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- W4313355013 abstract "Abstract We developed a minimalist cell-free antigen-processing system for MHC class II that can identify physiologically selected T cell epitopes from antigens. The system utilizes purified proteins: HLA-DR1, cathepsin B, H, S, and HLA-DM. It was designed to mimic the specialized compartment for antigen processing with known defined molecular composition so that it can be a useful tool for elucidating steps involved in antigen processing and understanding the mechanisms of epitope selection. We found that prior digestion of antigens even for a few minutes eliminated the possibility of their immunodominant epitope capture by DR1. However, if those antigens were captured by DR1 first in the presence of DM, dominant epitopes were successfully selected. We observed simultaneously binding of DR1 and DR4 to denatured proteins detected by the biacore method. In another case, pre-digestion of antigen did not destroy the dominant epitope even though it showed sensitivity to DM mediated dissociation. We saw that this epitope got selected because it was less susceptible to enzymatic digestions and it was able to rebind to DR1 even in the presence of DM. Therefore, In general, most peptides generated from proteins do not get a chance to bind MHC II for presentation because they are sensitive to both DM and enzymatic digestions. Selection of immunodominant epitope is the results of collaborative reactions of DR1, DM, and cathepsins by increasing abundance of epitope capture by MHC II." @default.
- W4313355013 created "2023-01-06" @default.
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- W4313355013 date "2013-05-01" @default.
- W4313355013 modified "2023-10-01" @default.
- W4313355013 title "Cooperative functions of MHC II, HLA-DM, and cathepsins enhance the selection of immunodominant epitopes (P5008)" @default.
- W4313355013 doi "https://doi.org/10.4049/jimmunol.190.supp.41.5" @default.
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