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

Anticancer Res. 2013 May;33(5):1853-9.

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.

Keywords: HLA class-I; antigenic peptide; cancer associated antigen; mass spectrometric analysis; prostate cancer.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biomarkers, Tumor / metabolism*
  • Chromatography, Liquid
  • Histocompatibility Antigens Class I / immunology
  • Histocompatibility Antigens Class I / metabolism*
  • Humans
  • Neoplasms / immunology
  • Neoplasms / metabolism*
  • Peptide Fragments / immunology
  • Peptide Fragments / metabolism*
  • Spectrometry, Mass, Electrospray Ionization*
  • Tandem Mass Spectrometry*
  • Tumor Cells, Cultured

Substances

  • Biomarkers, Tumor
  • Histocompatibility Antigens Class I
  • Peptide Fragments