Thioredoxin reductase is essential for thiol/disulfide redox control and oxidative stress survival of the anaerobe Bacteroides fragilis.
Identifieur interne : 000C41 ( Main/Exploration ); précédent : 000C40; suivant : 000C42Thioredoxin reductase is essential for thiol/disulfide redox control and oxidative stress survival of the anaerobe Bacteroides fragilis.
Auteurs : Edson R. Rocha [États-Unis] ; Arthur O. Tzianabos ; C Jeffrey SmithSource :
- Journal of bacteriology [ 1098-5530 ] ; 2007.
Descripteurs français
- KwdFr :
- Abcès abdominal (microbiologie), Anaérobiose (MeSH), Animaux (MeSH), Bacteroides fragilis (effets des médicaments et des substances chimiques), Bacteroides fragilis (enzymologie), Bacteroides fragilis (génétique), Disulfures (métabolisme), Données de séquences moléculaires (MeSH), Délétion de gène (MeSH), Facteurs temps (MeSH), Glutathion (métabolisme), Infections à Bacteroides (microbiologie), Oxydoréduction (effets des médicaments et des substances chimiques), Peroxydes (pharmacologie), Régulation de l'expression des gènes bactériens (effets des médicaments et des substances chimiques), Souris (MeSH), Stress oxydatif (effets des médicaments et des substances chimiques), Survie cellulaire (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH), Thiols (métabolisme), Thioredoxin-disulfide reductase (génétique), Thioredoxin-disulfide reductase (métabolisme), Tétraméthyl-diazènedicarboxamide (pharmacologie).
- MESH :
- effets des médicaments et des substances chimiques : Bacteroides fragilis, Oxydoréduction, Régulation de l'expression des gènes bactériens, Stress oxydatif.
- enzymologie : Bacteroides fragilis.
- génétique : Bacteroides fragilis, Thioredoxin-disulfide reductase.
- microbiologie : Abcès abdominal, Infections à Bacteroides.
- métabolisme : Disulfures, Glutathion, Thiols, Thioredoxin-disulfide reductase.
- pharmacologie : Peroxydes, Tétraméthyl-diazènedicarboxamide.
- Anaérobiose, Animaux, Données de séquences moléculaires, Délétion de gène, Facteurs temps, Souris, Survie cellulaire, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Abdominal Abscess (microbiology), Amino Acid Sequence (MeSH), Anaerobiosis (MeSH), Animals (MeSH), Bacteroides Infections (microbiology), Bacteroides fragilis (drug effects), Bacteroides fragilis (enzymology), Bacteroides fragilis (genetics), Base Sequence (MeSH), Cell Survival (MeSH), Diamide (pharmacology), Disulfides (metabolism), Gene Deletion (MeSH), Gene Expression Regulation, Bacterial (drug effects), Glutathione (metabolism), Mice (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (drug effects), Oxidative Stress (drug effects), Peroxides (pharmacology), Sulfhydryl Compounds (metabolism), Thioredoxin-Disulfide Reductase (genetics), Thioredoxin-Disulfide Reductase (metabolism), Time Factors (MeSH).
- MESH :
- chemical , genetics : Thioredoxin-Disulfide Reductase.
- chemical , metabolism : Disulfides, Glutathione, Sulfhydryl Compounds, Thioredoxin-Disulfide Reductase.
- chemical , pharmacology : Diamide, Peroxides.
- drug effects : Bacteroides fragilis, Gene Expression Regulation, Bacterial, Oxidation-Reduction, Oxidative Stress.
- enzymology : Bacteroides fragilis.
- genetics : Bacteroides fragilis.
- microbiology : Abdominal Abscess, Bacteroides Infections.
- Amino Acid Sequence, Anaerobiosis, Animals, Base Sequence, Cell Survival, Gene Deletion, Mice, Molecular Sequence Data, Time Factors.
Abstract
Results of this study showed that the anaerobic, opportunistic pathogen Bacteroides fragilis lacks the glutathione/glutaredoxin redox system and possesses an extensive number of putative thioredoxin (Trx) orthologs. Analysis of the genome sequence revealed six Trx orthologs and an absence of genes required for synthesis of glutathione and glutaredoxins. In addition, it was shown that the thioredoxin reductase (TrxB)/Trx system is the major or sole redox system for thiol/disulfide cellular homeostasis in this anaerobic bacterium. Expression of the B. fragilis trxB gene was induced following treatment with diamide or H(2)O(2) or exposure to oxygen. This inducible trxB expression was OxyR independent. Northern blot hybridization analysis showed that the trxB mRNA was cotranscribed with lolA as a bicistronic transcript or was present as a monocistronic transcript that was also highly induced under the same conditions. The role of LolA, a prokaryotic periplasmic lipoprotein-specific molecular chaperone in the thiol/disulfide redox system, is unknown. A trxB deletion mutant was more sensitive to the effects of diamide and oxygen than the parent strain. In addition, the trxB mutant was unable to grow in culture media without addition of a reductant. Furthermore, the trxB mutant was not able to induce intraabdominal abscess formation in a mouse model, whereas the parent strain was. Taken together, these data strongly suggest that TrxB/Trx is the major, if not the sole, thiol/disulfide redox system in this anaerobe required for survival and abscess formation in a peritoneal cavity infection model.
DOI: 10.1128/JB.00714-07
PubMed: 17873045
PubMed Central: PMC2168685
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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fragilis</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Bacteroides fragilis</term><term>Thioredoxin-disulfide reductase</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Abcès abdominal</term><term>Infections à Bacteroides</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Abdominal Abscess</term><term>Bacteroides Infections</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Disulfures</term><term>Glutathion</term><term>Thiols</term><term>Thioredoxin-disulfide reductase</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Peroxydes</term><term>Tétraméthyl-diazènedicarboxamide</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Anaerobiosis</term><term>Animals</term><term>Base Sequence</term><term>Cell Survival</term><term>Gene Deletion</term><term>Mice</term><term>Molecular Sequence Data</term><term>Time Factors</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Anaérobiose</term><term>Animaux</term><term>Données de séquences moléculaires</term><term>Délétion de gène</term><term>Facteurs temps</term><term>Souris</term><term>Survie cellulaire</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Results of this study showed that the anaerobic, opportunistic pathogen Bacteroides fragilis lacks the glutathione/glutaredoxin redox system and possesses an extensive number of putative thioredoxin (Trx) orthologs. Analysis of the genome sequence revealed six Trx orthologs and an absence of genes required for synthesis of glutathione and glutaredoxins. In addition, it was shown that the thioredoxin reductase (TrxB)/Trx system is the major or sole redox system for thiol/disulfide cellular homeostasis in this anaerobic bacterium. Expression of the B. fragilis trxB gene was induced following treatment with diamide or H(2)O(2) or exposure to oxygen. This inducible trxB expression was OxyR independent. Northern blot hybridization analysis showed that the trxB mRNA was cotranscribed with lolA as a bicistronic transcript or was present as a monocistronic transcript that was also highly induced under the same conditions. The role of LolA, a prokaryotic periplasmic lipoprotein-specific molecular chaperone in the thiol/disulfide redox system, is unknown. A trxB deletion mutant was more sensitive to the effects of diamide and oxygen than the parent strain. In addition, the trxB mutant was unable to grow in culture media without addition of a reductant. Furthermore, the trxB mutant was not able to induce intraabdominal abscess formation in a mouse model, whereas the parent strain was. Taken together, these data strongly suggest that TrxB/Trx is the major, if not the sole, thiol/disulfide redox system in this anaerobe required for survival and abscess formation in a peritoneal cavity infection model.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17873045</PMID><DateCompleted><Year>2008</Year><Month>01</Month><Day>14</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5530</ISSN><JournalIssue CitedMedium="Internet"><Volume>189</Volume><Issue>22</Issue><PubDate><Year>2007</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Journal of bacteriology</Title><ISOAbbreviation>J Bacteriol</ISOAbbreviation></Journal><ArticleTitle>Thioredoxin reductase is essential for thiol/disulfide redox control and oxidative stress survival of the anaerobe Bacteroides fragilis.</ArticleTitle><Pagination><MedlinePgn>8015-23</MedlinePgn></Pagination><Abstract><AbstractText>Results of this study showed that the anaerobic, opportunistic pathogen Bacteroides fragilis lacks the glutathione/glutaredoxin redox system and possesses an extensive number of putative thioredoxin (Trx) orthologs. Analysis of the genome sequence revealed six Trx orthologs and an absence of genes required for synthesis of glutathione and glutaredoxins. In addition, it was shown that the thioredoxin reductase (TrxB)/Trx system is the major or sole redox system for thiol/disulfide cellular homeostasis in this anaerobic bacterium. Expression of the B. fragilis trxB gene was induced following treatment with diamide or H(2)O(2) or exposure to oxygen. This inducible trxB expression was OxyR independent. Northern blot hybridization analysis showed that the trxB mRNA was cotranscribed with lolA as a bicistronic transcript or was present as a monocistronic transcript that was also highly induced under the same conditions. The role of LolA, a prokaryotic periplasmic lipoprotein-specific molecular chaperone in the thiol/disulfide redox system, is unknown. A trxB deletion mutant was more sensitive to the effects of diamide and oxygen than the parent strain. In addition, the trxB mutant was unable to grow in culture media without addition of a reductant. Furthermore, the trxB mutant was not able to induce intraabdominal abscess formation in a mouse model, whereas the parent strain was. Taken together, these data strongly suggest that TrxB/Trx is the major, if not the sole, thiol/disulfide redox system in this anaerobe required for survival and abscess formation in a peritoneal cavity infection model.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rocha</LastName><ForeName>Edson R</ForeName><Initials>ER</Initials><AffiliationInfo><Affiliation>Department of Microbiology & Immunology, East Carolina University Brody School of Medicine, 600 Moye Blvd., Greenville, NC 27834, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tzianabos</LastName><ForeName>Arthur O</ForeName><Initials>AO</Initials></Author><Author ValidYN="Y"><LastName>Smith</LastName><ForeName>C Jeffrey</ForeName><Initials>CJ</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R56 AI040588</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R21 AI068659</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI040588</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI068659</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI40588</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>09</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Bacteriol</MedlineTA><NlmUniqueID>2985120R</NlmUniqueID><ISSNLinking>0021-9193</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010545">Peroxides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>10465-78-8</RegistryNumber><NameOfSubstance UI="D003958">Diamide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber><NameOfSubstance UI="D013880">Thioredoxin-Disulfide Reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D018784" MajorTopicYN="N">Abdominal Abscess</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000693" MajorTopicYN="N">Anaerobiosis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001442" MajorTopicYN="N">Bacteroides Infections</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001441" MajorTopicYN="N">Bacteroides fragilis</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002470" MajorTopicYN="N">Cell Survival</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003958" MajorTopicYN="N">Diamide</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017353" MajorTopicYN="N">Gene Deletion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015964" MajorTopicYN="N">Gene Expression Regulation, Bacterial</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="Y">Oxidative Stress</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010545" MajorTopicYN="N">Peroxides</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013880" MajorTopicYN="N">Thioredoxin-Disulfide Reductase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013997" MajorTopicYN="N">Time Factors</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>9</Month><Day>18</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>1</Month><Day>15</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>9</Month><Day>18</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17873045</ArticleId><ArticleId IdType="pii">JB.00714-07</ArticleId><ArticleId IdType="doi">10.1128/JB.00714-07</ArticleId><ArticleId 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Nord</li></region></list><tree><noCountry><name sortKey="Smith, C Jeffrey" sort="Smith, C Jeffrey" uniqKey="Smith C" first="C Jeffrey" last="Smith">C Jeffrey Smith</name><name sortKey="Tzianabos, Arthur O" sort="Tzianabos, Arthur O" uniqKey="Tzianabos A" first="Arthur O" last="Tzianabos">Arthur O. 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