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The Journal of Immunology, 2003, 170: 1635-1639.
Copyright © 2003 by The American Association of Immunologists

CUTTING EDGE

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{dagger}, Sandra J. van Vliet{dagger}, Christina M. J. E. Vandenbroucke-Grauls*, Teunis B. H. Geijtenbeek{dagger} and Yvette van Kooyk1,{dagger}

Departments of * Medical Microbiology and {dagger} Molecular Cell Biology, Vrije Universiteit Medical Center, Amsterdam, The Netherlands

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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I. Pelletier, T. Hashidate, T. Urashima, N. Nishi, T. Nakamura, M. Futai, Y. Arata, K.-i. Kasai, M. Hirashima, J. Hirabayashi, et al.
Specific Recognition of Leishmania major Poly-{beta}-galactosyl Epitopes by Galectin-9: POSSIBLE IMPLICATION OF GALECTIN-9 IN INTERACTION BETWEEN L. MAJOR AND HOST CELLS
J. Biol. Chem., June 13, 2003; 278(25): 22223 - 22230.
[Abstract] [Full Text] [PDF]


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