Journal
PROTEOMICS
Volume 20, Issue 15-16, Pages -Publisher
WILEY
DOI: 10.1002/pmic.202000112
Keywords
elution techniques; HLA class I immunopeptidome; mass spectrometry; peptide splicing; proteasomes
Funding
- National Institute for Health Research (NIHR) Biomedical Research Centre based at Guy's and St Thomas' NHS Foundation Trust
- King's College London
- NIHR Clinical Research Facility
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The identification of peptides bound to human leukocyte antigen class I (HLA-I) molecules-that is, the HLA-I immunopeptidome-is a useful tool in the hunt for epitopes suitable for vaccinations and immunotherapies. These peptides are mainly generated by proteasomes through peptide hydrolysis and peptide splicing. In this issue, Nicastri and colleagues compared different methods for the elution of HLA class I-associated peptides. It is demonstrated that the choice of HLA-associated peptide enrichment and purification strategy affects peptide yields and creates a bias in detected sequence repertoire. The author carried out this technical brief through the analysis of canonical non-spliced peptides. However, their study left out any analysis of post-translationally spliced peptides, thereby missing an opportunity to shed light on the persistent debate of the frequency of these unconventional peptides.
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