Glycobiology Advance Access published online on February 20, 2003
Glycobiology, doi:10.1093/glycob/cwg052
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© 2003 Oxford University Press
ORIGINAL ARTICLES
1 Department of Molecular Cell Biology, VU University Medical Center, van der Boechorststraat 7, 1081 BT Amsterdam, The Netherlands Schistosoma mansoni soluble egg antigens (SEA) are crucially involved in modulating the host immune response to infection by S. mansoni. We report here that human dendritic cells bind SEA through the C-type lectin DC-SIGN. Monoclonal antibodies against the carbohydrate antigens Gal Previous studies have shown that DC-SIGN binds HIV gp120 that contains high-mannose-type N-glycans. Site-directed mutagenesis within the carbohydrate recognition domain (CRD) of DC-SIGN demonstrates that amino acids E324 and E347 are involved in binding to HIV gp120, Lex and SEA. By contrast, mutation of amino acid Val351 abrogates binding to SEA and Lex, but not to HIV gp120. These data suggest that DC-SIGN recognizes these ligands through different, but overlapping regions within its CRD. Our data imply that DC-SIGN is not only a pathogen receptor for HIV gp120, but may also function in pathogen recognition by interaction with the carbohydrate antigens Lex and possibly LDNF, that are found on important human pathogens such as Schistosomes and the bacterium Helicobacter pylori.
Revised on January 28, 2003
Accepted on January 28, 2003
The dendritic cell specific C-type lectin DC-SIGN is a receptor for Schistosoma mansoni egg antigens and recognizes the glycan antigen Lewis-x
2 Department of Biochemistry and Molecular Biology, the Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA
3 Department of Medical Microbiology, VU University Medical Center, van der Boechorststraat 7, 1081 BT Amsterdam, The Netherlands
1-4(Fuc
1-3)GlcNAc (Lex) and GalNAc1-4(Fuc1-3)GlcNAc (LDNF) inhibit binding of DC-SIGN to SEA, suggesting that these glycan antigens may be crucially involved in binding. In a solid-phase adhesion assay DC-SIGN-Fc binds polyvalent neoglycoconjugates that contain Lex antigen, whereas no binding was observed to Gal1-4GlcNAc, and binding to neoglycoconjugates containing only -fucose or oligosaccharides with a terminal 1-2-linked fucose is low. These data indicate that binding of DC-SIGN to Lex antigen is fucose-dependent, and that adjacent monosaccharides and/or the anomeric linkage of the fucose are important for binding activity.
adhesion, glycosylation, schistosomiasis, dendritic cells, carbohydrate-interaction
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