Impact of reducing and oxidizing agents on the infectivity of Qβ phage and the overall structure of its capsid.
Identifieur interne : 000157 ( Main/Exploration ); précédent : 000156; suivant : 000158Impact of reducing and oxidizing agents on the infectivity of Qβ phage and the overall structure of its capsid.
Auteurs : Pauline Loison [France] ; Didier Majou [France] ; Eric Gelhaye [France] ; Nicolas Boudaud [France] ; Christophe Gantzer [France]Source :
- FEMS microbiology ecology [ 1574-6941 ] ; 2016.
Descripteurs français
- KwdFr :
- Bactériophages (croissance et développement), Capside (physiologie), Dithiothréitol (composition chimique), Escherichia coli (virologie), Glutathion (composition chimique), Humains (MeSH), Microbiome gastro-intestinal (MeSH), Oxydants (composition chimique), Oxydoréduction (MeSH), Protéines de capside (métabolisme), Protéines de transport (MeSH), Tube digestif (microbiologie), Tube digestif (virologie), Étapes du cycle de vie (MeSH).
- MESH :
- composition chimique : Dithiothréitol, Glutathion, Oxydants.
- croissance et développement : Bactériophages.
- microbiologie : Tube digestif.
- métabolisme : Protéines de capside.
- physiologie : Capside.
- virologie : Escherichia coli, Tube digestif.
- Humains, Microbiome gastro-intestinal, Oxydoréduction, Protéines de transport, Étapes du cycle de vie.
English descriptors
- KwdEn :
- Bacteriophages (growth & development), Capsid (physiology), Capsid Proteins (metabolism), Carrier Proteins (MeSH), Dithiothreitol (chemistry), Escherichia coli (virology), Gastrointestinal Microbiome (MeSH), Gastrointestinal Tract (microbiology), Gastrointestinal Tract (virology), Glutathione (chemistry), Humans (MeSH), Life Cycle Stages (MeSH), Oxidants (chemistry), Oxidation-Reduction (MeSH).
- MESH :
- chemical , chemistry : Dithiothreitol, Glutathione, Oxidants.
- chemical , metabolism : Capsid Proteins.
- growth & development : Bacteriophages.
- microbiology : Gastrointestinal Tract.
- physiology : Capsid.
- virology : Escherichia coli, Gastrointestinal Tract.
- chemical : Carrier Proteins, Gastrointestinal Microbiome, Humans, Life Cycle Stages, Oxidation-Reduction.
Abstract
Qβ phages infect Escherichia coli in the human gut by recognizing F-pili as receptors. Infection therefore occurs under reducing conditions induced by physiological agents (e.g. glutathione) or the intestinal bacterial flora. After excretion in the environment, phage particles are exposed to oxidizing conditions and sometimes disinfection. If inactivation does not occur, the phage may infect new hosts in the human gut through the oral route. During such a life cycle, we demonstrated that, outside the human gut, cysteines of the major protein capsid of Qβ phage form disulfide bonds. Disinfection with NaClO does not allow overoxidation to occur. Such oxidation induces inactivation rather by irreversible damage to the minor proteins. In the presence of glutathione, most disulfide bonds are reduced, which slightly increases the capacity of the phage to infect E. coli in vitro Such reduction is reversible and barely alters infectivity of the phage. Reduction of all disulfide bonds by dithiothreitol leads to complete capsid destabilization. These data provide new insights into how the phages are impacted by oxidizing-reducing conditions outside their host cell and raises the possibility of the intervention of the redox during life cycle of the phage.
DOI: 10.1093/femsec/fiw153
PubMed: 27402711
Affiliations:
- France
- Basse-Normandie, Grand Est, Lorraine (région), Région Normandie, Île-de-France
- Champenoux, Paris
- Université de Lorraine
Links toward previous steps (curation, corpus...)
Le document en format XML
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UMR 7564, CNRS/Université de Lorraine, Nancy 54000, France CNRS, LCPME, UMR 7564, Institut Jean Barriol (IJB), Nancy 54000, France Food Safety Department, ACTALIA, Saint Lô 50000, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>LCPME (Laboratory of Physical Chemistry and Microbiology for the Environment), Joint Research Unit - UMR 7564, CNRS/Université de Lorraine, Nancy 54000, France CNRS, LCPME, UMR 7564, Institut Jean Barriol (IJB), Nancy 54000, France Food Safety Department, ACTALIA, Saint Lô 50000</wicri:regionArea><placeName><region type="region" nuts="2">Région Normandie</region><region type="old region" nuts="2">Basse-Normandie</region></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Majou, Didier" sort="Majou, Didier" uniqKey="Majou D" first="Didier" last="Majou">Didier Majou</name><affiliation wicri:level="3"><nlm:affiliation>ACTIA, 16 rue Claude Bernard, 75231 Paris Cedex 05, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>ACTIA, 16 rue Claude Bernard, 75231 Paris Cedex 05</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Tree-Microbe Interactions Department, UMR1136, F-54500 Vandœuvre-lès-Nancy, France INRA, Tree-Microbe Interactions Department, UMR1136, F-54280 Champenoux, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, Tree-Microbe Interactions Department, UMR1136, F-54500 Vandœuvre-lès-Nancy, France INRA, Tree-Microbe Interactions Department, UMR1136, F-54280 Champenoux</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Champenoux</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Boudaud, Nicolas" sort="Boudaud, Nicolas" uniqKey="Boudaud N" first="Nicolas" last="Boudaud">Nicolas Boudaud</name><affiliation wicri:level="3"><nlm:affiliation>Food Safety Department, ACTALIA, Saint Lô 50000, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Food Safety Department, ACTALIA, Saint Lô 50000</wicri:regionArea><placeName><region type="region" nuts="2">Région Normandie</region><region type="old region" nuts="2">Basse-Normandie</region></placeName></affiliation></author><author><name sortKey="Gantzer, Christophe" sort="Gantzer, Christophe" uniqKey="Gantzer C" first="Christophe" last="Gantzer">Christophe Gantzer</name><affiliation wicri:level="4"><nlm:affiliation>LCPME (Laboratory of Physical Chemistry and Microbiology for the Environment), Joint Research Unit - UMR 7564, CNRS/Université de Lorraine, Nancy 54000, France CNRS, LCPME, UMR 7564, Institut Jean Barriol (IJB), Nancy 54000, France christophe.gantzer@univ-lorraine.fr.</nlm:affiliation><country wicri:rule="url">France</country><wicri:regionArea>LCPME (Laboratory of Physical Chemistry and Microbiology for the Environment), Joint Research Unit - UMR 7564, CNRS/Université de Lorraine, Nancy 54000, France CNRS, LCPME, UMR 7564, Institut Jean Barriol (IJB), Nancy 54000</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author></analytic><series><title level="j">FEMS microbiology ecology</title><idno type="eISSN">1574-6941</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacteriophages (growth & development)</term><term>Capsid (physiology)</term><term>Capsid Proteins (metabolism)</term><term>Carrier Proteins (MeSH)</term><term>Dithiothreitol (chemistry)</term><term>Escherichia coli (virology)</term><term>Gastrointestinal Microbiome (MeSH)</term><term>Gastrointestinal Tract (microbiology)</term><term>Gastrointestinal Tract (virology)</term><term>Glutathione (chemistry)</term><term>Humans (MeSH)</term><term>Life Cycle Stages (MeSH)</term><term>Oxidants (chemistry)</term><term>Oxidation-Reduction (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Bactériophages (croissance et développement)</term><term>Capside (physiologie)</term><term>Dithiothréitol (composition chimique)</term><term>Escherichia coli (virologie)</term><term>Glutathion (composition chimique)</term><term>Humains (MeSH)</term><term>Microbiome gastro-intestinal (MeSH)</term><term>Oxydants (composition chimique)</term><term>Oxydoréduction (MeSH)</term><term>Protéines de capside (métabolisme)</term><term>Protéines de transport (MeSH)</term><term>Tube digestif (microbiologie)</term><term>Tube digestif (virologie)</term><term>Étapes du cycle de vie (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Dithiothreitol</term><term>Glutathione</term><term>Oxidants</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Capsid Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Dithiothréitol</term><term>Glutathion</term><term>Oxydants</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Bactériophages</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Bacteriophages</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Tube digestif</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Gastrointestinal Tract</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines de capside</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Capside</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Capsid</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Escherichia coli</term><term>Tube digestif</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Escherichia coli</term><term>Gastrointestinal Tract</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Carrier Proteins</term><term>Gastrointestinal Microbiome</term><term>Humans</term><term>Life Cycle Stages</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Microbiome gastro-intestinal</term><term>Oxydoréduction</term><term>Protéines de transport</term><term>Étapes du cycle de vie</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Qβ phages infect Escherichia coli in the human gut by recognizing F-pili as receptors. Infection therefore occurs under reducing conditions induced by physiological agents (e.g. glutathione) or the intestinal bacterial flora. After excretion in the environment, phage particles are exposed to oxidizing conditions and sometimes disinfection. If inactivation does not occur, the phage may infect new hosts in the human gut through the oral route. During such a life cycle, we demonstrated that, outside the human gut, cysteines of the major protein capsid of Qβ phage form disulfide bonds. Disinfection with NaClO does not allow overoxidation to occur. Such oxidation induces inactivation rather by irreversible damage to the minor proteins. In the presence of glutathione, most disulfide bonds are reduced, which slightly increases the capacity of the phage to infect E. coli in vitro Such reduction is reversible and barely alters infectivity of the phage. Reduction of all disulfide bonds by dithiothreitol leads to complete capsid destabilization. These data provide new insights into how the phages are impacted by oxidizing-reducing conditions outside their host cell and raises the possibility of the intervention of the redox during life cycle of the phage.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" IndexingMethod="Curated" Owner="NLM"><PMID Version="1">27402711</PMID><DateCompleted><Year>2017</Year><Month>07</Month><Day>10</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>02</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1574-6941</ISSN><JournalIssue CitedMedium="Internet"><Volume>92</Volume><Issue>11</Issue><PubDate><Year>2016</Year><Month>11</Month></PubDate></JournalIssue><Title>FEMS microbiology ecology</Title><ISOAbbreviation>FEMS Microbiol Ecol</ISOAbbreviation></Journal><ArticleTitle>Impact of reducing and oxidizing agents on the infectivity of Qβ phage and the overall structure of its capsid.</ArticleTitle><ELocationID EIdType="doi" ValidYN="Y">10.1093/femsec/fiw153</ELocationID><ELocationID EIdType="pii" ValidYN="Y">fiw153</ELocationID><Abstract><AbstractText>Qβ phages infect Escherichia coli in the human gut by recognizing F-pili as receptors. Infection therefore occurs under reducing conditions induced by physiological agents (e.g. glutathione) or the intestinal bacterial flora. After excretion in the environment, phage particles are exposed to oxidizing conditions and sometimes disinfection. If inactivation does not occur, the phage may infect new hosts in the human gut through the oral route. During such a life cycle, we demonstrated that, outside the human gut, cysteines of the major protein capsid of Qβ phage form disulfide bonds. Disinfection with NaClO does not allow overoxidation to occur. Such oxidation induces inactivation rather by irreversible damage to the minor proteins. In the presence of glutathione, most disulfide bonds are reduced, which slightly increases the capacity of the phage to infect E. coli in vitro Such reduction is reversible and barely alters infectivity of the phage. Reduction of all disulfide bonds by dithiothreitol leads to complete capsid destabilization. These data provide new insights into how the phages are impacted by oxidizing-reducing conditions outside their host cell and raises the possibility of the intervention of the redox during life cycle of the phage.</AbstractText><CopyrightInformation>© FEMS 2016. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Loison</LastName><ForeName>Pauline</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>LCPME (Laboratory of Physical Chemistry and Microbiology for the Environment), Joint Research Unit - UMR 7564, CNRS/Université de Lorraine, Nancy 54000, France CNRS, LCPME, UMR 7564, Institut Jean Barriol (IJB), Nancy 54000, France Food Safety Department, ACTALIA, Saint Lô 50000, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Majou</LastName><ForeName>Didier</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>ACTIA, 16 rue Claude Bernard, 75231 Paris Cedex 05, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gelhaye</LastName><ForeName>Eric</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Université de Lorraine, Tree-Microbe Interactions Department, UMR1136, F-54500 Vandœuvre-lès-Nancy, France INRA, Tree-Microbe Interactions Department, UMR1136, F-54280 Champenoux, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Boudaud</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Food Safety Department, ACTALIA, Saint Lô 50000, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gantzer</LastName><ForeName>Christophe</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>LCPME (Laboratory of Physical Chemistry and Microbiology for the Environment), Joint Research Unit - UMR 7564, CNRS/Université de Lorraine, Nancy 54000, France CNRS, LCPME, UMR 7564, Institut Jean Barriol (IJB), Nancy 54000, France christophe.gantzer@univ-lorraine.fr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>07</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEMS Microbiol Ecol</MedlineTA><NlmUniqueID>8901229</NlmUniqueID><ISSNLinking>0168-6496</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D036022">Capsid Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002352">Carrier Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016877">Oxidants</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>T8ID5YZU6Y</RegistryNumber><NameOfSubstance UI="D004229">Dithiothreitol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001435" MajorTopicYN="N">Bacteriophages</DescriptorName><QualifierName UI="Q000254" MajorTopicYN="Y">growth & development</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002213" MajorTopicYN="N">Capsid</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D036022" MajorTopicYN="N">Capsid Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002352" MajorTopicYN="N">Carrier Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004229" MajorTopicYN="N">Dithiothreitol</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000821" MajorTopicYN="Y">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000069196" MajorTopicYN="Y">Gastrointestinal Microbiome</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D041981" MajorTopicYN="N">Gastrointestinal Tract</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName><QualifierName UI="Q000821" MajorTopicYN="Y">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008018" MajorTopicYN="N">Life Cycle Stages</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016877" MajorTopicYN="N">Oxidants</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Qβ phage</Keyword><Keyword MajorTopicYN="Y">capsid proteins</Keyword><Keyword MajorTopicYN="Y">disulfide bonds</Keyword><Keyword MajorTopicYN="Y">inactivation</Keyword><Keyword MajorTopicYN="Y">oxidation</Keyword><Keyword MajorTopicYN="Y">reduction</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>07</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>7</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>7</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>7</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">27402711</ArticleId><ArticleId IdType="pii">fiw153</ArticleId><ArticleId IdType="doi">10.1093/femsec/fiw153</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Basse-Normandie</li><li>Grand Est</li><li>Lorraine (région)</li><li>Région Normandie</li><li>Île-de-France</li></region><settlement><li>Champenoux</li><li>Paris</li></settlement><orgName><li>Université de Lorraine</li></orgName></list><tree><country name="France"><region name="Région Normandie"><name sortKey="Loison, Pauline" sort="Loison, Pauline" uniqKey="Loison P" first="Pauline" last="Loison">Pauline Loison</name></region><name sortKey="Boudaud, Nicolas" sort="Boudaud, Nicolas" uniqKey="Boudaud N" first="Nicolas" last="Boudaud">Nicolas Boudaud</name><name sortKey="Gantzer, Christophe" sort="Gantzer, Christophe" uniqKey="Gantzer C" first="Christophe" last="Gantzer">Christophe Gantzer</name><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name><name sortKey="Majou, Didier" sort="Majou, Didier" uniqKey="Majou D" first="Didier" last="Majou">Didier Majou</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:27402711" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a TreeMicInterV1
| This area was generated with Dilib version V0.6.37. |  |