The assembly of functional β2-microglobulin-free MHC class I molecules that interact with peptides and CD8+ T lymphocytes

Todd D. Schell, Lawrence M. Mylin, Satvir S. Tevethia, Sebastian Joyce

Research output: Contribution to journalArticle

7 Scopus citations

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 languageEnglish (US)
Pages (from-to)775-782
Number of pages8
JournalInternational immunology
Volume14
Issue number7
StatePublished - Aug 7 2002

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Immunology

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