Typically, peptide receptive MHC-I multimer reagents are prepared in bacterial (E. coli) culture. While this is efficient, it does not result in glycosylation of the MHC-I peptide fragments as is done in mammalian cells. As a result, if such reagents are produced in mammalian cells, proper glycosylation would result and the reagents would have a potentially more accurate representation of the natural T-cell target.
This technology involves the coexpression of leucine zipper tagged single chain class I MHC molecules and the TAPBPR chaperone in mammalian cells to produce glycosylated MHC-I that are ready to accept an antigenic peptide of interest.
The expressed MHC-I can be purified from the supernatant, the leucine zippers removed through use of a specific protease (with a site engineered into the construct), multimerized, and contacted with the peptide of interest. In contrast with other technologies in this portfolio (e.g. 2018-408), no placeholder peptide is needed to create the peptide receptive MHC-I.
Peptide-receptive (empty) MHC-I reagents
MHC-I Multimer reagents
T Cell receptor discovery
T Cell epitope identification
Glycosylated MHC-I are more realistic
Efficient production of soluble MHC-I reagents from mammalian cells
MHC-I can be purified from supernatants
No need for placeholder peptide
|European Patent Office||Published Application||402841.2||07/20/2022||2020-251|
Additional Patents Pending
MHC-I, Glycosylated MHC-I, MHC-I multimer, Empty MHC-I, Peptide receptive MHC-I, Mammalian MHC-I, MHC-I tetramer, MHC-I reagent, TAPBPR, chaperone, MHC, Major Histocompatability Complex