig-count count="6"></fig-count><table-count count="0"></table-count><equation-count count="0"></equation-count><ref-count count="61"></ref-count><page-count count="11"></page-count><word-count count="8057"></word-count></counts></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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