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dc.rights.licenseopenen_US
dc.contributor.authorLAURIAN, Romain
dc.contributor.authorRAVENT, Jade
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorDEMENTHON, Karine
dc.contributor.authorLEMAIRE, Marc
dc.contributor.authorSOULARD, Alexandre
dc.contributor.authorCOTTON, Pascale
dc.date.accessioned2023-05-23T12:27:41Z
dc.date.available2023-05-23T12:27:41Z
dc.date.issued2021
dc.identifier.issn2076-2607en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/182264
dc.description.abstractEnSurvival of the pathogenic yeast Candida albicans depends upon assimilation of fermentable and non-fermentable carbon sources detected in host microenvironments. Among the various carbon sources encountered in a human body, glucose is the primary source of energy. Its effective detection, metabolism and prioritization via glucose repression are primordial for the metabolic adaptation of the pathogen. In C. albicans, glucose phosphorylation is mainly performed by the hexokinase 2 (CaHxk2). In addition, in the presence of glucose, CaHxK2 migrates in the nucleus and contributes to the glucose repression signaling pathway. Based on the known dual function of the Saccharomyces cerevisiae hexokinase 2 (ScHxk2), we intended to explore the impact of both enzymatic and regulatory functions of CaHxk2 on virulence, using a site-directed mutagenesis approach. We show that the conserved aspartate residue at position 210, implicated in the interaction with glucose, is essential for enzymatic and glucose repression functions but also for filamentation and virulence in macrophages. Point mutations and deletion into the N-terminal region known to specifically affect glucose repression in ScHxk2 proved to be ineffective in CaHxk2. These results clearly show that enzymatic and regulatory functions of the hexokinase 2 cannot be unlinked in C. albicans.
dc.language.isoENen_US
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.subject.enSaccharomyces cerevisiae
dc.subject.enhexokinase 2
dc.subject.englucose repression
dc.subject.enhexose kinase activity
dc.subject.enhyphal transition
dc.subject.envirulence
dc.title.enCandida albicans Hexokinase 2 Challenges the Saccharomyces cerevisiae Moonlight Protein Model
dc.typeArticle de revueen_US
dc.identifier.doi10.3390/microorganisms9040848en_US
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologie/Mycologieen_US
bordeaux.journalMicroorganismsen_US
bordeaux.page848en_US
bordeaux.volume9en_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.issue4en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcehal
hal.identifierhal-03199412
hal.version1
hal.exportfalse
workflow.import.sourcehal
dc.rights.ccCC BYen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Microorganisms&rft.date=2021&rft.volume=9&rft.issue=4&rft.spage=848&rft.epage=848&rft.eissn=2076-2607&rft.issn=2076-2607&rft.au=LAURIAN,%20Romain&RAVENT,%20Jade&DEMENTHON,%20Karine&LEMAIRE,%20Marc&SOULARD,%20Alexandre&rft.genre=article


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