Abstract
Class I major histocompatibility complex (MHC) molecules interact with a diverse array of self and foreign peptides, displaying them on the cell surface and providing an extracellular indication of intracellular invasion. The most clearly defined role for these class I/peptide complexes is to cause effector responses upon binding to antigen-specific receptors of cytotoxic T cells. We have characterized the mouse thymoma/rat Vβ8.2+ T-cell hybridoma C14/BW12-12A1 by fluorescence-activated cell sorting analysis and have used immunoaffinity chromatography to purify class I molecules from these cells. The peptides bound to the class I molecules were fractionated by high- performance liquid chromatography and sequenced. Self-peptide mixtures eluted from the mouse H-2K(k) class I allele revealed a dominant primary sequence motif, with a carboxyl-terminal residue that appeared to be invariantly valine and a secondary or auxiliary anchor residue at position 2 that could be either glutamate or proline. The majority of naturally processed peptide ligands appeared to be octamers. Although peptides eluted off H-2K(k) molecules from tissue derived from a number of different inbred mouse strains also appeared to be octamers, others have reported that isoleucine is the dominant carboxyl-terminal residue. Thus, different cell types displayed distinct differences in naturally processed peptides bound by the same class I alleles. The variation in naturally processed peptides loaded onto the same class I allele most likely reflects the nature of the pool of peptides within the cell available for loading class I molecules.
Original language | English (US) |
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Pages (from-to) | 803-811 |
Number of pages | 9 |
Journal | Journal of Neuroscience Research |
Volume | 45 |
Issue number | 6 |
DOIs | |
State | Published - Sep 15 1996 |
Keywords
- AKV virus
- H-2K(k)
- MHC class I
- autoimmune disease
- peptide-binding motif
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience