Cutting edge: carbohydrate profiling identifies new pathogens that interact with dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic cells
BJ Appelmelk, I van Die, SJ van Vliet… - The Journal of …, 2003 - journals.aai.org
BJ Appelmelk, I van Die, SJ van Vliet, CMJE Vandenbroucke-Grauls, TBH Geijtenbeek…
The Journal of Immunology, 2003•journals.aai.orgDendritic 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 …
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 …
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.
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