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Deciphering the landscape of phosphorylated HLA-II ligands
Published version of a preprint
Abstract
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.
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Metadata
- Authors
- Solleder, M., Racle, J., Guillaume, P., Coukos, G., Bassani-Sternberg, M., & Gfeller, D.
- Venue
- iScience
- Publisher
- Elsevier BV
- Published
- 2022-05
- Volume
- 25
- Issue
- 5
- Pages
- 104215
- ISSN
- 2589-0042
- Cited by
- 9
- References
- 49
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- creativecommons.org/licenses/by/4.0/ (vor)
- Funders
- Krebsliga Schweiz (KFS-4961-02-2020)
- European Molecular Biology Laboratory
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