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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.
- Source :
-
The Journal of experimental medicine [J Exp Med] 2001 Oct 15; Vol. 194 (8), pp. 1165-70. - Publication Year :
- 2001
-
Abstract
- 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.
- Subjects :
- Animals
Antigen Presentation immunology
Aspartic Acid immunology
Isoaspartic Acid immunology
Mice
Peptides immunology
Tumor Cells, Cultured
Asparagine immunology
Epitopes, T-Lymphocyte immunology
Major Histocompatibility Complex immunology
Muramidase immunology
Peptide Fragments immunology
T-Lymphocytes immunology
Subjects
Details
- Language :
- English
- ISSN :
- 0022-1007
- Volume :
- 194
- Issue :
- 8
- Database :
- MEDLINE
- Journal :
- The Journal of experimental medicine
- Publication Type :
- Academic Journal
- Accession number :
- 11602644
- Full Text :
- https://doi.org/10.1084/jem.194.8.1165