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Biochemical Characterization of CD1d Expression in the Absence of β2-Microglobulin*

H. S. Kim,Jorge A. Garcia,M. Exley,Kevin W. Johnson,S. Balk,R. Blumberg

Published 1999 in Journal of Biological Chemistry

ABSTRACT

CD1d is a major histocompatibility complex class I-like molecule that exhibits a distinct antigen processing pathway that functions in the presentation of hydrophobic antigens to T cells. CD1d has been previously shown to be expressed on the cell surface of human intestinal epithelial cell lines in vivo and a transfected cell line in vitro independently of β2-microglobulin (β2m). To define the relationship between CD1d and β2m and characterize the biochemical structure of CD1d in the absence of β2m, we have used a newly generated series of CD1d transfectants and CD1d-specific antibodies. These studies show that in the absence of β2m, CD1d is expressed on the cell surface as a 45-kDa glycoprotein that is sensitive to endoglycosidase-H and is reduced to 37-kDa after N-glycanase digestion. In contrast, in the presence of β2m, CD1d is expressed on the cell surface as a 48-kDa endoglycosidase-H-resistant glycoprotein. Pulse-chase metabolic labeling studies demonstrate that acquisition of endoglycosidase-H resistance of CD1d is observed in the presence of β2m but not in the absence of β2m even after a 24-h chase period. Thus, CD1d is able to be transported to the cell surface independently of β2m; however, in the absence of β2m, the glycosylation pattern of CD1d is altered and consistent with an immature glycoprotein.

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