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 languageEnglish
Pages (from-to)1635-9
Number of pages5
JournalJournal of Immunology
Volume170
Issue number4
Publication statusPublished - 15 Feb 2003

Cite this

@article{e6d9c9988a714b85b24264c0038e61d2,
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.",
keywords = "Animals, CHO Cells, Carbohydrate Metabolism, Carbohydrate Sequence, Carbohydrates/immunology, Cell Adhesion/immunology, Cell Adhesion Molecules/immunology, Cells, Cultured, Cricetinae, Dendritic Cells/immunology, Fucose/immunology, Helicobacter pylori/immunology, Humans, K562 Cells, Lectins, C-Type/immunology, Leishmania mexicana/immunology, Mannose/immunology, Molecular Sequence Data, Mycobacterium tuberculosis/immunology, Protein Binding/immunology, Receptors, Cell Surface/immunology, Recombinant Fusion Proteins/immunology, Schistosoma mansoni/immunology, Transfection",
author = "Appelmelk, {Ben J} and {van Die}, Irma and {van Vliet}, {Sandra J} and Vandenbroucke-Grauls, {Christina M J E} and Geijtenbeek, {Teunis B H} and {van Kooyk}, Yvette",
year = "2003",
month = "2",
day = "15",
language = "English",
volume = "170",
pages = "1635--9",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "4",

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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 -