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Global proteogenomic analysis of human MHC I peptides derived from noncanonical reading frames

ABSTRACT: Using highthroughput mass spectrometry, we probed the sixreadingframe translation of human B cells’ transcriptome. We report that about 10% of MHC Iassociated peptides (MAPs) derive from noncanonical reading frames. These socalled cryptic MAPs originate from allegedly non- coding genomic sequences and from outofframe translation. Their biogenesis and properties differ in many ways from those of conventional MAPs. Thus, cryptic MAPs come from very short proteins with atypical Ctermini, and they are coded by transcripts bearing long UTRs selectively enriched in destabilizing elements. Cryptic MAPs increase the complexity of the immunopeptidome and represent an heretofore unexploited source of potential tumorspecific epitopes. In a more general context, the features of cryptic MAPs suggest that mRNA instability is instrumental in the biogenesis of MAPs. Associated RNA-seq accession: GSE67174 .

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): B Cell, Cell Culture

SUBMITTER: Olivier Caron-Lizotte

LAB HEAD: Olivier Caron-Lizotte

PROVIDER: PXD001898 | Pride | 2016-01-28

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	F189658_Subject3_fromMinOcc10OfSubject2.dat	Other
	F189658_Subject3_fromMinOcc10OfSubject2.dat-pride.pride.mgf.gz	Mgf
	F189658_Subject3_fromMinOcc10OfSubject2.dat-pride.pride.mztab.gz	Mztab
	F189658_Subject3_fromMinOcc10OfSubject2.dat-pride.xml.gz	Xml
	F189659_Subject4_fromMinOcc10OfSubject2.dat	Other

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Global proteogenomic analysis of human MHC I peptides derived from noncanonical reading frames

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