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dc.contributor.author
Carroll, Maria V.
dc.contributor.author
Sim, Robert B.
dc.contributor.author
Bigi, Fabiana
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Jäkel, Anne
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Antrobus, Robin
dc.contributor.author
Mitchell, Daniel A.
dc.date.available
2023-03-14T13:13:36Z
dc.date.issued
2010-09
dc.identifier.citation
Carroll, Maria V.; Sim, Robert B.; Bigi, Fabiana; Jäkel, Anne; Antrobus, Robin; et al.; Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG; Springer; Protein and Cell; 1; 9; 9-2010; 859-870
dc.identifier.issn
1674-8018
dc.identifier.uri
http://hdl.handle.net/11336/190455
dc.description.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. 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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
DC-SIGN
dc.subject
LECTINS
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MYCOBACTERIA
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Biología Celular, Microbiología
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2023-03-12T15:48:16Z
dc.journal.volume
1
dc.journal.number
9
dc.journal.pagination
859-870
dc.journal.pais
China
dc.description.fil
Fil: Carroll, Maria V.. University of Oxford; Reino Unido
dc.description.fil
Fil: Sim, Robert B.. University of Oxford; Reino Unido
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Fil: Bigi, Fabiana. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
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Fil: Jäkel, Anne. University of Oxford; Reino Unido
dc.description.fil
Fil: Antrobus, Robin. Cambridge Institute of Medical Research; Reino Unido
dc.description.fil
Fil: Mitchell, Daniel A.. University of Warwick; Reino Unido
dc.journal.title
Protein and Cell
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s13238-010-0101-3
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s13238-010-0101-3
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