Targeting the Thioredoxin Reductase-Thioredoxin System from Staphylococcus aureus by Silver Ions.
Identifieur interne : 000306 ( Main/Exploration ); précédent : 000305; suivant : 000307Targeting the Thioredoxin Reductase-Thioredoxin System from Staphylococcus aureus by Silver Ions.
Auteurs : Xiangwen Liao ; Fang Yang ; Hongyan Li [République populaire de Chine] ; Pui-Kin So [République populaire de Chine] ; Zhongping Yao [République populaire de Chine] ; Wei Xia ; Hongzhe Sun [République populaire de Chine]Source :
- Inorganic chemistry [ 1520-510X ] ; 2017.
Descripteurs français
- KwdFr :
- Antibactériens (pharmacologie), Argent (pharmacologie), Domaine catalytique (effets des médicaments et des substances chimiques), Humains (MeSH), Infections à staphylocoques (microbiologie), Infections à staphylocoques (traitement médicamenteux), Modèles moléculaires (MeSH), Multimérisation de protéines (effets des médicaments et des substances chimiques), Protéines bactériennes (antagonistes et inhibiteurs), Protéines bactériennes (métabolisme), Staphylococcus aureus (effets des médicaments et des substances chimiques), Staphylococcus aureus (métabolisme), Thioredoxin-disulfide reductase (antagonistes et inhibiteurs), Thioredoxin-disulfide reductase (métabolisme), Thiorédoxines (antagonistes et inhibiteurs), Thiorédoxines (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Protéines bactériennes, Thioredoxin-disulfide reductase, Thiorédoxines.
- effets des médicaments et des substances chimiques : Domaine catalytique, Multimérisation de protéines, Staphylococcus aureus.
- microbiologie : Infections à staphylocoques.
- métabolisme : Protéines bactériennes, Staphylococcus aureus, Thioredoxin-disulfide reductase, Thiorédoxines.
- pharmacologie : Antibactériens, Argent.
- traitement médicamenteux : Infections à staphylocoques.
- Humains, Modèles moléculaires.
English descriptors
- KwdEn :
- Anti-Bacterial Agents (pharmacology), Bacterial Proteins (antagonists & inhibitors), Bacterial Proteins (metabolism), Catalytic Domain (drug effects), Humans (MeSH), Models, Molecular (MeSH), Protein Multimerization (drug effects), Silver (pharmacology), Staphylococcal Infections (drug therapy), Staphylococcal Infections (microbiology), Staphylococcus aureus (drug effects), Staphylococcus aureus (metabolism), Thioredoxin-Disulfide Reductase (antagonists & inhibitors), Thioredoxin-Disulfide Reductase (metabolism), Thioredoxins (antagonists & inhibitors), Thioredoxins (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Bacterial Proteins, Thioredoxin-Disulfide Reductase, Thioredoxins.
- chemical , metabolism : Bacterial Proteins, Thioredoxin-Disulfide Reductase, Thioredoxins.
- chemical , pharmacology : Anti-Bacterial Agents, Silver.
- drug effects : Catalytic Domain, Protein Multimerization, Staphylococcus aureus.
- drug therapy : Staphylococcal Infections.
- metabolism : Staphylococcus aureus.
- microbiology : Staphylococcal Infections.
- Humans, Models, Molecular.
Abstract
The thioredoxin system, which is composed of NADPH, thioredoxin reductase (TrxR), and thioredoxin (Trx), is one of the major disulfide reductase systems used by bacteria against oxidative stress. In particular, this reductase system is crucial for the survival of the pathogenic bacterium Staphylococcus aureus, which lacks a natural glutathione/glutaredoxin (Grx) system. Although silver ions and silver-containing materials have been used as antibacterial agents for centuries, the antibacterial mechanism of silver is not well-understood. Herein, we demonstrate that silver ions bind to the active sites of S. aureus TrxR and Trx with dissociation constants of 1.4 ± 0.1 μM and 15.0 ± 5.0 μM and stoichiometries of 1 and 2 Ag+ ions per protein, respectively. Importantly, silver ion binding leads to oligomerization and functional disruption of TrxR as well as Trx. Silver also depleted intracellular thiol levels in S. aureus, disrupting bacterial thiol-redox homeostasis. Our study provides new insights into the antibacterial mechanism of silver ions. Moreover, the Trx and TrxR system might serve as a feasible target for the design of antibacterial drugs.
DOI: 10.1021/acs.inorgchem.7b01904
PubMed: 29182243
Affiliations:
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sortKey="Liao, Xiangwen" sort="Liao, Xiangwen" uniqKey="Liao X" first="Xiangwen" last="Liao">Xiangwen Liao</name><affiliation><nlm:affiliation>MOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University , Guangzhou, China , 510275.</nlm:affiliation><wicri:noCountry code="subField">510275</wicri:noCountry></affiliation><affiliation><nlm:affiliation>Hunan Provincial Key Laboratory for Ethnic Dong Medicine Research, Hunan University of Medicine , Huaihua, China , 418000.</nlm:affiliation><wicri:noCountry code="subField">418000</wicri:noCountry></affiliation></author><author><name sortKey="Yang, Fang" sort="Yang, Fang" uniqKey="Yang F" first="Fang" last="Yang">Fang Yang</name><affiliation><nlm:affiliation>MOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University , Guangzhou, China , 510275.</nlm:affiliation><wicri:noCountry code="subField">510275</wicri:noCountry></affiliation></author><author><name 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Kong SAR</wicri:noRegion></affiliation></author></analytic><series><title level="j">Inorganic chemistry</title><idno type="eISSN">1520-510X</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Anti-Bacterial Agents (pharmacology)</term><term>Bacterial Proteins (antagonists & inhibitors)</term><term>Bacterial Proteins (metabolism)</term><term>Catalytic Domain (drug effects)</term><term>Humans (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Protein Multimerization (drug effects)</term><term>Silver (pharmacology)</term><term>Staphylococcal Infections (drug therapy)</term><term>Staphylococcal Infections (microbiology)</term><term>Staphylococcus aureus (drug effects)</term><term>Staphylococcus aureus (metabolism)</term><term>Thioredoxin-Disulfide Reductase (antagonists & inhibitors)</term><term>Thioredoxin-Disulfide Reductase (metabolism)</term><term>Thioredoxins (antagonists & inhibitors)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antibactériens (pharmacologie)</term><term>Argent (pharmacologie)</term><term>Domaine catalytique (effets des médicaments et des substances chimiques)</term><term>Humains (MeSH)</term><term>Infections à staphylocoques (microbiologie)</term><term>Infections à staphylocoques (traitement médicamenteux)</term><term>Modèles moléculaires (MeSH)</term><term>Multimérisation de protéines (effets des médicaments et des substances chimiques)</term><term>Protéines bactériennes (antagonistes et inhibiteurs)</term><term>Protéines bactériennes (métabolisme)</term><term>Staphylococcus aureus (effets des médicaments et des substances chimiques)</term><term>Staphylococcus aureus (métabolisme)</term><term>Thioredoxin-disulfide reductase (antagonistes et inhibiteurs)</term><term>Thioredoxin-disulfide reductase (métabolisme)</term><term>Thiorédoxines (antagonistes et inhibiteurs)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Bacterial Proteins</term><term>Thioredoxin-Disulfide Reductase</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>Thioredoxin-Disulfide Reductase</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Anti-Bacterial Agents</term><term>Silver</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Protéines bactériennes</term><term>Thioredoxin-disulfide reductase</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Catalytic Domain</term><term>Protein Multimerization</term><term>Staphylococcus aureus</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Staphylococcal Infections</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Domaine catalytique</term><term>Multimérisation de protéines</term><term>Staphylococcus aureus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Staphylococcus aureus</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Infections à staphylocoques</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Staphylococcal Infections</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines bactériennes</term><term>Staphylococcus aureus</term><term>Thioredoxin-disulfide reductase</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antibactériens</term><term>Argent</term></keywords><keywords scheme="MESH" qualifier="traitement médicamenteux" xml:lang="fr"><term>Infections à staphylocoques</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Models, Molecular</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Modèles moléculaires</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The thioredoxin system, which is composed of NADPH, thioredoxin reductase (TrxR), and thioredoxin (Trx), is one of the major disulfide reductase systems used by bacteria against oxidative stress. In particular, this reductase system is crucial for the survival of the pathogenic bacterium Staphylococcus aureus, which lacks a natural glutathione/glutaredoxin (Grx) system. Although silver ions and silver-containing materials have been used as antibacterial agents for centuries, the antibacterial mechanism of silver is not well-understood. Herein, we demonstrate that silver ions bind to the active sites of S. aureus TrxR and Trx with dissociation constants of 1.4 ± 0.1 μM and 15.0 ± 5.0 μM and stoichiometries of 1 and 2 Ag<sup>+</sup> ions per protein, respectively. Importantly, silver ion binding leads to oligomerization and functional disruption of TrxR as well as Trx. Silver also depleted intracellular thiol levels in S. aureus, disrupting bacterial thiol-redox homeostasis. Our study provides new insights into the antibacterial mechanism of silver ions. Moreover, the Trx and TrxR system might serve as a feasible target for the design of antibacterial drugs.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29182243</PMID><DateCompleted><Year>2018</Year><Month>02</Month><Day>28</Day></DateCompleted><DateRevised><Year>2018</Year><Month>02</Month><Day>28</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-510X</ISSN><JournalIssue CitedMedium="Internet"><Volume>56</Volume><Issue>24</Issue><PubDate><Year>2017</Year><Month>Dec</Month><Day>18</Day></PubDate></JournalIssue><Title>Inorganic chemistry</Title><ISOAbbreviation>Inorg Chem</ISOAbbreviation></Journal><ArticleTitle>Targeting the Thioredoxin Reductase-Thioredoxin System from Staphylococcus aureus by Silver Ions.</ArticleTitle><Pagination><MedlinePgn>14823-14830</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/acs.inorgchem.7b01904</ELocationID><Abstract><AbstractText>The thioredoxin system, which is composed of NADPH, thioredoxin reductase (TrxR), and thioredoxin (Trx), is one of the major disulfide reductase systems used by bacteria against oxidative stress. In particular, this reductase system is crucial for the survival of the pathogenic bacterium Staphylococcus aureus, which lacks a natural glutathione/glutaredoxin (Grx) system. Although silver ions and silver-containing materials have been used as antibacterial agents for centuries, the antibacterial mechanism of silver is not well-understood. Herein, we demonstrate that silver ions bind to the active sites of S. aureus TrxR and Trx with dissociation constants of 1.4 ± 0.1 μM and 15.0 ± 5.0 μM and stoichiometries of 1 and 2 Ag<sup>+</sup> ions per protein, respectively. Importantly, silver ion binding leads to oligomerization and functional disruption of TrxR as well as Trx. Silver also depleted intracellular thiol levels in S. aureus, disrupting bacterial thiol-redox homeostasis. Our study provides new insights into the antibacterial mechanism of silver ions. Moreover, the Trx and TrxR system might serve as a feasible target for the design of antibacterial drugs.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Liao</LastName><ForeName>Xiangwen</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>MOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University , Guangzhou, China , 510275.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Hunan Provincial Key Laboratory for Ethnic Dong Medicine Research, Hunan University of Medicine , Huaihua, China , 418000.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Fang</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>MOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University , Guangzhou, China , 510275.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Hongyan</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Chemistry, The University of Hong Kong , Pokfulam Road, Hong Kong SAR, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>So</LastName><ForeName>Pui-Kin</ForeName><Initials>PK</Initials><AffiliationInfo><Affiliation>State Key Laboratory for Chirosciences and Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University , Hung Hom, Kowloon, Hong Kong SAR, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yao</LastName><ForeName>Zhongping</ForeName><Initials>Z</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-3555-9632</Identifier><AffiliationInfo><Affiliation>State Key Laboratory for Chirosciences and Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University , Hung Hom, Kowloon, Hong Kong SAR, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Xia</LastName><ForeName>Wei</ForeName><Initials>W</Initials><Identifier Source="ORCID">http://orcid.org/0000-0001-6480-3265</Identifier><AffiliationInfo><Affiliation>MOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University , Guangzhou, China , 510275.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sun</LastName><ForeName>Hongzhe</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>MOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University , Guangzhou, China , 510275.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry, The University of Hong Kong , Pokfulam Road, Hong Kong SAR, China.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>11</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Inorg Chem</MedlineTA><NlmUniqueID>0366543</NlmUniqueID><ISSNLinking>0020-1669</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000900">Anti-Bacterial Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>3M4G523W1G</RegistryNumber><NameOfSubstance UI="D012834">Silver</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber><NameOfSubstance UI="D013880">Thioredoxin-Disulfide Reductase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000900" MajorTopicYN="N">Anti-Bacterial Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012834" MajorTopicYN="N">Silver</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013203" MajorTopicYN="N">Staphylococcal Infections</DescriptorName><QualifierName UI="Q000188" MajorTopicYN="N">drug therapy</QualifierName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013211" MajorTopicYN="N">Staphylococcus aureus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013880" MajorTopicYN="N">Thioredoxin-Disulfide Reductase</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>11</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>3</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>11</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29182243</ArticleId><ArticleId IdType="doi">10.1021/acs.inorgchem.7b01904</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><noCountry><name sortKey="Liao, Xiangwen" sort="Liao, Xiangwen" uniqKey="Liao X" first="Xiangwen" last="Liao">Xiangwen Liao</name><name sortKey="Xia, Wei" sort="Xia, Wei" uniqKey="Xia W" first="Wei" last="Xia">Wei Xia</name><name sortKey="Yang, Fang" sort="Yang, Fang" uniqKey="Yang F" first="Fang" last="Yang">Fang Yang</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Li, Hongyan" sort="Li, Hongyan" uniqKey="Li H" first="Hongyan" last="Li">Hongyan Li</name></noRegion><name sortKey="So, Pui Kin" sort="So, Pui Kin" uniqKey="So P" first="Pui-Kin" last="So">Pui-Kin So</name><name sortKey="Sun, Hongzhe" sort="Sun, Hongzhe" uniqKey="Sun H" first="Hongzhe" last="Sun">Hongzhe Sun</name><name sortKey="Yao, Zhongping" sort="Yao, Zhongping" uniqKey="Yao Z" first="Zhongping" last="Yao">Zhongping Yao</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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