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

T. P. Cirrito, Z. Pu, M. B. Deck, E. R. Unanue

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

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.

Original languageEnglish
Pages (from-to)1165-1169
Number of pages5
JournalJournal of Experimental Medicine
Volume194
Issue number8
DOIs
StatePublished - Oct 15 2001

Keywords

  • Antigen presentation
  • Class II major histocompatibility molecules
  • Isoaspartate
  • Lysozyme
  • Posttranslational modification of peptides

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