The Optimization of Bioorthogonal Epitope Ligation within MHC-I ComplexesClick to copy article linkArticle link copied!
- Joanna B. Pawlak
- Brett J. Hos
- Michel J. van de Graaff
- Otty A. Megantari
- Nico Meeuwenoord
- Herman S. Overkleeft
- Dmitri V. Filippov
- Ferry Ossendorp
- Sander I. van Kasteren
Abstract
Antigen recognition followed by the activation of cytotoxic T-cells (CTLs) is a key step in adaptive immunity, resulting in clearance of viruses and cancers. The repertoire of peptides that have the ability to bind to the major histocompatibility type-I (MHC-I) is enormous, but the approaches available for studying the diversity of the peptide repertoire on a cell are limited. Here, we explore the use of bioorthogonal chemistry to quantify specific peptide–MHC-I complexes (pMHC-I) on cells. We show that modifying epitope peptides with bioorthogonal groups in surface accessible positions allows wild-type-like MHC-I binding and bioorthogonal ligation using fluorogenic chromophores in combination with a Cu(I)-catalyzed Huisgen cycloaddition reaction. We expect that this approach will make a powerful addition to the antigen presentation toolkit as for the first time it allows quantification of antigenic peptides for which no detection tools exist.
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