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J. Exp. Med.,
Volume 187, Number 2, January 19, 1998 245-251
By
From the * Howard Hughes Medical Institute and the Efficient loading of major histocompatibility complex class II molecules with peptides requires
the invariant chain (Ii) and the class II-like molecule H-2M. Recent in vitro biochemical studies suggest that H2-M may function as a chaperone to rescue empty class II dimers. To test this
hypothesis in vivo, we generated mice lacking both Ii and H-2M (Ii Department of Immunology, University of
Washington School of Medicine, Seattle, Washington 98195; and the § Department of Microbiology
and Immunology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232
/M/). Antigen presenting cells (APCs) from Ii/M/ mice, as compared with APCs from Ii/ mice, exhibit a
significant reduction in their ability to present self-peptides to a panel of class II I-Ab-restricted
T cells. As a consequence of this defect in the loading of self peptides, CD4+ thymocyte development is profoundly impaired in Ii/M/ mice, resulting in a peripheral CD4+ T cell population with low levels of T cell receptor expression. These findings are consistent with the
idea that H-2M functions as a chaperone in the peptide loading of class II molecules in vivo.
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