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Originally published In Press as doi:10.1074/jbc.M207831200 on September 17, 2002

J. Biol. Chem., Vol. 277, Issue 47, 44838-44844, November 22, 2002
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Calnexin, Calreticulin, and ERp57 Cooperate in Disulfide Bond Formation in Human CD1d Heavy Chain*

Suk-Jo Kang and Peter CresswellDagger

From the Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06520-8011

Members of the CD1 family of membrane glycoproteins can present antigenic lipids to T lymphocytes. Like major histocompatibility complex class I molecules, they form a heterodimeric complex of a heavy chain and beta 2-microglobulin (beta 2m) in the endoplasmic reticulum (ER). Binding of lipid antigens, however, takes place in endosomal compartments, similar to class II molecules, and on the plasma membrane. Unlike major histocompatibility complex class I or CD1b molecules, which need beta 2m to exit the ER, CD1d can be expressed on the cell surface as either a free heavy chain or associated with beta 2m. These differences led us to investigate early events of CD1d biosynthesis and maturation and the role of ER chaperones in its assembly. Here we show that CD1d associates in the ER with both calnexin and calreticulin and with the thiol oxidoreductase ERp57 in a manner dependent on glucose trimming of its N-linked glycans. Complete disulfide bond formation in the CD1d heavy chain was substantially impaired if the chaperone interactions were blocked by the glucosidase inhibitors castanospermine or N-butyldeoxynojirimycin. The formation of at least one of the disulfide bonds in the CD1d heavy chain is coupled to its glucose trimming-dependent association with ERp57, calnexin, and calreticulin.


* This work was supported by the Howard Hughes Medical Institute and National Institutes of Health Grant AI23081.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 203-785-5176; Fax: 203-737-1764; E-mail: peter.cresswell@yale.edu.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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