Epitope Analysis of Murine and Chimeric Monoclonal Antibodies Recognizing the Cancer Testis Antigen PRAME

Dokl Biochem Biophys. 2020 May;492(1):135-138. doi: 10.1134/S1607672920030072. Epub 2020 Jul 6.

Abstract

We investigated the epitope specificity of different monoclonal antibodies recognizing the cancer testis antigen PRAME. Antibody 5D3 binds to the fragment of PRAME corresponding to 160-180 amino acid residues. Antibodies 6H8 and F11 bind to the fragment corresponding to 180-200 amino acid residues of PRAME. These antibodies retained the ability to recognize these PRAME fragments after chimerization.

Keywords: PRAME; cancer testis antigen; epitope analysis; monoclonal antibodies.

MeSH terms

  • Animals
  • Antibodies, Monoclonal / immunology*
  • Antigens, Neoplasm / immunology*
  • Antigens, Neoplasm / metabolism
  • Cells, Cultured
  • Cricetinae
  • Epitopes / chemistry
  • Epitopes / immunology*
  • Epitopes / metabolism
  • Humans
  • Male
  • Mice
  • Neoplasms / immunology*
  • Neoplasms / metabolism
  • Neoplasms / pathology
  • Testis / immunology*
  • Testis / metabolism

Substances

  • Antibodies, Monoclonal
  • Antigens, Neoplasm
  • Epitopes
  • PRAME protein, human