期刊
MOLECULAR IMMUNOLOGY
卷 46, 期 15, 页码 3157-3162出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.molimm.2009.07.001
关键词
Antigen presentation; Antigen processing; Peptide-receptive HLA-DR; HLA-DM; Peptide; Kinetics; Surface plasmon resonance; Diffusion; Superantigen; Viscosity
资金
- National Institutes of Health [R01 A1063764, R01 GM53549]
- United States Division of Defense
The peptide editor HLA-DM (DM) catalyzes the exchange of peptides bound to MHC class II molecules within antigen presenting cells by generating a peptide-receptive MHC class II conformation (MHCreceptive) to which peptides readily bind and rapidly unbind. While recent work has uncovered the determinants of DM recognition and effector functions, the nature of MHCreceptive and its interaction with DM remains unclear. Here, we show that DM induces but does not stabilize MHCreceptive in the absence of peptides. We demonstrate that DM is out-competed by certain superantigens, and increasing solvent viscosity inhibits DM-induced peptide association. We suggest that DM mediates peptide exchange by interacting transiently and repeatedly with MHC class II molecules, continually generating MHCreceptive. The simultaneous presence of peptide and DM in the milieu is thus crucial for the efficient generation of specific peptide-MHC class II complexes over time. (C) 2009 Elsevier Ltd. All rights reserved.
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