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* Department of Microbiology and Immunology, Indiana University School of Medicine and Walther Oncology Center, Indianapolis, IN 46202, and Walther Cancer Institute, Indianapolis, IN 46208;
Institute of Cancer Research, Fox Chase Cancer Center, Philadelphia, PA 19111; and
Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892
Mouse CD1d1 molecules present endogenous glycolipids to NKT cells.
Although glycolipid presentation requires CD1d1 transport through the
endocytic pathway, the processing requirements for such endogenous Ag
presentation by CD1d1 molecules are undefined. We examined CD1d1 Ag
presentation to NKT cells by disrupting endocytic trafficking and
function in cells expressing normal and mutated CD1d1 expressed by
recombinant vaccinia viruses. Consistent with previous studies, we
found that preventing CD1d1 localization to endosomes by altering its
cytoplasmic targeting sequences abrogated recognition by
V
14J281+ NKT cells without affecting recognition by
V14- NKT cells. Increasing the pH of acidic
compartments by incubating cells with chloroquine or bafilomycin A1
blocked CD1d1 recognition by V14+ (but not
V14-) NKT cells without reducing levels of cell surface
CD1d1. Similar results were obtained with primaquine, which interferes
with the recycling of cell surface glycoproteins. These results suggest
that the loading of a subset of glycolipid ligands onto CD1d1 molecules
entails the delivery of cell surface CD1d1 molecules and an acidic
environment in the endocytic pathway.
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