Journal
PROTEOMICS
Volume 21, Issue 7-8, Pages -Publisher
WILEY
DOI: 10.1002/pmic.202000176
Keywords
hybrid insulin peptides; immunopeptidomics; spliced peptides
Funding
- National Institutes of Health [DK120340]
Ask authors/readers for more resources
Proteasomal spliced peptides (PSPs) have been identified as novel neoantigens that can stimulate specific T cells in tumors. While some false positive PSPs arise from modified peptides, others may stem from data processing errors. The reported numbers of PSPs in the literature are likely inflated due to errors associated with data processing and analysis.
Proteasomal spliced peptides (PSPs) have been identified in the class I major histocompatibility complex (MHC) peptidomes of several tumors and have emerged as novel neoantigens that can stimulate highly specific T cells. Much debate has surrounded the percentage of PSPs in the immunopeptidome; reported numbers have ranged from <1-5% to 12-45%. Recently, our laboratory demonstrated in nonobese diabetic (NOD) mice that hybrid insulin peptides (HIPs), a special class of spliced peptides, are formed during insulin granule degradation in crinosomes of the pancreatic beta cells and that modified peptides comprised a significant source of false positive HIP assignments. Herein, this study is extended to crinosomes isolated from other mouse strains and to two recent MHC class I studies, to see if modified peptides explained discrepancies in reported percentages of PSPs. This analysis revealed that both MHC-I peptidomes contained many spectra erroneously assigned as PSPs. While many false positive PSPs did arise from modified peptides, others arose from probable data processing errors. Thus, the reported numbers of PSPs in the literature are likely elevated due to errors associated with data processing and analysis.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available