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J Biol Chem, Vol. 274, Issue 14, 9289-9295, April 2, 1999

Biochemical Characterization of CD1d Expression in the Absence of beta 2-Microglobulin

Hyun Sil KimDagger , Jorge Garcia, Mark Exley, Kevin W. JohnsonDagger , Steven P. Balk, and Richard S. BlumbergDagger

From the Dagger  Division of Gastroenterology, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, and the  Division of Hematology/Oncology, Department of Medicine, Beth Israel-Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02215

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 beta 2-microglobulin (beta 2m). To define the relationship between CD1d and beta 2m and characterize the biochemical structure of CD1d in the absence of beta 2m, we have used a newly generated series of CD1d transfectants and CD1d-specific antibodies. These studies show that in the absence of beta 2m, 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 beta 2m, 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 beta 2m but not in the absence of beta 2m even after a 24-h chase period. Thus, CD1d is able to be transported to the cell surface independently of beta 2m; however, in the absence of beta 2m, the glycosylation pattern of CD1d is altered and consistent with an immature glycoprotein.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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