DC-SIGN: escape mechanism for pathogens
Top Cited Papers
- 1 September 2003
- journal article
- review article
- Published by Springer Nature in Nature Reviews Immunology
- Vol. 3 (9) , 697-709
- https://doi.org/10.1038/nri1182
Abstract
Dendritic cells (DCs) are crucial in the defence against pathogens. Invading pathogens are recognized by Toll-like receptors (TLRs) and receptors such as C-type lectins expressed on the surface of DCs. However, it is becoming evident that some pathogens, including viruses, such as HIV-1, and non-viral pathogens, such as Mycobacterium tuberculosis, subvert DC functions to escape immune surveillance by targeting the C-type lectin DC-SIGN (DC-specific intercellular adhesion molecule-grabbing nonintegrin). Notably, these pathogens misuse DC-SIGN by distinct mechanisms that either circumvent antigen processing or alter TLR-mediated signalling, skewing T-cell responses. This implies that adaptation of pathogens to target DC-SIGN might support pathogen survival.Keywords
This publication has 144 references indexed in Scilit:
- DC-SIGN (CD209) Mediates Dengue Virus Infection of Human Dendritic CellsThe Journal of Experimental Medicine, 2003
- The dendritic cell-specific C-type lectin DC-SIGN is a receptor for Schistosoma mansoni egg antigens and recognizes the glycan antigen Lewis xGlycobiology, 2003
- Involvement of macrophage mannose receptor in the binding and transmission of HIV by macrophagesEuropean Journal of Immunology, 2003
- Identification of Different Binding Sites in the Dendritic Cell-specific Receptor DC-SIGN for Intercellular Adhesion Molecule 3 and HIV-1Journal of Biological Chemistry, 2002
- Specialization and complementarity in microbial molecule recognition by human myeloid and plasmacytoid dendritic cellsEuropean Journal of Immunology, 2001
- Binding Properties of the Mannose ReceptorImmunobiology, 2001
- New structural insights into the molecular deciphering of mycobacterial lipoglycan binding to C-type lectins: lipoarabinomannan glycoform characterization and quantification by capillary electrophoresis at the subnanomole levelJournal of Molecular Biology, 2000
- The Immunological Synapse: A Molecular Machine Controlling T Cell ActivationScience, 1999
- Ligand-specificity of the selectinsJournal of Cellular Biochemistry, 1996
- Heterogenous glycosylation of ICAM‐3 and lack of interaction with Mac‐1 and p150,95European Journal of Immunology, 1995