Abstract：
:Major Histocompatibility Complex (MHC) class II molecules, including Human Leukocyte Antigen (HLA)-DR, present peptide fragments from proteins degraded in the endocytic pathway. HLA-DR is targeted to late-endocytic structures named MHC class II-containing Compartments (MIIC), where it interacts with HLA-DM. This chaperone stabilizes HLA-DR during peptide exchange and is critical for successful peptide loading. To follow this process in living cells, we have generated cells containing HLA-DR3/Cyan Fluorescent Protein (CFP), HLA-DM/Yellow Fluorescent Protein (YFP), and invariant chain. HLA-DR/DM interactions were observed by Fluorescence Resonance Energy Transfer (FRET). These interactions were pH insensitive, yet occurred only in internal structures and not at the limiting membrane of MIIC. In a cellular model of infection, phagosomes formed a limiting membrane surrounding internalized Salmonella. HLA-DR and HLA-DM did not interact in Salmonella-induced vacuoles, and HLA-DR was not loaded with antigens. The absence of HLA-DR/DM interactions at the limiting membrane prevents local loading of MHC class II molecules in phagosomes. This may allow these bacteria to successfully evade the immune system.
journal_name
Immunityjournal_title
Immunityauthors
Zwart W,Griekspoor A,Kuijl C,Marsman M,van Rheenen J,Janssen H,Calafat J,van Ham M,Janssen L,van Lith M,Jalink K,Neefjes Jdoi
10.1016/j.immuni.2005.01.006keywords:
subject
Has Abstractpub_date
2005-02-01 00:00:00pages
221-33issue
2eissn
1074-7613issn
1097-4180pii
S1074-7613(05)00030-0journal_volume
22pub_type
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