MEDIATION BY HLA-DM OF DISSOCIATION OF PEPTIDES FROM HLA-DR

Citation
Vs. Sloan et al., MEDIATION BY HLA-DM OF DISSOCIATION OF PEPTIDES FROM HLA-DR, Nature, 375(6534), 1995, pp. 802-806
Citations number
30
Categorie Soggetti
Multidisciplinary Sciences
Journal title
NatureACNP
ISSN journal
00280836
Volume
375
Issue
6534
Year of publication
1995
Pages
802 - 806
Database
ISI
SICI code
0028-0836(1995)375:6534<802:MBHODO>2.0.ZU;2-Q
Abstract
HUMAN leukocyte antigen (HLA)-DM is an unconventional major histocompa tibility complex (MHC) class II heterodimer that is important for B-ce ll-mediated antigen processing and presentation to MHC class II-restri cted T cells(1-12). HLA-DM is encoded by two genes, DMA and DMB, which map to the MHC class II region(1), and shares some homology with MHC class I and class II proteins(2,3). Here we define the biochemical rol e of HLA-DM. Recombinant soluble HLA-DM heterodimers have been purifie d from culture supernatants of insect cell transformants. At pH 5.0, t hey induce the dissociation of a subset of peptides bound to HLA-DR, i ncluding a nested set of class-II-associated invariant chain peptides (CLIP). This process liberates HLA-DR and leads to the enhanced bindin g of exogenous peptides.