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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 isoaspa...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2001
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2193507/ https://www.ncbi.nlm.nih.gov/pubmed/11602644 |
Sumario: | 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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