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Direct Binding of the MHC Class I Molecule H-2L^d to CD8: Interaction with the Amino Terminus of a Mature Cell Surface Protein

Marie T. Jelonek^*, Brendan J. Classon, Peter J. Hudson and David H. Margulies^1,*

^* Molecular Biology Section, Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892; The Walter and Eliza Hall Institute of Medical Research, Victoria, Australia; and CSIRO Molecular Science, CRC for Diagnostic Technologies, Victoria, Australia

MHC class I molecules (MHC-I) display peptides from the intracellular pool at the cell surface for recognition by T lymphocytes bearing ß TCR. Although the activation of T cells is controlled by the interaction of the TCR with MHC/peptide complexes, the degree and extent of the activation is influenced by the binding in parallel of the CD8 coreceptor with MHC-I. In the course of quantitative evaluation of the binding of purified MHC-I to engineered CD8, we observed that peptide-deficient H-2L^d (MHC-I) molecules bound with moderate affinity (K_d = 7.96 x 10^-7 M), but in the presence of H-2L^d-binding peptides, no interaction was observed. Examination of the amino terminal sequences of CD8 and ß chains suggested that H-2L^d might bind these protein termini via its peptide binding cleft. Using both competition and real-time direct assays based on surface plasmon resonance, we detected binding of empty H-2L^d to synthetic peptides representing these termini. These results suggest that some MHC molecules are capable of binding the amino termini of intact cell surface proteins through their binding groove and provide alternative explanations for the observed binding of MHC molecules to a variety of cell surface receptors and coreceptors.

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