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Abstract
Dendritic-cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN; CD209) has an important role in mediating adherence of Mycobacteria species, including M. tuberculosis and M. bovis BCG to human dendritic cells and macrophages, in which these bacteria can survive intracellularly. DC-SIGN is a C-type lectin, and interactions with mycobacterial cells are believed to occur via mannosylated structures on the mycobacterial surface. [ver mas...]
dc.contributor.authorCarroll, Maria V.
dc.contributor.authorSim, Robert B.
dc.contributor.authorBigi, Fabiana
dc.contributor.authorJäkel, Anne
dc.contributor.authorAntrobus, Robin
dc.contributor.authorMitchell, Daniel A.
dc.date.accessioned2019-05-15T14:50:34Z
dc.date.available2019-05-15T14:50:34Z
dc.date.issued2010-09
dc.identifier.issn1674-800X
dc.identifier.issn1674-8018
dc.identifier.otherhttps://doi.org/10.1007/s13238-010-0101-3
dc.identifier.urihttps://link.springer.com/article/10.1007%2Fs13238-010-0101-3
dc.identifier.urihttp://hdl.handle.net/20.500.12123/5119
dc.description.abstractDendritic-cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN; CD209) has an important role in mediating adherence of Mycobacteria species, including M. tuberculosis and M. bovis BCG to human dendritic cells and macrophages, in which these bacteria can survive intracellularly. DC-SIGN is a C-type lectin, and interactions with mycobacterial cells are believed to occur via mannosylated structures on the mycobacterial surface. Recent studies suggest more varied modes of binding to multiple mycobacterial ligands. Here we identify, by affinity chromatography and mass-spectrometry, four novel ligands of M. bovis BCG that bind to DC-SIGN. The novel ligands are chaperone protein DnaK, 60 kDa chaperonin-1 (Cpn60.1), glyceraldehyde-3 phosphate dehydrogenase (GAPDH) and lipoprotein lprG. Other published work strongly suggests that these are on the cell surface. Of these ligands, lprG appears to bind DC-SIGN via typical proteinglycan interactions, but DnaK and Cpn60.1 binding do not show evidence of carbohydrate-dependent interactions. LprG was also identified as a ligand for DC-SIGNR (L-SIGN; CD299) and the M. tuberculosis orthologue of lprG has been found previously to interact with human toll-like receptor 2. Collectively, these findings offer new targets for combating mycobacterial adhesion and within-host survival, and reinforce the role of DCSIGN as an important host ligand in mycobacterial infection.eng
dc.formatapplication/pdfes_AR
dc.language.isoenges_AR
dc.publisherSpringeres_AR
dc.rightsinfo:eu-repo/semantics/openAccesses_AR
dc.sourceProtein & Cell 1 (9) : 859–870 (September 2010)es_AR
dc.subjectMycobacterium Bovises_AR
dc.subjectIdentificaciónes_AR
dc.subjectIdentificationeng
dc.subjectLectinases_AR
dc.subjectLectinseng
dc.subjectProteínases_AR
dc.subjectProteinseng
dc.titleIdentification of four novel DC-SIGN ligands on Mycobacterium bovis BCGes_AR
dc.typeinfo:ar-repo/semantics/artículoes_AR
dc.typeinfo:eu-repo/semantics/articlees_AR
dc.typeinfo:eu-repo/semantics/publishedVersiones_AR
dc.description.origenInstituto de Biotecnologíaes_AR
dc.description.filFil: Carroll, Maria V. University of Oxford. Department of Pharmacology; Gran Bretañaes_AR
dc.description.filFil: Sim, Robert B. University of Oxford. Department of Pharmacology; Gran Bretañaes_AR
dc.description.filFil: Bigi, Fabiana. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentinaes_AR
dc.description.filFil: Jäkel, Anne. University of Oxford. Department of Pharmacology; Gran Bretañaes_AR
dc.description.filFil: Antrobus, Robin. Addenbrooke’s Hospital. Cambridge Institute of Medical Research; Gran Bretañaes_AR
dc.description.filFil: Mitchell, Daniel A. University of Warwick. CSRI-UHCW Walsgrave Campus; Gran Bretañaes_AR
dc.subtypecientifico


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