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International Immunology Advance Access originally published online on March 31, 2005
International Immunology 2005 17(5):661-669; doi:10.1093/intimm/dxh246
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© The Japanese Society for Immunology. 2005. All rights reserved. For permissions, please e-mail: journals.permissions@oupjournals.org

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 Vliet1, Ellis van Liempt1,*, Eirikur Saeland1,*, Corlien A. Aarnoudse1, Ben Appelmelk2, Tatsuro Irimura3, Teunis B. H. Geijtenbeek1, Ola Blixt4, Richard Alvarez5, Irma van Die1 and Yvette van Kooyk1,6

1 Department of Molecular Cell Biology & Immunology and 2 Medical Microbiology, VU Medical Center, Amsterdam, the Netherlands
3 Department of Cancer Biology and Molecular Immunology, University of Tokyo, Tokyo, Japan
4 Core D, Consortium for Functional Glycomics, Scripps Research Institute, La Jolla, CA 92037, USA
5 Core H, Consortium for Functional Glycomics, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA
6 Present address: PO Box 7057, 1007 MB Amsterdam, The Netherlands

Correspondence to: Y. van Kooyk; E-mail: y.vankooyk{at}vumc.nl

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 ß-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: carbohydrate recognition profile, C-type lectins, GalNAc, glycan array

* These authors contributed equally to this work.

Transmitting editor: J. Borst


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