Proteomics

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Identification of HLA class I immunopeptide from human colon tissue (Normal)

ABSTRACT: HLA Class I immunopeptides were affinity purified by W6/32 antibody and analyzed by Orbitrap Fusion Lumos with FAIMS. Personalized database which includes patient-specific somatic mutations obtained from whole exome sequencing (WES) data was used for database search. Identification results were filtered at 1% FDR thresholds by searching against a randomized decoy database using Proteome Discoverer 2.4 (Sequest HT).

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Koji UEDA 

PROVIDER: PXD023804 | JPOST Repository | Sat Aug 20 00:00:00 BST 2022

REPOSITORIES: jPOST

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Dataset's files

Source:
Action DRS
200727_Lumos_FAIMS_CID_IT_CVSet1_1ul_51N.raw Raw
200727_Lumos_FAIMS_CID_IT_CVSet1_1ul_60N.raw Raw
200727_Lumos_FAIMS_CID_IT_CVSet1_1ul_78N.raw Raw
200727_Lumos_FAIMS_CID_IT_CVSet1_1ul_84N.raw Raw
200727_Lumos_FAIMS_CID_IT_CVSet1_5ul_51N.raw Raw
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Publications

Differential ion mobility mass spectrometry in immunopeptidomics identifies neoantigens carrying colorectal cancer driver mutations.

Minegishi Yuriko Y   Kiyotani Kazuma K   Nemoto Kensaku K   Inoue Yoshikage Y   Haga Yoshimi Y   Fujii Risa R   Saichi Naomi N   Nagayama Satoshi S   Ueda Koji K  

Communications biology 20220818 1

Understanding the properties of human leukocyte antigen (HLA) peptides (immunopeptides) is essential for precision cancer medicine, while the direct identification of immunopeptides from small biopsies of clinical tissues by mass spectrometry (MS) is still confronted with technical challenges. Here, to overcome these hindrances, high-field asymmetric waveform ion mobility spectrometry (FAIMS) is introduced to conduct differential ion mobility (DIM)-MS by seamless gas-phase fractionation optimal  ...[more]

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