Carbohydrate profiling reveals a distinctive role for the C-type lectin MGL in the recognition of helminth parasites and tumor antigens by dendritic cells

Sandra J van Vliet, Ellis van Liempt, Eirikur Saeland, Corlien A Aarnoudse, Ben Appelmelk, Tatsuro Irimura, Teunis B H Geijtenbeek, Ola Blixt, Richard Alvarez, Irma van Die, Yvette van Kooyk

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Abstract

Dendritic cells (DCs) are key to the maintenance of peripheral tolerance to self-antigens and the orchestration of an immune reaction to foreign antigens. C-type lectins, expressed by DCs, recognize carbohydrate moieties on antigens that can be internalized for processing and presentation. Little is known about the exact glycan structures on self-antigens and pathogens that are specifically recognized by the different C-type lectins and how this interaction influences DC function. We have analyzed the carbohydrate specificity of the human C-type lectin macrophage galactose-type lectin (MGL) using glycan microarray profiling and identified an exclusive specificity for terminal alpha- and beta-linked GalNAc residues that naturally occur as parts of glycoproteins or glycosphingolipids. Specific glycan structures containing terminal GalNAc moieties, expressed by the human helminth parasite Schistosoma mansoni as well as tumor antigens and a subset of gangliosides, were identified as ligands for MGL. Our results indicate an endogenous function for DC-expressed MGL in the clearance and tolerance to self-gangliosides, and in the pattern recognition of tumor antigens and foreign glycoproteins derived from helminth parasites.

Original languageEnglish
Pages (from-to)661-669
Number of pages9
JournalInternational Immunology
Volume17
Issue number5
DOIs
Publication statusPublished - May 2005

Cite this

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title = "Carbohydrate profiling reveals a distinctive role for the C-type lectin MGL in the recognition of helminth parasites and tumor antigens by dendritic cells",
abstract = "Dendritic cells (DCs) are key to the maintenance of peripheral tolerance to self-antigens and the orchestration of an immune reaction to foreign antigens. C-type lectins, expressed by DCs, recognize carbohydrate moieties on antigens that can be internalized for processing and presentation. Little is known about the exact glycan structures on self-antigens and pathogens that are specifically recognized by the different C-type lectins and how this interaction influences DC function. We have analyzed the carbohydrate specificity of the human C-type lectin macrophage galactose-type lectin (MGL) using glycan microarray profiling and identified an exclusive specificity for terminal alpha- and beta-linked GalNAc residues that naturally occur as parts of glycoproteins or glycosphingolipids. Specific glycan structures containing terminal GalNAc moieties, expressed by the human helminth parasite Schistosoma mansoni as well as tumor antigens and a subset of gangliosides, were identified as ligands for MGL. Our results indicate an endogenous function for DC-expressed MGL in the clearance and tolerance to self-gangliosides, and in the pattern recognition of tumor antigens and foreign glycoproteins derived from helminth parasites.",
keywords = "Animals, Antigen Presentation, Antigens, Helminth/immunology, Antigens, Tumor-Associated, Carbohydrate/immunology, Carbohydrates/immunology, Cell Line, Tumor, Cells, Cultured, Dendritic Cells/immunology, Galactose/immunology, Glucose/immunology, Glycoproteins/immunology, Glycosphingolipids/immunology, Humans, Lectins, C-Type/metabolism, Receptors, Cell Surface/immunology, Schistosoma mansoni/immunology",
author = "{van Vliet}, {Sandra J} and {van Liempt}, Ellis and Eirikur Saeland and Aarnoudse, {Corlien A} and Ben Appelmelk and Tatsuro Irimura and Geijtenbeek, {Teunis B H} and Ola Blixt and Richard Alvarez and {van Die}, Irma and {van Kooyk}, Yvette",
year = "2005",
month = "5",
doi = "10.1093/intimm/dxh246",
language = "English",
volume = "17",
pages = "661--669",
journal = "International Immunology",
issn = "0953-8178",
publisher = "Oxford University Press",
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Carbohydrate profiling reveals a distinctive role for the C-type lectin MGL in the recognition of helminth parasites and tumor antigens by dendritic cells. / van Vliet, Sandra J; van Liempt, Ellis; Saeland, Eirikur; Aarnoudse, Corlien A; Appelmelk, Ben; Irimura, Tatsuro; Geijtenbeek, Teunis B H; Blixt, Ola; Alvarez, Richard; van Die, Irma; van Kooyk, Yvette.

In: International Immunology, Vol. 17, No. 5, 05.2005, p. 661-669.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Carbohydrate profiling reveals a distinctive role for the C-type lectin MGL in the recognition of helminth parasites and tumor antigens by dendritic cells

AU - van Vliet, Sandra J

AU - van Liempt, Ellis

AU - Saeland, Eirikur

AU - Aarnoudse, Corlien A

AU - Appelmelk, Ben

AU - Irimura, Tatsuro

AU - Geijtenbeek, Teunis B H

AU - Blixt, Ola

AU - Alvarez, Richard

AU - van Die, Irma

AU - van Kooyk, Yvette

PY - 2005/5

Y1 - 2005/5

N2 - Dendritic cells (DCs) are key to the maintenance of peripheral tolerance to self-antigens and the orchestration of an immune reaction to foreign antigens. C-type lectins, expressed by DCs, recognize carbohydrate moieties on antigens that can be internalized for processing and presentation. Little is known about the exact glycan structures on self-antigens and pathogens that are specifically recognized by the different C-type lectins and how this interaction influences DC function. We have analyzed the carbohydrate specificity of the human C-type lectin macrophage galactose-type lectin (MGL) using glycan microarray profiling and identified an exclusive specificity for terminal alpha- and beta-linked GalNAc residues that naturally occur as parts of glycoproteins or glycosphingolipids. Specific glycan structures containing terminal GalNAc moieties, expressed by the human helminth parasite Schistosoma mansoni as well as tumor antigens and a subset of gangliosides, were identified as ligands for MGL. Our results indicate an endogenous function for DC-expressed MGL in the clearance and tolerance to self-gangliosides, and in the pattern recognition of tumor antigens and foreign glycoproteins derived from helminth parasites.

AB - Dendritic cells (DCs) are key to the maintenance of peripheral tolerance to self-antigens and the orchestration of an immune reaction to foreign antigens. C-type lectins, expressed by DCs, recognize carbohydrate moieties on antigens that can be internalized for processing and presentation. Little is known about the exact glycan structures on self-antigens and pathogens that are specifically recognized by the different C-type lectins and how this interaction influences DC function. We have analyzed the carbohydrate specificity of the human C-type lectin macrophage galactose-type lectin (MGL) using glycan microarray profiling and identified an exclusive specificity for terminal alpha- and beta-linked GalNAc residues that naturally occur as parts of glycoproteins or glycosphingolipids. Specific glycan structures containing terminal GalNAc moieties, expressed by the human helminth parasite Schistosoma mansoni as well as tumor antigens and a subset of gangliosides, were identified as ligands for MGL. Our results indicate an endogenous function for DC-expressed MGL in the clearance and tolerance to self-gangliosides, and in the pattern recognition of tumor antigens and foreign glycoproteins derived from helminth parasites.

KW - Animals

KW - Antigen Presentation

KW - Antigens, Helminth/immunology

KW - Antigens, Tumor-Associated, Carbohydrate/immunology

KW - Carbohydrates/immunology

KW - Cell Line, Tumor

KW - Cells, Cultured

KW - Dendritic Cells/immunology

KW - Galactose/immunology

KW - Glucose/immunology

KW - Glycoproteins/immunology

KW - Glycosphingolipids/immunology

KW - Humans

KW - Lectins, C-Type/metabolism

KW - Receptors, Cell Surface/immunology

KW - Schistosoma mansoni/immunology

U2 - 10.1093/intimm/dxh246

DO - 10.1093/intimm/dxh246

M3 - Article

VL - 17

SP - 661

EP - 669

JO - International Immunology

JF - International Immunology

SN - 0953-8178

IS - 5

ER -