Abstract
Functional MHC class I molecules are expressed on the cell surface in the absence of β2-microglobulin (β2m) light chain that can interact with CD8+ T lymphocytes. Whether their assembly requires peptide binding and whether their recognition by CD8+ T lymphocytes involves the presentation of peptide epitopes remains unknown. We show that β2m-free H-2Db assembles with short peptides that are ∼9 amino acid residues in length, akin to ligands associated with completely assembled β2m+ H-2Db. Remarkably, a subset of the peptides associated with the β2m-free H-2Db has an altered anchor motif. However, they also include peptides that contain a β2m+ H-2Db binding anchor motif. Further, the H-2Kb- and H-2Db-restricted peptide epitopes derived from SV-40 T antigen also assemble with H-2b class I in β2m-deficient cells and are recognized by epitope-specific CD8+ T lymphocytes. Taken together our data reveal that functional MHC class I molecules assemble in the absence of β2m with peptides and form CD8+ T lymphocyte epitopes.
Original language | English (US) |
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Pages (from-to) | 775-782 |
Number of pages | 8 |
Journal | International immunology |
Volume | 14 |
Issue number | 7 |
State | Published - 2002 |
All Science Journal Classification (ASJC) codes
- Immunology and Allergy
- Immunology