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.
| Original language | English |
|---|---|
| Pages (from-to) | 1635-9 |
| Number of pages | 5 |
| Journal | Journal of Immunology |
| Volume | 170 |
| Issue number | 4 |
| Publication status | Published - 15 Feb 2003 |
Cite this
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Cutting edge : carbohydrate profiling identifies new pathogens that interact with dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic cells. / Appelmelk, Ben J; van Die, Irma; van Vliet, Sandra J; Vandenbroucke-Grauls, Christina M J E; Geijtenbeek, Teunis B H; van Kooyk, Yvette.
In: Journal of Immunology, Vol. 170, No. 4, 15.02.2003, p. 1635-9.Research output: Contribution to journal › Article › Academic › peer-review
TY - JOUR
T1 - Cutting edge
T2 - carbohydrate profiling identifies new pathogens that interact with dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic cells
AU - Appelmelk, Ben J
AU - van Die, Irma
AU - van Vliet, Sandra J
AU - Vandenbroucke-Grauls, Christina M J E
AU - Geijtenbeek, Teunis B H
AU - van Kooyk, Yvette
PY - 2003/2/15
Y1 - 2003/2/15
N2 - 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.
AB - 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.
KW - Animals
KW - CHO Cells
KW - Carbohydrate Metabolism
KW - Carbohydrate Sequence
KW - Carbohydrates/immunology
KW - Cell Adhesion/immunology
KW - Cell Adhesion Molecules/immunology
KW - Cells, Cultured
KW - Cricetinae
KW - Dendritic Cells/immunology
KW - Fucose/immunology
KW - Helicobacter pylori/immunology
KW - Humans
KW - K562 Cells
KW - Lectins, C-Type/immunology
KW - Leishmania mexicana/immunology
KW - Mannose/immunology
KW - Molecular Sequence Data
KW - Mycobacterium tuberculosis/immunology
KW - Protein Binding/immunology
KW - Receptors, Cell Surface/immunology
KW - Recombinant Fusion Proteins/immunology
KW - Schistosoma mansoni/immunology
KW - Transfection
M3 - Article
VL - 170
SP - 1635
EP - 1639
JO - Journal of Immunology
JF - Journal of Immunology
SN - 0022-1767
IS - 4
ER -