The assembly of functional beta(2)-microglobulin-free MHC class I molecules that interact with peptides and CD8(+) T lymphocytes.

Schell TD, Mylin LM, Tevethia SS, Joyce S
Int Immunol. 2002 14 (7): 775-82

PMID: 12096037 · DOI:10.1093/intimm/dxf041

Functional MHC class I molecules are expressed on the cell surface in the absence of beta(2)-microglobulin (beta(2)m) 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 beta(2)m-free H-2D(b) assembles with short peptides that are approximately 9 amino acid residues in length, akin to ligands associated with completely assembled beta(2)m(+) H-2D(b). Remarkably, a subset of the peptides associated with the beta(2)m-free H-2D(b) has an altered anchor motif. However, they also include peptides that contain a beta(2)m(+)H-2D(b) binding anchor motif. Further, the H-2K(b)- and H-2D(b)-restricted peptide epitopes derived from SV-40 T antigen also assemble with H-2(b) class I in beta(2)m-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 beta(2)m with peptides and form CD8(+) T lymphocyte epitopes.

MeSH Terms (12)

Animals Antigen Presentation Antigens, Polyomavirus Transforming beta 2-Microglobulin CD8-Positive T-Lymphocytes Cell Line Epitopes, T-Lymphocyte H-2 Antigens Histocompatibility Antigens Class I Mice Peptides T-Lymphocytes, Cytotoxic

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