Cutting edge: carbohydrate profiling identifies new pathogens that interact with dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic cells.
Ben J Appelmelk, Irma van Die, Sandra J van Vliet, Christina M J E Vandenbroucke-Grauls, Teunis B H Geijtenbeek, Yvette van Kooyk
Index: J. Toxicol. Environ. Health A 77(22-24) , 1419-30, (2014)
Full Text: HTML
Abstract
Dendritic cells (DC) are instrumental in handling pathogens for processing and presentation to T cells, thus eliciting an appropriate immune response. C-type lectins expressed by DC function as pathogen-recognition receptors; yet their specificity for carbohydrate structures on pathogens is not fully understood. In this study, we analyzed the carbohydrate specificity of DC-specific ICAM-3-grabbing nonintegrin (SIGN)/CD209, the recently documented HIV-1 receptor on DC. Our studies show that DC-SIGN binds with high affinity to both synthetic mannose- and fucose-containing glycoconjugates. These carbohydrate structures are abundantly expressed by pathogens as demonstrated by the affinity of DC-SIGN for natural surface glycans of the human pathogens Mycobacterium tuberculosis, Helicobacter pylori, Leishmania mexicana, and Schistosoma mansoni. This analysis expands our knowledge on the carbohydrate and pathogen-specificity of DC-SIGN and identifies this lectin to be central in pathogen-DC interactions.
Related Compounds
Related Articles:
2015-01-01
[Arch. Toxicol. 89(1) , 107-19, (2015)]
2014-10-15
[Biochem. Pharmacol. 91(4) , 543-51, (2014)]
2014-07-01
[G3 (Bethesda) 4(7) , 1247-58, (2014)]
2010-01-01
[Chem. Res. Toxicol. 23 , 171-83, (2010)]
2011-12-01
[J. Sci. Ind. Res. 65(10) , 808, (2006)]