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- W2005504195 abstract "Abstract Peptide affinity for MHC molecules determines the number of MHC/peptide complexes stabilized at the cell surface in in vitro tests or in vaccination protocols. We isolated a high affinity monoclonal antibody specific for the HLA‐A2/Mage3 complex that enables an equilibrium binding assay to be performed on T2 cell line loaded with a range of Mage3 peptides. Binding of Mage3 to the HLA‐A2 molecule can be modeled by a standard receptor‐ligand interaction characterized by an affinity constant. This model enables the measurement of the affinity of other immunogenic peptides for HLA‐A2 by a competition test and the calculation of the density of complexes stabilized at the T2 cell surface for all peptide concentrations. Quantification of the HLA‐A2/Mage3 complexes at target cell surfaces was used to estimate the number of complexes required to reach cytotoxicity ED 50 of human T cell clones sorted from an unprimed repertoire. We confirm with this antibody the direct relationship between clone avidity and TCR affinity, and the moderate contribution of the CD8 co‐receptor in the reinforcement of TCR‐MHC/peptide contact. Nevertheless, CD8 plays a critical role in the amplification of the specific signal to establish an efficient T cell response at low specific complex densities found in physiological situations." @default.
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- W2005504195 date "2005-10-01" @default.
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- W2005504195 title "Assessment of CD8 involvement in T cell clone avidity by direct measurement of HLA-A2/Mage3 complex density using a high-affinity TCR like monoclonal antibody" @default.
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- W2005504195 doi "https://doi.org/10.1002/eji.200526307" @default.
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