Author: Mishto, Michele
Title: What we see, what we do not see and what we do not want to see in HLA class I Immunopeptidomes. Cord-id: dzj2ysvx Document date: 2020_6_12
ID: dzj2ysvx
Snippet: The identification of peptides bound to HLA class I molecules - i.e. 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. They demonstrated that the choice of HLA-associated peptide enrichment and purification strategy
Document: The identification of peptides bound to HLA class I molecules - i.e. 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. They demonstrated that the choice of HLA-associated peptide enrichment and purification strategy affects peptide yields and creates a bias in detected sequence repertoire. The authors 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. This article is protected by copyright. All rights reserved.
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