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Protein O-mannosylation deficiency increases LprG-associated lipoarabinomannan release by Mycobacterium tuberculosis and enhances the TLR2-associated inflammatory response

dc.contributor.authorALONSO, Henar
hal.structure.identifierInstitut de pharmacologie et de biologie structurale [IPBS]
dc.contributor.authorPARRA, Julien
hal.structure.identifierInstitut de pharmacologie et de biologie structurale [IPBS]
dc.contributor.authorMALAGA, Wladimir
hal.structure.identifierInstitut de pharmacologie et de biologie structurale [IPBS]
dc.contributor.authorPAYROS, Delphine
dc.contributor.authorLIU, Chia-Fang
dc.contributor.authorBERRONE, Céline
hal.structure.identifierLaboratoire Angevin de Mécanique, Procédés et InnovAtion [LAMPA]
dc.contributor.authorROBERT, Camille
hal.structure.identifierPolarisation des Macrophages et Récepteurs Nucléaires dans les Pathologies Inflammatoires et Infectieuses
dc.contributor.authorMEUNIER, Etienne
hal.structure.identifierInstitut de pharmacologie et de biologie structurale [IPBS]
dc.contributor.authorBURLET-SCHILTZ, Odile
hal.structure.identifierInstitut de pharmacologie et de biologie structurale [IPBS]
dc.contributor.authorRIVIÈRE, Michel
hal.structure.identifierInstitut de pharmacologie et de biologie structurale [IPBS]
dc.contributor.authorGUILHOT, Christophe
dc.date.accessioned2021-05-14T09:30:15Z
dc.date.available2021-05-14T09:30:15Z
dc.date.issued2017-12
dc.identifier.issn2045-2322
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/75797
dc.description.abstractEnProtein O-mannosylation is crucial for the biology of Mycobacterium tuberculosis but the key mannosylated protein(s) involved and its(their) underlying function(s) remain unknown. Here, we demonstrated that the M. tuberculosis mutant (Δpmt) deficient for protein O-mannosylation exhibits enhanced release of lipoarabinomannan (LAM) in a complex with LprG, a lipoprotein required for LAM translocation to the cell surface. We determined that LprG is O-mannosylated at a unique threonine position by mass spectrometry analyses of the purified protein. However, although replacement of this amino acid by an alanine residue completely abolished LprG O-mannosylation, the increased release of the LAM/LprG complex was preserved. We found that the increased secretion of this complex is due to enhanced LAM production in the Δpmt M. tuberculosis and M. smegmatis mutants relative to their wildtype counterparts. This abnormal release of LAM/LprG has functional consequences on the induction of inflammatory responses and provides a possible explanation for the reduced virulence of the M. tuberculosis Δpmt mutant.
dc.language.isoen
dc.publisherNature Publishing Group
dc.title.enProtein O-mannosylation deficiency increases LprG-associated lipoarabinomannan release by Mycobacterium tuberculosis and enhances the TLR2-associated inflammatory response
dc.typeArticle de revue
dc.identifier.doi10.1038/s41598-017-08489-7
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie moléculaire
bordeaux.journalScientific Reports
bordeaux.volume7
bordeaux.hal.laboratoriesInstitut de Mécanique et d’Ingénierie de Bordeaux (I2M) - UMR 5295*
bordeaux.issue1
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
bordeaux.institutionCNRS
bordeaux.institutionINRAE
bordeaux.institutionArts et Métiers
bordeaux.peerReviewedoui
hal.identifierhal-02323721
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02323721v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Scientific%20Reports&rft.date=2017-12&rft.volume=7&rft.issue=1&rft.eissn=2045-2322&rft.issn=2045-2322&rft.au=ALONSO,%20Henar&PARRA,%20Julien&MALAGA,%20Wladimir&PAYROS,%20Delphine&LIU,%20Chia-Fang&rft.genre=article


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