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Binding by the Nonclassical Class I Molecule, Thymic Leukemia Antigen1
* Department of Pathology, School of Medicine and
Microchemical Facility, Emory University, Atlanta, GA 30322;
Division of Developmental Immunology, La Jolla Institute for Allergy and Immunology, San Diego, CA 92121; and
Laboratory of Immunobiology, Dana-Farber Cancer Institute, Boston, MA 02115
The nonclassical class I molecule, thymic leukemia (TL), has
been shown to be expressed on intestinal epithelial cells and to
interact with CD8+ intraepithelial T lymphocytes. We
generated recombinant soluble TL (T18d) H chains in
bacteria as inclusion bodies and refolded them with
2-microglobulin in the presence or absence of a random
peptide library. Using a mAb, HD168, that recognizes a conformational
epitope on native TL molecules, we observed that protein folds
efficiently in the absence of peptide. Circular dichroism analysis
demonstrated that TL molecules have structural features similar to
classical class I molecules. Moreover, thermal denaturation experiments
indicated that the melting temperature for peptide-free TL is similar
to values reported previously for conventional class I-peptide
complexes. Our results also show that CD8
binding is not
dependent on either TL-associated peptide or TL
glycosylation.
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