Deamidation of asparagine in a major histocompatibility complex-bound peptide affects T cell recognition but does not explain type B reactivity

J Exp Med. 2001 Oct 15;194(8):1165-70. doi: 10.1084/jem.194.8.1165.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antigen Presentation / immunology
  • Asparagine / immunology*
  • Aspartic Acid / immunology
  • Epitopes, T-Lymphocyte / immunology*
  • Isoaspartic Acid / immunology
  • Major Histocompatibility Complex / immunology*
  • Mice
  • Muramidase / immunology*
  • Peptide Fragments / immunology*
  • Peptides / immunology
  • T-Lymphocytes / immunology*
  • Tumor Cells, Cultured

Substances

  • Epitopes, T-Lymphocyte
  • Isoaspartic Acid
  • Peptide Fragments
  • Peptides
  • hen egg lysozyme peptide (48-61)
  • Aspartic Acid
  • Asparagine
  • Muramidase