Thioredoxin glutathione reductase as a novel drug target: evidence from Schistosoma japonicum.
Identifieur interne : 000795 ( Main/Exploration ); précédent : 000794; suivant : 000796Thioredoxin glutathione reductase as a novel drug target: evidence from Schistosoma japonicum.
Auteurs : Lijun Song [République populaire de Chine] ; Jiahuang Li ; Shuying Xie ; Chunyan Qian ; Jie Wang ; Wei Zhang ; Xuren Yin ; Zichun Hua ; Chuanxin YuSource :
- PloS one [ 1932-6203 ] ; 2012.
Descripteurs français
- KwdFr :
- ADN complémentaire (métabolisme), ARN messager (métabolisme), Animaux (MeSH), Antienzymes (pharmacologie), Auranofine (composition chimique), Cinétique (MeSH), Clonage moléculaire (MeSH), Complexes multienzymatiques (antagonistes et inhibiteurs), Complexes multienzymatiques (métabolisme), Helminthes (MeSH), Homéostasie (MeSH), NADH, NADPH oxidoreductases (antagonistes et inhibiteurs), NADH, NADPH oxidoreductases (métabolisme), Oxydoréduction (MeSH), Protéines recombinantes (métabolisme), Schistosoma japonicum (métabolisme), Schistosoma mansoni (métabolisme), Schistosomiase (thérapie), Sélénium (composition chimique), Étiquettes de séquences exprimées (MeSH).
- MESH :
- antagonistes et inhibiteurs : Complexes multienzymatiques, NADH, NADPH oxidoreductases.
- composition chimique : Auranofine, Sélénium.
- métabolisme : ADN complémentaire, ARN messager, Complexes multienzymatiques, NADH, NADPH oxidoreductases, Protéines recombinantes, Schistosoma japonicum, Schistosoma mansoni.
- pharmacologie : Antienzymes.
- thérapie : Schistosomiase.
- Animaux, Cinétique, Clonage moléculaire, Helminthes, Homéostasie, Oxydoréduction, Étiquettes de séquences exprimées.
English descriptors
- KwdEn :
- Animals (MeSH), Auranofin (chemistry), Cloning, Molecular (MeSH), DNA, Complementary (metabolism), Enzyme Inhibitors (pharmacology), Expressed Sequence Tags (MeSH), Helminths (MeSH), Homeostasis (MeSH), Kinetics (MeSH), Multienzyme Complexes (antagonists & inhibitors), Multienzyme Complexes (metabolism), NADH, NADPH Oxidoreductases (antagonists & inhibitors), NADH, NADPH Oxidoreductases (metabolism), Oxidation-Reduction (MeSH), RNA, Messenger (metabolism), Recombinant Proteins (metabolism), Schistosoma japonicum (metabolism), Schistosoma mansoni (metabolism), Schistosomiasis (therapy), Selenium (chemistry).
- MESH :
- chemical , antagonists & inhibitors : Multienzyme Complexes, NADH, NADPH Oxidoreductases.
- chemical , chemistry : Auranofin, Selenium.
- chemical , metabolism : DNA, Complementary, Multienzyme Complexes, NADH, NADPH Oxidoreductases, RNA, Messenger, Recombinant Proteins.
- chemical , pharmacology : Enzyme Inhibitors.
- metabolism : Schistosoma japonicum, Schistosoma mansoni.
- therapy : Schistosomiasis.
- Animals, Cloning, Molecular, Expressed Sequence Tags, Helminths, Homeostasis, Kinetics, Oxidation-Reduction.
Abstract
BACKGROUND
Schistosomiasis remains a major public health concern affecting billions of people around the world. Currently, praziquantel is the only drug of choice for treatment of human schistosomiasis. The emergence of drug resistance to praziquantel in schistosomes makes the development of novel drugs an urgent task. Thioredoxin glutathione reductase (TGR) enzymes in Schistosoma mansoni and some other platyhelminths have been identified as alternative targets. The present study was designed to confirm the existense and the potential value of TGR as a target for development of novel antischistosomal agents in Schistosoma japonicum, a platyhelminth endemic in Asia.
METHODS AND FINDINGS
After cloning the S. japonicum TGR (SjTGR) gene, the recombinant SjTGR selenoprotein was purified and characterized in enzymatic assays as a multifunctional enzyme with thioredoxin reductase (TrxR), glutathione reductase (GR) and glutaredoxin (Grx) activities. Immunological and bioinformatic analyses confirmed that instead of having separate TrxR and GR proteins in mammalian, S. japonicum only encodes TGR, which performs the functions of both enzymes and plays a critical role in maintaining the redox balance in this parasite. These results were in good agreement with previous findings in Schistosoma mansoni and some other platyhelminths. Auranofin, a known inhibitor against TGR, caused fatal toxicity in S. japonicum adult worms in vitro and reduced worm and egg burdens in S. japonicum infected mice.
CONCLUSIONS
Collectively, our study confirms that a multifunctional enzyme SjTGR selenoprotein, instead of separate TrxR and GR enzymes, exists in S. japonicum. Furthermore, TGR may be a potential target for development of novel agents against schistosomes. This assumption is strengthened by our demonstration that the SjTGR is an essential enzyme for maintaining the thiol-disulfide redox homeostasis of S. japonicum.
DOI: 10.1371/journal.pone.0031456
PubMed: 22384025
PubMed Central: PMC3285170
Affiliations:
Links toward previous steps (curation, corpus...)
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sort="Xie, Shuying" uniqKey="Xie S" first="Shuying" last="Xie">Shuying Xie</name></author><author><name sortKey="Qian, Chunyan" sort="Qian, Chunyan" uniqKey="Qian C" first="Chunyan" last="Qian">Chunyan Qian</name></author><author><name sortKey="Wang, Jie" sort="Wang, Jie" uniqKey="Wang J" first="Jie" last="Wang">Jie Wang</name></author><author><name sortKey="Zhang, Wei" sort="Zhang, Wei" uniqKey="Zhang W" first="Wei" last="Zhang">Wei Zhang</name></author><author><name sortKey="Yin, Xuren" sort="Yin, Xuren" uniqKey="Yin X" first="Xuren" last="Yin">Xuren Yin</name></author><author><name sortKey="Hua, Zichun" sort="Hua, Zichun" uniqKey="Hua Z" first="Zichun" last="Hua">Zichun Hua</name></author><author><name sortKey="Yu, Chuanxin" sort="Yu, Chuanxin" uniqKey="Yu C" first="Chuanxin" last="Yu">Chuanxin Yu</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:22384025</idno><idno 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first="Xuren" last="Yin">Xuren Yin</name></author><author><name sortKey="Hua, Zichun" sort="Hua, Zichun" uniqKey="Hua Z" first="Zichun" last="Hua">Zichun Hua</name></author><author><name sortKey="Yu, Chuanxin" sort="Yu, Chuanxin" uniqKey="Yu C" first="Chuanxin" last="Yu">Chuanxin Yu</name></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Auranofin (chemistry)</term><term>Cloning, Molecular (MeSH)</term><term>DNA, Complementary (metabolism)</term><term>Enzyme Inhibitors (pharmacology)</term><term>Expressed Sequence Tags (MeSH)</term><term>Helminths (MeSH)</term><term>Homeostasis (MeSH)</term><term>Kinetics (MeSH)</term><term>Multienzyme Complexes (antagonists & inhibitors)</term><term>Multienzyme Complexes (metabolism)</term><term>NADH, NADPH Oxidoreductases (antagonists & inhibitors)</term><term>NADH, NADPH Oxidoreductases (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>RNA, Messenger (metabolism)</term><term>Recombinant Proteins (metabolism)</term><term>Schistosoma japonicum (metabolism)</term><term>Schistosoma mansoni (metabolism)</term><term>Schistosomiasis (therapy)</term><term>Selenium (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN complémentaire (métabolisme)</term><term>ARN messager (métabolisme)</term><term>Animaux (MeSH)</term><term>Antienzymes (pharmacologie)</term><term>Auranofine (composition chimique)</term><term>Cinétique (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Complexes multienzymatiques (antagonistes et inhibiteurs)</term><term>Complexes multienzymatiques (métabolisme)</term><term>Helminthes (MeSH)</term><term>Homéostasie (MeSH)</term><term>NADH, NADPH oxidoreductases (antagonistes et inhibiteurs)</term><term>NADH, NADPH oxidoreductases (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Protéines recombinantes (métabolisme)</term><term>Schistosoma japonicum (métabolisme)</term><term>Schistosoma mansoni (métabolisme)</term><term>Schistosomiase (thérapie)</term><term>Sélénium (composition chimique)</term><term>Étiquettes de séquences exprimées (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Multienzyme Complexes</term><term>NADH, NADPH Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Auranofin</term><term>Selenium</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA, Complementary</term><term>Multienzyme Complexes</term><term>NADH, NADPH Oxidoreductases</term><term>RNA, Messenger</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Enzyme 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qualifier="thérapie" xml:lang="fr"><term>Schistosomiase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cloning, Molecular</term><term>Expressed Sequence Tags</term><term>Helminths</term><term>Homeostasis</term><term>Kinetics</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cinétique</term><term>Clonage moléculaire</term><term>Helminthes</term><term>Homéostasie</term><term>Oxydoréduction</term><term>Étiquettes de séquences exprimées</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b></p><p>Schistosomiasis remains a major public health concern affecting billions of people around the world. Currently, praziquantel is the only drug of choice for treatment of human schistosomiasis. The emergence of drug resistance to praziquantel in schistosomes makes the development of novel drugs an urgent task. Thioredoxin glutathione reductase (TGR) enzymes in Schistosoma mansoni and some other platyhelminths have been identified as alternative targets. The present study was designed to confirm the existense and the potential value of TGR as a target for development of novel antischistosomal agents in Schistosoma japonicum, a platyhelminth endemic in Asia.</p></div><div type="abstract" xml:lang="en"><p><b>METHODS AND FINDINGS</b></p><p>After cloning the S. japonicum TGR (SjTGR) gene, the recombinant SjTGR selenoprotein was purified and characterized in enzymatic assays as a multifunctional enzyme with thioredoxin reductase (TrxR), glutathione reductase (GR) and glutaredoxin (Grx) activities. Immunological and bioinformatic analyses confirmed that instead of having separate TrxR and GR proteins in mammalian, S. japonicum only encodes TGR, which performs the functions of both enzymes and plays a critical role in maintaining the redox balance in this parasite. These results were in good agreement with previous findings in Schistosoma mansoni and some other platyhelminths. Auranofin, a known inhibitor against TGR, caused fatal toxicity in S. japonicum adult worms in vitro and reduced worm and egg burdens in S. japonicum infected mice.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSIONS</b></p><p>Collectively, our study confirms that a multifunctional enzyme SjTGR selenoprotein, instead of separate TrxR and GR enzymes, exists in S. japonicum. Furthermore, TGR may be a potential target for development of novel agents against schistosomes. This assumption is strengthened by our demonstration that the SjTGR is an essential enzyme for maintaining the thiol-disulfide redox homeostasis of S. japonicum.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22384025</PMID><DateCompleted><Year>2012</Year><Month>08</Month><Day>27</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>7</Volume><Issue>2</Issue><PubDate><Year>2012</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>Thioredoxin glutathione reductase as a novel drug target: evidence from Schistosoma japonicum.</ArticleTitle><Pagination><MedlinePgn>e31456</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0031456</ELocationID><Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Schistosomiasis remains a major public health concern affecting billions of people around the world. Currently, praziquantel is the only drug of choice for treatment of human schistosomiasis. The emergence of drug resistance to praziquantel in schistosomes makes the development of novel drugs an urgent task. Thioredoxin glutathione reductase (TGR) enzymes in Schistosoma mansoni and some other platyhelminths have been identified as alternative targets. The present study was designed to confirm the existense and the potential value of TGR as a target for development of novel antischistosomal agents in Schistosoma japonicum, a platyhelminth endemic in Asia.</AbstractText><AbstractText Label="METHODS AND FINDINGS" NlmCategory="RESULTS">After cloning the S. japonicum TGR (SjTGR) gene, the recombinant SjTGR selenoprotein was purified and characterized in enzymatic assays as a multifunctional enzyme with thioredoxin reductase (TrxR), glutathione reductase (GR) and glutaredoxin (Grx) activities. Immunological and bioinformatic analyses confirmed that instead of having separate TrxR and GR proteins in mammalian, S. japonicum only encodes TGR, which performs the functions of both enzymes and plays a critical role in maintaining the redox balance in this parasite. These results were in good agreement with previous findings in Schistosoma mansoni and some other platyhelminths. Auranofin, a known inhibitor against TGR, caused fatal toxicity in S. japonicum adult worms in vitro and reduced worm and egg burdens in S. japonicum infected mice.</AbstractText><AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">Collectively, our study confirms that a multifunctional enzyme SjTGR selenoprotein, instead of separate TrxR and GR enzymes, exists in S. japonicum. Furthermore, TGR may be a potential target for development of novel agents against schistosomes. This assumption is strengthened by our demonstration that the SjTGR is an essential enzyme for maintaining the thiol-disulfide redox homeostasis of S. japonicum.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Song</LastName><ForeName>LiJun</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Key Laboratory on Technology for Parasitic Disease Prevention and Control, Ministry of Health, Jiangsu Institute of Parasitic Diseases, Wuxi, Jiangsu, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>JiaHuang</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Xie</LastName><ForeName>ShuYing</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Qian</LastName><ForeName>ChunYan</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Jie</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Wei</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Yin</LastName><ForeName>Xuren</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Hua</LastName><ForeName>ZiChun</ForeName><Initials>Z</Initials></Author><Author ValidYN="Y"><LastName>Yu</LastName><ForeName>ChuanXin</ForeName><Initials>C</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>02</Month><Day>22</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009097">Multienzyme Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012333">RNA, Messenger</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>3H04W2810V</RegistryNumber><NameOfSubstance UI="D001310">Auranofin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.6.-</RegistryNumber><NameOfSubstance UI="D009247">NADH, NADPH Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.6.4.-</RegistryNumber><NameOfSubstance UI="C466433">thioredoxin glutathione reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>H6241UJ22B</RegistryNumber><NameOfSubstance UI="D012643">Selenium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001310" MajorTopicYN="N">Auranofin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020224" MajorTopicYN="N">Expressed Sequence Tags</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006376" MajorTopicYN="N">Helminths</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006706" MajorTopicYN="N">Homeostasis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009097" MajorTopicYN="N">Multienzyme Complexes</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009247" MajorTopicYN="N">NADH, NADPH Oxidoreductases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012333" MajorTopicYN="N">RNA, Messenger</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012549" MajorTopicYN="N">Schistosoma japonicum</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012550" MajorTopicYN="N">Schistosoma mansoni</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012552" MajorTopicYN="N">Schistosomiasis</DescriptorName><QualifierName UI="Q000628" MajorTopicYN="Y">therapy</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012643" MajorTopicYN="N">Selenium</DescriptorName><QualifierName UI="Q000737" 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sortKey="Xie, Shuying" sort="Xie, Shuying" uniqKey="Xie S" first="Shuying" last="Xie">Shuying Xie</name><name sortKey="Yin, Xuren" sort="Yin, Xuren" uniqKey="Yin X" first="Xuren" last="Yin">Xuren Yin</name><name sortKey="Yu, Chuanxin" sort="Yu, Chuanxin" uniqKey="Yu C" first="Chuanxin" last="Yu">Chuanxin Yu</name><name sortKey="Zhang, Wei" sort="Zhang, Wei" uniqKey="Zhang W" first="Wei" last="Zhang">Wei Zhang</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Song, Lijun" sort="Song, Lijun" uniqKey="Song L" first="Lijun" last="Song">Lijun Song</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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