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Peptide ligand-induced conformation and surface expression of the Ld class I MHC molecule

Abstract

NEWLY synthesized major histocompatibility complex (MHC) class I molecules in the endoplasmic reticulum are thought to bind peptides of foreign and endogenous antigens1–4. Several lines of evidence indicate that β-2 microglobulin (β2m) and/or peptide ligand participate in the intracellular transport and surface expression of class I molecules, but the nature of their involvement is still unclear5,6. Here we present evidence that culturing non-mutant cells (fibroblast, thymoma or mastocytoma) with a peptide ligand specific for the Ld class I molecule of the mouse leads to a dramatic (fourfold) and specific induction of Ld surface expression. Surprisingly, this peptide ligand-induced expression of Ld does not result in an increased intracellular association of Ld with β 2m. These findings demonstrate that the previously reported decrease in surface expression of Ld results from its failure to be saturated with endogenous self-peptide ligands. This unique feature of Ld could also contribute to the fact that several virus-specific cytotoxic ? cell responses have been found to be Ld-restricted.

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Lie, WR., Myers, N., Gorka, J. et al. Peptide ligand-induced conformation and surface expression of the Ld class I MHC molecule. Nature 344, 439–441 (1990). https://doi.org/10.1038/344439a0

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