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CUTTING EDGE |
,§
*
Department of Microbiology and Beirne B. Carter Center for Immunology Research, University of Virginia, Charlottesville, VA 22908;
Department of Chemistry, University of Virginia, Charlottesville, VA 22901;
Department of Immunohematology and Bloodbank, Leiden University Medical Center, Leiden, The Netherlands; and
§
Department of Pathology, University of Virginia, Charlottesville, VA 22908
In this report, we describe the use of novel mass spectrometry instrumentation to identify a male-specific minor histocompatibility Ag restricted by HLA-A*0101 (A1-HY). This Ag has the sequence IVDC*LTEMY, where C* represents a cysteine disulfide bonded to a second cysteine residue. The core peptide sequence is found in the protein product of DFFRY, a Y chromosome gene not previously identified as the source of an HY Ag. The male-specific form of the peptide differs from its X chromosomal counterpart by the substitution of serine for the C* residue. Both peptides are expressed on the cell surface at 30 or fewer copies per cell. However, A1-HY-specific CTL recognize the DFFRY-derived peptide at a 1500-fold lower dose than the female homologue. Thus, these studies have identified a new source of HY epitopes and provide additional information about the influence of posttranslational modifications of class I-associated peptides on T cell recognition.
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