Alloreactive monoclonal antibodies select K^d molecules with different peptide profiles

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• 作者：Noun ; Ghada ; Reboul ; Murielle ; Abastado ; Jean-Pierre ; Jaulin ; Christian ; Kourilsky ; Philippe ; et. al.
• 刊名：Human Immunology
• 出版年：6 -,
• 出版时间：April, 15 1996 -,
• 年：0
• 卷：47
• 期：1-2
• 页码：166
• 全文大小：95.0 K

文摘

As a part of our continuing effort to study the antigenic structure of class I molecules we have undertaken two types of studies. First, we have studied the capacity of five different K^d-reactive mAbs to recognize a panel of 25 site-directed mutants of the H-2K^d molecule. Both the gain and the decrease of antibody binding were found resulting from a single amino acid substitution at different positions. All mutations increasing the binding of the tested mAbs are located on the α-helices indicating that the replacement of an Ig-contacting surface residue with a charged or polar side chain by a short one generally favours antibody binding. The overwhelming majority of mutations which diminished antibody binding concerns residues buried within the antigen binding groove suggesting the possibility of peptide contribution to serologic epitopes defined by alloreactive antibodies. We have addressed this issue by the comparison of the repertoire of peptides eluted from K^d molecules precipitated by different K^d-reactive mAbs. The results reveal that alloreactive mAbs select K^d molecules with different peptide profiles. Thus we have shown that at least in some instances, changes induced in the MHC molecules by the binding of distinct peptides can be recognized as alterations in serologic determinants expressed on the class I molecules.