Researchers identify phosphorylated binding motifs to train the first predictor for HLA-II – phosphorylated peptide interactions.
CD4+ T-cell activation in infectious diseases and cancer is governed by the recognition of peptides presented on class II human leukocyte antigen (HLA-II) molecules. Therefore, HLA-II ligands represent promising targets for vaccine design and personalized cancer immunotherapy. Much work has been done to identify and predict unmodified peptides presented on HLA-II molecules. However, little is known about the presentation of phosphorylated HLA-II ligands.
A paper* published in iScience, describes research led by David Gfeller (first author Marthe Solleder) whereby the analysis of Mass Spectrometry HLA-II peptidomics data resulted in identification of 1,943 unique phosphorylated HLA-II ligands. This allowed the precise definition of phosphorylated binding motifs for more than 30 common HLA-II alleles and to explore various molecular properties of phosphorylated peptides. The project’s data was further used to develop the first predictor of phosphorylated peptide presentation on HLA-II molecules.
*Deciphering the landscape of phosphorylated HLA-II ligands