Increased diversity of the HLA-B40 ligandome by the presentation of peptides phosphorylated at their main anchor residue.

ABSTRACT: Human leukocyte antigen (HLA) class I molecules bind peptides derived from the intracellular degradation of endogenous proteins and present them to cytotoxic T lymphocytes, allowing the immune system to detect transformed or virally infected cells. It is known that HLA class I-associated peptides may harbor posttranslational modifications. In particular, phosphorylated ligands have raised much interest as potential targets for cancer immunotherapy. By combining affinity purification with high-resolution mass spectrometry, we identified more than 2000 unique ligands bound to HLA-B40. Sequence analysis revealed two major anchor motifs: aspartic or glutamic acid at peptide position 2 (P2) and methionine, phenylalanine, or aliphatic residues at the C terminus. The use of immobilized metal ion

SUBMITTER: Marcilla M 

PROVIDER: S-EPMC3916647 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature