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Molecular Basis for the High Affinity Interaction between the Thymic Leukemia Antigen and the CD8 Molecule¹

Antoine Attinger^*, Lesley Devine, Yiran Wang-Zhu^*, Donald Martin^*, Jia-huai Wang, Ellis L. Reinherz, Mitchell Kronenberg^*, Hilde Cheroutre^* and Paula Kavathas^2,

^* La Jolla Institute for Allergy and Immunology, San Diego, CA 92121; Department of Laboratory Medicine and Section of Immunobiology, Yale University School of Medicine, New Haven, CT 06520; and Laboratory of Immunobiology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115

The mouse thymic leukemia (TL) Ag is a nonclassical MHC class I molecule that binds with higher affinity to CD8 than CD8. The interaction of CD8 with TL is important for lymphocyte regulation in the intestine. Therefore, we studied the molecular basis for TL Ag binding to CD8. The stronger affinity of the TL Ag for CD8 is largely mediated by three amino acids on exposed loops of the conserved ₃ domain. Mutant classical class I molecules substituted with TL Ag amino acids at these positions mimic the ability to interact with CD8 and modulate lymphocyte function. These data indicate that small changes in the ₃ domain of class I molecules potentially can have profound physiologic consequences.

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The JI 2005 174: 3135-3136. [Full Text]  

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