Deamidation of asparagine in a major histocompatibility complex-bound peptide affects T cell recognition but does not explain type B reactivity.
We have analyzed a panel of T cell hybridomas specific for the chemically dominant epitope of hen egg-white lysozyme 48-61 which has asparagine 59 as an important T cell receptor contact residue. A number of T cells recognize 48-61 with asparagine at position 59, but not the aspartic acid or isoaspartic acid derivatives. Conversely, we find T cells that specifically recognize 48-61 bearing an isoaspartic acid at residue 59, but not asparagine. For other T cells, asparagine, aspartic acid, or isoaspartic acid at residue 59 is irrelevant. We present evidence that our previous distinction between type A and type B T cells is not explained by asparagine deamidation at residue 59.
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Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA.
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D000818:Animals; D017951:Antigen Presentation / Q000276:immunology; D001216:Asparagine / Q000276:immunology*; D001224:Aspartic Acid / Q000276:immunology; D018984:Epitopes, T-Lymphocyte / Q000276:immunology*; D026581:Isoaspartic Acid / Q000276:immunology; D008285:Major Histocompatibility Complex / Q000276:immunology*; D051379:Mice; D009113:Muramidase / Q000276:immunology*; D010446:Peptide Fragments / Q000276:immunology*; D010455:Peptides / Q000276:immunology; D013601:T-Lymphocytes / Q000276:immunology*; D014407:Tumor Cells, Cultured
D018984:Epitopes, T-Lymphocyte; D026581:Isoaspartic Acid; D010446:Peptide Fragments; D010455:Peptides; C400524:hen egg lysozyme peptide (48-61); D001224:Aspartic Acid; D001216:Asparagine; D009113:Muramidase