The adaptive metabolic response involves specific protein glutathionylation during the filamentation process in the pathogen Candida albicans.
Identifieur interne : 000406 ( Main/Exploration ); précédent : 000405; suivant : 000407The adaptive metabolic response involves specific protein glutathionylation during the filamentation process in the pathogen Candida albicans.
Auteurs : R. Gergondey [France] ; C. Garcia [France] ; V. Serre [France] ; J M Camadro [France] ; F. Auchère [France]Source :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2016.
Descripteurs français
- KwdFr :
- Aconitate hydratase (analyse), Aconitate hydratase (métabolisme), Alignement de séquences (MeSH), Candida albicans (composition chimique), Candida albicans (croissance et développement), Candida albicans (enzymologie), Candida albicans (métabolisme), Candidose (microbiologie), Glutathion (métabolisme), Humains (MeSH), Hyphae (composition chimique), Hyphae (croissance et développement), Hyphae (enzymologie), Hyphae (métabolisme), Isocitrate lyase (analyse), Isocitrate lyase (métabolisme), Malate synthase (analyse), Malate synthase (métabolisme), Modèles moléculaires (MeSH), Protéines fongiques (analyse), Protéines fongiques (métabolisme), Protéines mitochondriales (analyse), Protéines mitochondriales (métabolisme), Séquence d'acides aminés (MeSH).
- MESH :
- analyse : Aconitate hydratase, Isocitrate lyase, Malate synthase, Protéines fongiques, Protéines mitochondriales.
- composition chimique : Candida albicans, Hyphae.
- croissance et développement : Candida albicans, Hyphae.
- enzymologie : Candida albicans, Hyphae.
- microbiologie : Candidose.
- métabolisme : Aconitate hydratase, Candida albicans, Glutathion, Hyphae, Isocitrate lyase, Malate synthase, Protéines fongiques, Protéines mitochondriales.
- Alignement de séquences, Humains, Modèles moléculaires, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Aconitate Hydratase (analysis), Aconitate Hydratase (metabolism), Amino Acid Sequence (MeSH), Candida albicans (chemistry), Candida albicans (enzymology), Candida albicans (growth & development), Candida albicans (metabolism), Candidiasis (microbiology), Fungal Proteins (analysis), Fungal Proteins (metabolism), Glutathione (metabolism), Humans (MeSH), Hyphae (chemistry), Hyphae (enzymology), Hyphae (growth & development), Hyphae (metabolism), Isocitrate Lyase (analysis), Isocitrate Lyase (metabolism), Malate Synthase (analysis), Malate Synthase (metabolism), Mitochondrial Proteins (analysis), Mitochondrial Proteins (metabolism), Models, Molecular (MeSH), Sequence Alignment (MeSH).
- MESH :
- chemical , analysis : Aconitate Hydratase, Fungal Proteins, Isocitrate Lyase, Malate Synthase, Mitochondrial Proteins.
- chemical , metabolism : Aconitate Hydratase, Fungal Proteins, Glutathione, Isocitrate Lyase, Malate Synthase, Mitochondrial Proteins.
- chemistry : Candida albicans, Hyphae.
- enzymology : Candida albicans, Hyphae.
- growth & development : Candida albicans, Hyphae.
- metabolism : Candida albicans, Hyphae.
- microbiology : Candidiasis.
- Amino Acid Sequence, Humans, Models, Molecular, Sequence Alignment.
Abstract
Candida albicans is an opportunist pathogen responsible for a large spectrum of infections, from superficial mycosis to the systemic disease candidiasis. Its ability to adopt various morphological forms, such as unicellular yeasts, filamentous pseudohyphae and hyphae, contributes to its ability to survive within the host. It has been suggested that the antioxidant glutathione is involved in the filamentation process. We investigated S-glutathionylation, the reversible binding of glutathione to proteins, and the functional consequences on C. albicans metabolic remodeling during the yeast-to-hyphae transition. Our work provided evidence for the specific glutathionylation of mitochondrial proteins involved in bioenergetics pathways in filamentous forms and a regulation of the main enzyme of the glyoxylate cycle, isocitrate lyase, by glutathionylation. Isocitrate lyase inactivation in the hyphal forms was reversed by glutaredoxin treatment, in agreement with a glutathionylation process, which was confirmed by proteomic data showing the binding of one glutathione molecule to the enzyme (data are available via ProteomeXchange with identifier PXD003685). We also assessed the effect of alternative carbon sources on glutathione levels and isocitrate lyase activity. Changes in nutrient availability led to morphological flexibility and were related to perturbations in glutathione levels and isocitrate lyase activity, confirming the key role of the maintenance of intracellular redox status in the adaptive metabolic strategy of the pathogen.
DOI: 10.1016/j.bbadis.2016.04.004
PubMed: 27083931
Affiliations:
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(metabolism)</term><term>Candidiasis (microbiology)</term><term>Fungal Proteins (analysis)</term><term>Fungal Proteins (metabolism)</term><term>Glutathione (metabolism)</term><term>Humans (MeSH)</term><term>Hyphae (chemistry)</term><term>Hyphae (enzymology)</term><term>Hyphae (growth & development)</term><term>Hyphae (metabolism)</term><term>Isocitrate Lyase (analysis)</term><term>Isocitrate Lyase (metabolism)</term><term>Malate Synthase (analysis)</term><term>Malate Synthase (metabolism)</term><term>Mitochondrial Proteins (analysis)</term><term>Mitochondrial Proteins (metabolism)</term><term>Models, Molecular (MeSH)</term><term>Sequence Alignment (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Aconitate hydratase (analyse)</term><term>Aconitate hydratase (métabolisme)</term><term>Alignement de séquences (MeSH)</term><term>Candida albicans (composition chimique)</term><term>Candida albicans (croissance et développement)</term><term>Candida albicans (enzymologie)</term><term>Candida albicans (métabolisme)</term><term>Candidose (microbiologie)</term><term>Glutathion (métabolisme)</term><term>Humains (MeSH)</term><term>Hyphae (composition chimique)</term><term>Hyphae (croissance et développement)</term><term>Hyphae (enzymologie)</term><term>Hyphae (métabolisme)</term><term>Isocitrate lyase (analyse)</term><term>Isocitrate lyase (métabolisme)</term><term>Malate synthase (analyse)</term><term>Malate synthase (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Protéines fongiques (analyse)</term><term>Protéines fongiques (métabolisme)</term><term>Protéines mitochondriales (analyse)</term><term>Protéines mitochondriales (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Aconitate Hydratase</term><term>Fungal Proteins</term><term>Isocitrate Lyase</term><term>Malate Synthase</term><term>Mitochondrial Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Aconitate Hydratase</term><term>Fungal Proteins</term><term>Glutathione</term><term>Isocitrate Lyase</term><term>Malate Synthase</term><term>Mitochondrial Proteins</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Aconitate hydratase</term><term>Isocitrate lyase</term><term>Malate synthase</term><term>Protéines fongiques</term><term>Protéines mitochondriales</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Candida albicans</term><term>Hyphae</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Candida albicans</term><term>Hyphae</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Candida albicans</term><term>Hyphae</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Candida albicans</term><term>Hyphae</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Candida albicans</term><term>Hyphae</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Candida albicans</term><term>Hyphae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Candida albicans</term><term>Hyphae</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Candidose</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Candidiasis</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Aconitate hydratase</term><term>Candida albicans</term><term>Glutathion</term><term>Hyphae</term><term>Isocitrate lyase</term><term>Malate synthase</term><term>Protéines fongiques</term><term>Protéines mitochondriales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Humans</term><term>Models, Molecular</term><term>Sequence Alignment</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Humains</term><term>Modèles moléculaires</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Candida albicans is an opportunist pathogen responsible for a large spectrum of infections, from superficial mycosis to the systemic disease candidiasis. Its ability to adopt various morphological forms, such as unicellular yeasts, filamentous pseudohyphae and hyphae, contributes to its ability to survive within the host. It has been suggested that the antioxidant glutathione is involved in the filamentation process. We investigated S-glutathionylation, the reversible binding of glutathione to proteins, and the functional consequences on C. albicans metabolic remodeling during the yeast-to-hyphae transition. Our work provided evidence for the specific glutathionylation of mitochondrial proteins involved in bioenergetics pathways in filamentous forms and a regulation of the main enzyme of the glyoxylate cycle, isocitrate lyase, by glutathionylation. Isocitrate lyase inactivation in the hyphal forms was reversed by glutaredoxin treatment, in agreement with a glutathionylation process, which was confirmed by proteomic data showing the binding of one glutathione molecule to the enzyme (data are available via ProteomeXchange with identifier PXD003685). We also assessed the effect of alternative carbon sources on glutathione levels and isocitrate lyase activity. Changes in nutrient availability led to morphological flexibility and were related to perturbations in glutathione levels and isocitrate lyase activity, confirming the key role of the maintenance of intracellular redox status in the adaptive metabolic strategy of the pathogen.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27083931</PMID><DateCompleted><Year>2019</Year><Month>01</Month><Day>24</Day></DateCompleted><DateRevised><Year>2019</Year><Month>01</Month><Day>24</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1862</Volume><Issue>7</Issue><PubDate><Year>2016</Year><Month>07</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>The adaptive metabolic response involves specific protein glutathionylation during the filamentation process in the pathogen Candida albicans.</ArticleTitle><Pagination><MedlinePgn>1309-23</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbadis.2016.04.004</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0925-4439(16)30075-8</ELocationID><Abstract><AbstractText>Candida albicans is an opportunist pathogen responsible for a large spectrum of infections, from superficial mycosis to the systemic disease candidiasis. Its ability to adopt various morphological forms, such as unicellular yeasts, filamentous pseudohyphae and hyphae, contributes to its ability to survive within the host. It has been suggested that the antioxidant glutathione is involved in the filamentation process. We investigated S-glutathionylation, the reversible binding of glutathione to proteins, and the functional consequences on C. albicans metabolic remodeling during the yeast-to-hyphae transition. Our work provided evidence for the specific glutathionylation of mitochondrial proteins involved in bioenergetics pathways in filamentous forms and a regulation of the main enzyme of the glyoxylate cycle, isocitrate lyase, by glutathionylation. Isocitrate lyase inactivation in the hyphal forms was reversed by glutaredoxin treatment, in agreement with a glutathionylation process, which was confirmed by proteomic data showing the binding of one glutathione molecule to the enzyme (data are available via ProteomeXchange with identifier PXD003685). We also assessed the effect of alternative carbon sources on glutathione levels and isocitrate lyase activity. Changes in nutrient availability led to morphological flexibility and were related to perturbations in glutathione levels and isocitrate lyase activity, confirming the key role of the maintenance of intracellular redox status in the adaptive metabolic strategy of the pathogen.</AbstractText><CopyrightInformation>Copyright © 2016 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gergondey</LastName><ForeName>R</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Laboratoire Mitochondries, Métaux et Stress Oxydant, Institut Jacques Monod, UMR 7592, Université Paris-Diderot/CNRS, 15 rue Hélène Brion, 75013 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Garcia</LastName><ForeName>C</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Plateforme Protéomique structurale et fonctionnelle/Spectrométrie de masse, Institut Jacques Monod, UMR 7592, Université Paris-Diderot/CNRS, 15 rue Hélène Brion, 75013 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Serre</LastName><ForeName>V</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Laboratoire Mitochondries, Métaux et Stress Oxydant, Institut Jacques Monod, UMR 7592, Université Paris-Diderot/CNRS, 15 rue Hélène Brion, 75013 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Camadro</LastName><ForeName>J M</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Laboratoire Mitochondries, Métaux et Stress Oxydant, Institut Jacques Monod, UMR 7592, Université Paris-Diderot/CNRS, 15 rue Hélène Brion, 75013 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Auchère</LastName><ForeName>F</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Laboratoire Mitochondries, Métaux et Stress Oxydant, Institut Jacques Monod, UMR 7592, Université Paris-Diderot/CNRS, 15 rue Hélène Brion, 75013 Paris, France. Electronic address: francoise.auchere@ijm.fr.</Affiliation></AffiliationInfo></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>2016</Year><Month>04</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D024101">Mitochondrial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.3.3.9</RegistryNumber><NameOfSubstance UI="D008292">Malate Synthase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.1.3.1</RegistryNumber><NameOfSubstance UI="D007522">Isocitrate Lyase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.1.3</RegistryNumber><NameOfSubstance UI="D000154">Aconitate Hydratase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000154" MajorTopicYN="N">Aconitate Hydratase</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002176" MajorTopicYN="N">Candida albicans</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000254" MajorTopicYN="Y">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002177" MajorTopicYN="N">Candidiasis</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D025301" MajorTopicYN="N">Hyphae</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000254" MajorTopicYN="Y">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007522" MajorTopicYN="N">Isocitrate Lyase</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008292" MajorTopicYN="N">Malate Synthase</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D024101" MajorTopicYN="N">Mitochondrial Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Candida albicans</Keyword><Keyword MajorTopicYN="Y">Filamentation</Keyword><Keyword MajorTopicYN="Y">Glutathionylation</Keyword><Keyword MajorTopicYN="Y">Isocitrate lyase</Keyword><Keyword MajorTopicYN="Y">Mitochondria</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>11</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2016</Year><Month>02</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>04</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>4</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>4</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>1</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">27083931</ArticleId><ArticleId IdType="pii">S0925-4439(16)30075-8</ArticleId><ArticleId IdType="doi">10.1016/j.bbadis.2016.04.004</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Île-de-France</li></region><settlement><li>Paris</li></settlement></list><tree><country name="France"><region name="Île-de-France"><name sortKey="Gergondey, R" sort="Gergondey, R" uniqKey="Gergondey R" first="R" last="Gergondey">R. Gergondey</name></region><name sortKey="Auchere, F" sort="Auchere, F" uniqKey="Auchere F" first="F" last="Auchère">F. Auchère</name><name sortKey="Camadro, J M" sort="Camadro, J M" uniqKey="Camadro J" first="J M" last="Camadro">J M Camadro</name><name sortKey="Garcia, C" sort="Garcia, C" uniqKey="Garcia C" first="C" last="Garcia">C. Garcia</name><name sortKey="Serre, V" sort="Serre, V" uniqKey="Serre V" first="V" last="Serre">V. Serre</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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