Selective release of some invariant chain-derived peptides from HLA-DR1 molecules at endosomal pH

doi:10.1084/jem.180.2.751

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Selective release of some invariant chain-derived peptides from HLA-DR1 molecules at endosomal pH

RG Urban, RM Chicz and JL Strominger
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.

The predominant peptides bound to major histocompatibility complex class II molecules expressed on human B cells are derived from a relatively limited number of self proteins. To determine whether any of the prebound self peptides might be released in endosomes during recycling, water-soluble HLA-DR1 molecules were incubated with a high affinity synthetic peptide at pH 4.0 and 7.0 at 37 degrees C. The resulting bound peptide repertoire was then acid extracted, and separated by reversed-phase high performance liquid chromatography. Using a combination of mass spectrometry and ultraviolet spectroscopy, prebound self peptides and newly bound synthetic peptide were characterized. Most self peptides bound to HLA-DR1 were not appreciably released during extended exposure to pH 4.0. However, some invariant chain-derived peptides were uniquely released at this pH.
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