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The H4^b Minor Histocompatibility Antigen Is Caused by a Combination of Genetically Determined and Posttranslational Modifications¹

Rajwardhan Yadav^2,*, Yoshitaka Yoshimura^2,*, Alina Boesteanu, Gregory J. Christianson, Wilfred U. Ajayi^*, R. Shashidharamurthy^*, Aleksandar K. Stanic^*, Derry C. Roopenian and Sebastian Joyce^3,*

^* Department of Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, TN 37232; The Wistar Institute, Philadelphia, PA 19104; and The Jackson Laboratory, Bar Harbor, ME 04609

Minor histocompatibility (H) Ag disparities result in graft-vs-host disease and chronic solid allograft rejection in MHC-identical donor-recipient combinations. Minor H Ags are self protein-derived peptides presented by MHC class I molecules. Most arise as a consequence of allelic variation in the bound peptide (p) that results in TCR recognizing the p/MHC as foreign. We used a combinational peptide screening approach to identify the immune dominant H2K^b-restricted epitope defining the mouse H4^b minor H Ag. H4^b is a consequence of a P3 threonine to isoleucine change in the MHC-bound peptide derived from epithelial membrane protein-3. This allelic variation also leads to phosphorylation of the H4^b but not the H4^a epitope. Further, ex vivo CD8⁺ T lymphocytes bind phosphorylated Ag tetramers with high efficiency. Although we document the above process in the minor H Ag system, posttranslational modifications made possible by subtle amino acid changes could also contribute to immunogenicity and immune dominance in tumor immunotherapeutic settings.

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