Inefficient peptide binding by cell-surface class II MHC molecules

Cellular Immunology
M A ShermanP E Jensen

Abstract

The efficiency of peptide loading onto surface class II MHC molecules in intact APC was investigated, using a previously defined europium immunoassay as well as a simplified Western blot procedure. Conditions normally employed for peptide loading in T cell stimulation assays were suboptimal for peptide binding, which is enhanced at low pH, in the presence of protease inhibitors, and the absence of competing serum proteins. In contrast to some earlier reports, our results indicate that the rate of peptide loading by class II molecules is not enhanced in the environment of the plasma membrane. Peptide association rates were similar for purified and cell-surface class II molecules. As previously reported, rapid peptide binding can be achieved by reconstituting class II molecules into total cellular membranes. We report that this activity is due solely to HLA-DM (which is not present at the cell surface), since it can be specifically removed by immunodepletion with an anti-DM mAb. Thus, we find no evidence for additional cellular cofactors capable of catalyzing peptide binding to class II molecules.

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Citations

Dec 27, 2007·PloS One·Zuojia LiuErkang Wang
Dec 28, 1999·Proceedings of the National Academy of Sciences of the United States of America·L SantambrogioL J Stern
Dec 28, 1999·Proceedings of the National Academy of Sciences of the United States of America·L SantambrogioL J Stern
Sep 18, 2007·Molecular Immunology·Matthew N DaviesPaul J Travers
Dec 16, 2010·Tissue Antigens·Y JaimesC Figueiredo
Mar 9, 2000·Nature Cell Biology·J Davoust, J Banchereau
May 31, 2011·The Journal of Immunology : Official Journal of the American Association of Immunologists·Abdul Mohammad PezeshkiJacques Thibodeau
Dec 17, 2009·The Journal of Physical Chemistry. B·Zuojia LiuErkang Wang

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