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Identification of HLA class I-binding peptides derived from unique cancer-associated proteins by mass spectrometric
Yuko Kamata1, Akiko Kuhara, Takeo Iwamoto
1Department of Oncology, Institute of DNA Medicine, The Jikei University School of Medicine, 3-25-8 Nishi-shimbashi Minato-ku, Tokyo 105-8461 Japan. ykama@jikei.ac.jp
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.
