Cutting edge: carbohydrate profiling identifies new pathogens that interact with dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic cells

J Immunol. 2003 Feb 15;170(4):1635-9. doi: 10.4049/jimmunol.170.4.1635.

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.

MeSH terms

  • Animals
  • CHO Cells
  • Carbohydrate Metabolism*
  • Carbohydrate Sequence
  • Carbohydrates / immunology*
  • Cell Adhesion / immunology
  • Cell Adhesion Molecules / immunology
  • Cell Adhesion Molecules / metabolism*
  • Cells, Cultured
  • 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

Substances

  • Carbohydrates
  • Cell Adhesion Molecules
  • DC-specific ICAM-3 grabbing nonintegrin
  • Lectins, C-Type
  • Receptors, Cell Surface
  • Recombinant Fusion Proteins
  • Fucose
  • Mannose