Abstract：
: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 (MHC(receptive)) to which peptides readily bind and rapidly unbind. While recent work has uncovered the determinants of DM recognition and effector functions, the nature of MHC(receptive) and its interaction with DM remains unclear. Here, we show that DM induces but does not stabilize MHC(receptive) 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 MHC(receptive). 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.
journal_name
Mol Immunoljournal_title
Molecular immunologyauthors
Narayan K,Su KW,Chou CL,Khoruzhenko S,Sadegh-Nasseri Sdoi
10.1016/j.molimm.2009.07.001subject
Has Abstractpub_date
2009-09-01 00:00:00pages
3157-62issue
15eissn
0161-5890issn
1872-9142pii
S0161-5890(09)00591-4journal_volume
46pub_type
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pub_type： 杂志文章
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pub_type： 杂志文章
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更新日期：1994-04-01 00:00:00
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pub_type： 杂志文章
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journal_title：Molecular immunology
pub_type： 杂志文章
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更新日期：2009-01-01 00:00:00
abstract：AIM:To study the role of complement receptor 1 (CR1) for binding of Escherichia coli (E. coli) to erythrocytes, for leukocyte phagocytosis, oxidative burst and complement activation in human whole blood from a CR1 deficient (CR1D) patient and healthy controls with low, medium and high CR1 numbers. METHODS:Alexa-labell...
journal_title：Molecular immunology
pub_type： 杂志文章
doi：10.1016/j.molimm.2019.07.014
更新日期：2019-10-01 00:00:00
