Cutting Edge: Carbohydrate Profiling Identifies New Pathogens That Interact with Dendritic Cell-Specific ICAM-3-Grabbing Nonintegrin on Dendritic Cells

• Published in: The Journal of immunology (1950) Vol. 170; no. 4; pp. 1635 - 1639
• Main Authors: Appelmelk, Ben J, van Die, Irma, van Vliet, Sandra J, Vandenbroucke-Grauls, Christina M. J. E, Geijtenbeek, Teunis B. H, van Kooyk, Yvette
• Format: Journal Article
• Language: English
• Published: United States Am Assoc Immnol 15-02-2003
• Subjects: Animals; Carbohydrate Metabolism; Carbohydrate Sequence; Carbohydrates - immunology; Cell Adhesion - immunology; Cell Adhesion Molecules - immunology; Cell Adhesion Molecules - metabolism; Cells, Cultured; CHO Cells; Cricetinae; Dendritic Cells - immunology; Dendritic Cells - metabolism; Dendritic Cells - microbiology; Dendritic Cells - parasitology; Fucose - immunology; Fucose - metabolism; Helicobacter pylori - immunology; Helicobacter pylori - pathogenicity; Humans; K562 Cells; Lectins, C-Type - immunology; Lectins, C-Type - metabolism; Leishmania mexicana - immunology; Leishmania mexicana - pathogenicity; Mannose - immunology; Mannose - metabolism; Molecular Sequence Data; Mycobacterium tuberculosis - immunology; Mycobacterium tuberculosis - pathogenicity; Protein Binding - immunology; Receptors, Cell Surface - immunology; Receptors, Cell Surface - metabolism; Recombinant Fusion Proteins - immunology; Recombinant Fusion Proteins - metabolism; Schistosoma mansoni - immunology; Schistosoma mansoni - pathogenicity; Transfection
• ISSN: 0022-1767; 1550-6606
• DOI: 10.4049/jimmunol.170.4.1635

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.