title: Cutting edge: carbohydrate profiling identifies new pathogens that interact with dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic cells.
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.
authors.affiliation: Department of Medical Microbiology, Vrije Universiteit Medical Center, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands.
authors.forename: Ben J
authors.initials: BJ
authors.lastname: Appelmelk
authors.forename: Irma
authors.initials: I
authors.lastname: van Die
authors.forename: Sandra J
authors.initials: SJ
authors.lastname: van Vliet
authors.forename: Christina M J E
authors.initials: CM
authors.lastname: Vandenbroucke-Grauls
authors.forename: Teunis B H
authors.initials: TB
authors.lastname: Geijtenbeek
authors.forename: Yvette
authors.initials: Y
authors.lastname: van Kooyk
mesh_terms: D000818:Animals; D016466:CHO Cells; D050260:Carbohydrate Metabolism; D002240:Carbohydrate Sequence; D002241:Carbohydrates / Q000276:immunology*; D002448:Cell Adhesion / Q000276:immunology; D015815:Cell Adhesion Molecules / Q000276:immunology / Q000378:metabolism*; D002478:Cells, Cultured; D006224:Cricetinae; D003713:Dendritic Cells / Q000276:immunology / Q000378:metabolism / Q000382:microbiology* / Q000469:parasitology*; D005643:Fucose / Q000276:immunology / Q000378:metabolism; D016480:Helicobacter pylori / Q000276:immunology / Q000472:pathogenicity; D006801:Humans; D020014:K562 Cells; D037181:Lectins, C-Type / Q000276:immunology / Q000378:metabolism*; D007894:Leishmania mexicana / Q000276:immunology / Q000472:pathogenicity; D008358:Mannose / Q000276:immunology / Q000378:metabolism; D008969:Molecular Sequence Data; D009169:Mycobacterium tuberculosis / Q000276:immunology / Q000472:pathogenicity; D011485:Protein Binding / Q000276:immunology; D011956:Receptors, Cell Surface / Q000276:immunology / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000276:immunology / Q000378:metabolism; D012550:Schistosoma mansoni / Q000276:immunology / Q000472:pathogenicity; D014162:Transfection; D000099215:DC-Specific ICAM-3 Grabbing Nonintegrin
chemical_list: D002241:Carbohydrates; D015815:Cell Adhesion Molecules; D005643:Fucose; D037181:Lectins, C-Type; D008358:Mannose; D011956:Receptors, Cell Surface; D011993:Recombinant Fusion Proteins; D000099215:DC-Specific ICAM-3 Grabbing Nonintegrin