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N-linked glycosylation differentially affects the functional expression of the mouse CD1d1 glycoprotein

, : N-linked glycosylation differentially affects the functional expression of the mouse CD1d1 glycoprotein. FASEB Journal 18(4-5): Abst 82 6

The mouse CD1d1 glycoprotein is antigen-presenting molecule specialized in presenting lipid antigens to a distinct class of invariant T cells called NKT cells. Mouse CD1d1 is predicted to contain five potential N-linked glycosylation sites (asparagine residues at positions 25, 38, 60, 128 and 183). Because glycosylation invariably affects the molecular and functional properties of various glycoproteins, we analyzed the role of glycosylation on the mouse CD1d1 glycoprotein. Tunicamycin, an inhibitor of protein N-linked glycosylation was found to prevent the cell surface expression of mouse CD1d1. Site-directed mutagenesis that conservatively changed the individual endogenous asparagine residues to glutamic acid showed that glycosylation differentially affects the functional surface expression of CD1d1. Upon the stable transfection of cDNA encoding the wild type and mutant CD1d1 molecules into mouse fibroblasts, we found that all five glycosylation mutants of CD1 were detected on the cell surface but differed in their levels of expression. The cell surface levels of the N183Q mutant were decreased by ~35%, whereas the N38Q and N60Q mutants were expressed at two- to three-fold higher levels as compared to the wild type CD1d1 molecule. Not surprisingly, the ability of the CD1d1 glycosylation mutants to stimulate NKT cells correlated with their cell surface levels. Our results therefore suggest that glycosylation plays an important role in the functional expression of CD1d1.


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