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• W1570667313 startingPage "523" @default.
• W1570667313 abstract "Following biosynthesis, class II MHC molecules are transported through a lysosome-like compartment, where they acquire antigenic peptides for presentation to T cells at the cell surface. This compartment is characterized by the presence of HLA-DM, which catalyzes the peptide loading process. Here we report that the morphology and function of the class II loading compartment is affected in diseases with a phenotypic change in lysosome morphology. Swollen lysosomes are observed in cells from patients with the hereditary immunodeficiency Chediak-Higashi syndrome and in cells infected with Coxiella burnetii, the rickettsial organism that causes Q fever. In both disease states, we observed that HLA-DR and HLA-DM accumulate in enlarged intracellular compartments, which label with the lysosomal marker LAMP-1. The distribution of class I MHC molecules was not affected, localizing disease effects to the endocytic pathway. Thus, cellular mechanisms controlling lysosome biogenesis also affect formation of the class II loading compartment. Analysis of cell surface class II molecules revealed that their steady-state levels were not reduced on diseased cells. However, in both disease states, enhanced interaction between HLA-DR and HLA-DM was detected. In the Chediak-Higashi syndrome cells, this correlated with more efficient removal of the CLIP peptide. These findings suggest a mechanism for perturbation of Ag presentation by class II molecules and consequent immune deficiencies in both diseases." @default.
• W1570667313 created "2016-06-24" @default.
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• W1570667313 date "1999-01-01" @default.
• W1570667313 modified "2023-10-06" @default.
• W1570667313 title "Enhanced Interaction of HLA-DM with HLA-DR in Enlarged Vacuoles of Hereditary and Infectious Lysosomal Diseases" @default.
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• W1570667313 doi "https://doi.org/10.4049/jimmunol.162.1.523" @default.
• W1570667313 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9886429" @default.
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