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Molecular Recognition of Human CD1b Antigen Complexes: Evidence for a Common Pattern of Interaction with ß TCRs¹

Agustín Melián^*, Gerald F. M. Watts^*, Abdijapar Shamshiev, Gennaro De Libero, Anne Clatworthy, Michael Vincent^*, Michael B. Brenner^*, Samuel Behar^*, Kayvan Niazi^§, Robert L. Modlin^§, Steven Almo^¶, David Ostrov^||, Stanley G. Nathenson^||,# and Steven A. Porcelli^2,3,*

^* Division of Rheumatology, Immunology, and Allergy, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02115; Department of Research, University Hospital Basel, Basel, Switzerland; Department of Molecular Biology, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02114; ^§ Division of Dermatology, Department of Medicine, University of California, Los Angeles Medical Center, Los Angeles, CA 90095; ^¶ Departments of Biochemistry, ^|| Cell Biology, and ^# Microbiology and Immunology, Albert Einstein College of Medicine of Yeshiva University, Bronx, NY 10461

Ag-specific T cell recognition is mediated through direct interaction of clonotypic TCRs with complexes formed between Ag-presenting molecules and their bound ligands. Although characterized in substantial detail for class I and class II MHC encoded molecules, the molecular interactions responsible for TCR recognition of the CD1 lipid and glycolipid Ag-presenting molecules are not yet well understood. Using a panel of epitope-specific Abs and site-specific mutants of the CD1b molecule, we showed that TCR interactions occur on the membrane distal aspects of the CD1b molecule over the 1 and 2 domain helices. The location of residues on CD1b important for this interaction suggested that TCRs bind in a diagonal orientation relative to the longitudinal axes of the helices. The data point to a model in which TCR interaction extends over the opening of the putative Ag-binding groove, making multiple direct contacts with both helices and bound Ag. Although reminiscent of TCR interaction with MHC class I, our data also pointed to significant differences between the TCR interactions with CD1 and MHC encoded Ag-presenting molecules, indicating that Ag receptor binding must be modified to accommodate the unique molecular structure of the CD1b molecule and the unusual Ags it presents.

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