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J. Biol. Chem., Vol. 277, Issue 45, 42514-42522, November 8, 2002

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Chemical Identification of a Low Abundance Lysozyme Peptide Family Bound to I-A^k Histocompatibility Molecules^*

Carlos Velazquez^§, Ilan Vidavsky^¶, Koen van der Drift^¶, Michael L. Gross^¶, and Emil R. Unanue

From the  Department of Pathology and Immunology, Washington University School of Medicine and the ^¶ Department of Chemistry, Washington University, St. Louis, Missouri 63110

The processing by antigen-presenting cells (APC) of the protein hen egg-white lysozyme (HEL) results in the selection of a number of peptide families by the class II major histocompatibility complex (MHC) molecule, I-A^k. Some of these families are expressed in very small amounts, in the order of a few picomoles/10⁹ APC. We detected these peptides from an extract of class II MHC molecules by using monoclonal anti-peptide antibodies to capture the MHC-bound peptides prior to their examination by HPLC tandem mass spectrometry. Here, we have identified several members of a family of peptides encompassing residues 20-35, which represent less than 1% of the total HEL peptides. Binding analysis indicated that the core segment of the family was represented by residues 24-32 (SLGNWVCAA). Asn-27 (shown in boldface) is the main MHC-binding residue, mapped as interacting with the P4 pocket of the I-A^k molecule. Analysis of several T cell hybridomas indicated that three residues contacted the T cell receptor: Tyr-23 (P1), Leu-25 (P3), and Trp-28 (P5). The HEL peptides isolated from the APC extract were sulfated on Tyr-23, but further analysis showed that this modification did not occur physiologically but took place during the peptide isolation.

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