Journal
JOURNAL OF IMMUNOLOGY
Volume 183, Issue 3, Pages 1884-1891Publisher
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.0900798
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Funding
- Chief Scientist Office [CZB/4/562] Funding Source: researchfish
- Versus Arthritis [18440] Funding Source: researchfish
- Arthritis Research UK [18440] Funding Source: Medline
- Versus Arthritis [18440] Funding Source: Medline
- Chief Scientist Office [CZB/4/562] Funding Source: Medline
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Exosomes are nanometer-sized vesicles released by a number of cell types including those of the immune system, and often contain numerous immune recognition molecules including MHC molecules. We demonstrate in this study that exosomes can display a significant proportion of their MHC class I (MHC I) content in the form of disulfide-linked MHC I dimers. These MHC I dimers can be detected after release from various cell lines, human monocyte-derived dendritic cells, and can also be found in human plasma. Exosome-associated dimers exhibit novel characteristics which include 1) being composed of folded MHC I, as detected by conformational-dependent Abs, and 2) dimers forming between two different MHC I alleles. We show that dimer formation is mediated through cysteine residues located in the cytoplasmic tail domains of many MHC I molecules, and is associated with a low level of glutathione in exosomes when compared with whole cell lysates. We propose these exosomal MHC I dimers as novel structures for recognition by immune receptors. The Journal of Immunology, 2009, 183: 1884-1891.
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