Identification of HLA class I-binding peptides derived from unique cancer-associated proteins by mass spectrometric analysis.

Abstract:

BACKGROUND/AIM:Since antigenic peptides of the cancer-associated antigens presented on human leukocyte antigen (HLA) molecules are recognized by specific cytotoxic T-lymphocytes, they have the potential to becoming effective peptide vaccines for cancer immunotherapy. MATERIALS AND METHODS:Peptides binding to HLA-A*0201 and HLA-A*2402 obtained from human prostate cancer cells by acid-elution were analyzed by liquid chromatography-tandem mass spectrometry (LC-MS/MS) and source proteins of the peptides were determined based on the HLA-binding capacity listed on the Syfpeithi. RESULTS:We identified TKLSA possibly derived from absent in melanoma 1-like protein (AIM1L), and RLRYT from trans-membrane protein-191C (TMEM 191C) or c20orf201. Messenger RNAs encoding these proteins were expressed in various cancer cell types but none or very few in non-cancerous tissues except for testis, cerebellum and ovary. CONCLUSION:HLA class I-binding peptides of unique cancer-associated proteins were identified by MS analysis, and might become a promising tool for the generation of novel cancer vaccines.

journal_name

Anticancer Res

journal_title

Anticancer research

authors

Kamata Y,Kuhara A,Iwamoto T,Hayashi K,Koido S,Kimura T,Egawa S,Homma S

subject

Has Abstract

pub_date

2013-05-01 00:00:00

pages

1853-9

issue

5

eissn

0250-7005

issn

1791-7530

pii

33/5/1853

journal_volume

33

pub_type

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