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. 1990 Aug 10;62(3):563-7.
doi: 10.1016/0092-8674(90)90020-f.

Direct binding of peptide to empty MHC class I molecules on intact cells and in vitro

T N Schumacher  1 , M T Heemels, J J Neefjes, W M Kast, C J Melief, H L Ploegh
Affiliations

Direct binding of peptide to empty MHC class I molecules on intact cells and in vitro

T N Schumacher et al. Cell. .

Abstract

MHC class I molecules devoid of peptide are expressed on the cell surface of the mouse mutant lymphoma cell line RMA-S upon culture at reduced temperature. Empty class I molecules are thermolabile at the cell surface and in detergent lysates, but can be stabilized by the addition of presentable peptide; peptide binding appears to be a rapid process. Furthermore, class I molecules on the surface of RMA-S (H-2b haplotype) cells cultured at 26 degrees C can efficiently and specifically bind iodinated peptide presented by H-2Kb. Binding of iodinated peptide is also observed at a lower level for nonmutant cells (RMA) cultured at 26 degrees C. These experiments underscore the role for peptide in maintenance of the structure of class I molecules and, more importantly, provide two assay systems to study the interactions of peptides with MHC class I molecules independent of the availability of T cells that recognize a particular peptide-MHC class I complex.

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