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. 1995 Jun 29;375(6534):802-6.
doi: 10.1038/375802a0.

Mediation by HLA-DM of dissociation of peptides from HLA-DR

V S Sloan  1 , P Cameron, G Porter, M Gammon, M Amaya, E Mellins, D M Zaller
Affiliations

Mediation by HLA-DM of dissociation of peptides from HLA-DR

V S Sloan et al. Nature. .

Abstract

Human leukocyte antigen (HLA)-DM is an unconventional major histocompatibility complex (MHC) class II heterodimer that is important for B-cell-mediated antigen processing and presentation to MHC class II-restricted T cells. HLA-DM is encoded by two genes, DMA and DMB, which map to the MHC class II region, and shares some homology with MHC class I and class II proteins. Here we define the biochemical role of HLA-DM. Recombinant soluble HLA-DM heterodimers have been purified from culture supernatants of insect cell transformants. At pH 5.0, they induce the dissociation of a subset of peptides bound to HLA-DR, including a nested set of class-II-associated invariant chain peptides (CLIP). This process liberates HLA-DR and leads to the enhanced binding of exogenous peptides.

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