Isoaspartyl post-translational modification triggers anti-tumor T and B lymphocyte immunity

J Biol Chem. 2006 Oct 27;281(43):32676-83. doi: 10.1074/jbc.M604847200. Epub 2006 Sep 1.

Abstract

A hallmark of the immune system is the ability to ignore self-antigens. In attempts to bypass normal immune tolerance, a post-translational protein modification was introduced into self-antigens to break T and B cell tolerance. We demonstrate that immune tolerance is bypassed by immunization with a post-translationally modified melanoma antigen. In particular, the conversion of an aspartic acid to an isoaspartic acid within the melanoma antigen tyrosinase-related protein (TRP)-2 peptide-(181-188) makes the otherwise immunologically ignored TRP-2 antigen immunogenic. Tetramer analysis of iso-Asp TRP-2 peptide-immunized mice demonstrated that CD8+ T cells not only recognized the isoaspartyl TRP-2 peptide but also the native TRP-2 peptide. These CD8+ T cells functioned as cytotoxic T lymphocytes, as they effectively lysed TRP-2 peptide-pulsed targets both in vitro and in vivo. Potentially, post-translational protein modification can be utilized to trigger strong immune responses to either tumor proteins or potentially weakly immunogenic pathogens.

Publication types

  • Comparative Study
  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Antigens, Neoplasm / immunology
  • B-Lymphocytes / immunology*
  • CD8-Positive T-Lymphocytes / immunology
  • Cell Line, Tumor
  • In Vitro Techniques
  • Isoaspartic Acid / chemistry
  • Isoaspartic Acid / metabolism*
  • Melanoma, Experimental / immunology
  • Melanoma, Experimental / pathology
  • Mice
  • Mice, Inbred C57BL
  • Molecular Structure
  • Protein Processing, Post-Translational*
  • T-Lymphocytes / immunology*
  • Vaccination*

Substances

  • Antigens, Neoplasm
  • Isoaspartic Acid