The Journal of Experimental Medicine
Cytokines Montreal 2008
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Published 15 October 2001. doi:10.1084/jem.194.8.1165
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© The Rockefeller University Press, 0022-1007/2001/10/1165/ $5.00
The Journal of Experimental Medicine, Volume 194, Number 8, October 15, 2001 1165-1170


Brief Definitive Report

Deamidation of Asparagine in a Major Histocompatibility Complex–bound Peptide Affects T Cell Recognition but Does Not Explain Type B Reactivity

Thomas P. Cirritoa, Zheng Pua, M. Brian Decka, and Emil R. Unanuea
a Department of Pathology and Immunology, and Center for Immunology, Washington University School of Medicine, St. Louis, MO 63110

Correspondence to: Emil R. Unanue, Department of Pathology and Immunology, Washington University School of Medicine, St. Louis MO 63110. Tel:314-362-7440 Fax:314-362-4096 E-mail:unanue{at}pathbox.wustl.edu.

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.

Key Words: class II major histocompatibility molecules, posttranslational modification of peptides, lysozyme, antigen presentation, isoaspartate


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