Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG
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 intracellula...
| Autores principales: | , , , , , |
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| Formato: | info:ar-repo/semantics/artículo |
| Lenguaje: | Inglés |
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Springer
2019
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| Materias: | |
| Acceso en línea: | https://link.springer.com/article/10.1007%2Fs13238-010-0101-3 http://hdl.handle.net/20.500.12123/5119 https://doi.org/10.1007/s13238-010-0101-3 |
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| author | Carroll, Maria V. Sim, Robert B. Bigi, Fabiana Jäkel, Anne Antrobus, Robin Mitchell, Daniel A. |
| author_browse | Antrobus, Robin Bigi, Fabiana Carroll, Maria V. Jäkel, Anne Mitchell, Daniel A. Sim, Robert B. |
| author_facet | Carroll, Maria V. Sim, Robert B. Bigi, Fabiana Jäkel, Anne Antrobus, Robin Mitchell, Daniel A. |
| author_sort | Carroll, Maria V. |
| collection | INTA Digital |
| description | 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. |
| format | info:ar-repo/semantics/artículo |
| id | INTA5119 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2019 |
| publishDateRange | 2019 |
| publishDateSort | 2019 |
| publisher | Springer |
| publisherStr | Springer |
| record_format | dspace |
| spelling | INTA51192019-05-15T14:52:56Z Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG Carroll, Maria V. Sim, Robert B. Bigi, Fabiana Jäkel, Anne Antrobus, Robin Mitchell, Daniel A. Mycobacterium Bovis Identificación Lectinas Proteínas Identification Lectins Proteins 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. Instituto de Biotecnología Fil: Carroll, Maria V. University of Oxford. Department of Pharmacology; Gran Bretaña Fil: Sim, Robert B. University of Oxford. Department of Pharmacology; Gran Bretaña Fil: Bigi, Fabiana. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina Fil: Jäkel, Anne. University of Oxford. Department of Pharmacology; Gran Bretaña Fil: Antrobus, Robin. Addenbrooke’s Hospital. Cambridge Institute of Medical Research; Gran Bretaña Fil: Mitchell, Daniel A. University of Warwick. CSRI-UHCW Walsgrave Campus; Gran Bretaña 2019-05-15T14:50:34Z 2019-05-15T14:50:34Z 2010-09 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion https://link.springer.com/article/10.1007%2Fs13238-010-0101-3 http://hdl.handle.net/20.500.12123/5119 1674-800X 1674-8018 https://doi.org/10.1007/s13238-010-0101-3 eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) application/pdf Springer Protein & Cell 1 (9) : 859–870 (September 2010) |
| spellingShingle | Mycobacterium Bovis Identificación Lectinas Proteínas Identification Lectins Proteins Carroll, Maria V. Sim, Robert B. Bigi, Fabiana Jäkel, Anne Antrobus, Robin Mitchell, Daniel A. Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG |
| title | Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG |
| title_full | Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG |
| title_fullStr | Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG |
| title_full_unstemmed | Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG |
| title_short | Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG |
| title_sort | identification of four novel dc sign ligands on mycobacterium bovis bcg |
| topic | Mycobacterium Bovis Identificación Lectinas Proteínas Identification Lectins Proteins |
| url | https://link.springer.com/article/10.1007%2Fs13238-010-0101-3 http://hdl.handle.net/20.500.12123/5119 https://doi.org/10.1007/s13238-010-0101-3 |
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