Deciphering the landscape of phosphorylated HLA-II ligands

iScience

Julien Racle¹  George Coukos¹  Michal Bassani-Sternberg²  David Gfeller²  Marthe Solleder²  Philippe Guillaume² 

[1] Swiss Institute of Bioinformatics (SIB), 1015 Lausanne, Switzerland;Department of Oncology, Ludwig Institute for Cancer Research, University of Lausanne, 1011 Lausanne, Switzerland;

关键词: Immunology;    Cell biology;    Omics;   

DOI  :  

来源: DOAJ

【 摘 要 】

Summary: 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. Here, we analyzed Mass Spectrometry HLA-II peptidomics data and identified 1,943 unique phosphorylated HLA-II ligands. This enabled us to precisely define phosphorylated binding motifs for more than 30 common HLA-II alleles and to explore various molecular properties of phosphorylated peptides. Our data were further used to develop the first predictor of phosphorylated peptide presentation on HLA-II molecules.

【 授权许可】

Unknown