The antigenic identity of human class I MHC phosphopeptides is critically dependent upon phosphorylation status.

ABSTRACT: Dysregulated post-translational modification provides a source of altered self-antigens that can stimulate immune responses in autoimmunity, inflammation, and cancer. In recent years, phosphorylated peptides have emerged as a group of tumour-associated antigens presented by MHC molecules and recognised by T cells, and represent promising candidates for cancer immunotherapy. However, the impact of phosphorylation on the antigenic identity of phosphopeptide epitopes is unclear. Here we examined this by determining structures of MHC-bound phosphopeptides bearing canonical position 4-phosphorylations in the presence and absence of their phosphate moiety, and examining phosphopeptide recognition by the T cell receptor (TCR). Strikingly, two peptides exhibited major conformational changes upon p

SUBMITTER: Mohammed F 

PROVIDER: S-EPMC5589570 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature