PMID: 9448031Feb 3, 1998Paper

An improved assembly assay for peptide binding to HLA-B*2705 and H-2K(k) class I MHC molecules

Journal of Immunological Methods
L TanJ S Haurum

Abstract

The assembly assay for peptide binding to class I major histocompatibility complex (MHC) is based on the ability to stabilise MHC class I molecules from mutant cell lines by the addition of suitable peptides. Such cell lines lack a functional transporter associated with antigen presentation (TAP) and as a result accumulate empty, unstable class I molecules in the ER. These dissociate rapidly in cell lysates unless they are stabilised by the addition of an appropriate binding peptide during lysis. The extent of stabilisation of class I molecules is directly related to the binding affinity of the added peptide. However, some MHC class I molecules, including HLA-B * 2705 and H-2Kk are unusually stable in their peptide-receptive state making them inappropriate for analysis using this assay or assays which depend on the ability of peptides to stabilise MHC class I molecules at the cell surface. Here we present an improved method that permits reliable measurements of peptide binding to such class I MHC molecules that are unusually stable in the absence of peptide. Cells are lysed in the presence of peptide and incubated at 4 degrees C. After 2 h, during which peptide binding to empty MHC molecules occurs, the lysate is heated to a te...Continue Reading

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Citations

Sep 17, 1999·Tissue Antigens·M H AndersenJ S Haurum
Mar 23, 2007·Annals of the New York Academy of Sciences·W W J UngerB O Roep
Sep 16, 2004·Blood·Mads Hald AndersenPer Thor Straten
Mar 10, 2001·The Journal of Immunology : Official Journal of the American Association of Immunologists·M RegnerA Müllbacher
Jan 6, 2001·The Journal of Immunology : Official Journal of the American Association of Immunologists·A W PurcellJ McCluskey
Aug 4, 2004·Cancer Research·Mads Hald AndersenJürgen C Becker

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