Drug interference in immunogenicity assays depends on valency

J Pharm Biomed Anal. 2013 Nov:85:179-85. doi: 10.1016/j.jpba.2013.07.022. Epub 2013 Jul 30.

Abstract

Direct comparison of immunogenicity data is hampered by differential drug interference in different assay formats. In this paper we identify a drug-related factor that influences the extent of drug interference. We systematically investigated the influence of drug valency of different antibody-derived biologicals on the drug interference, using mono- and bivalent formats of adalimumab as a model system. Our results indicate that compared to regular bivalent antibodies, antibody-derived drugs that are monovalent result in less drug interference. Two real-life examples were examined: natalizumab, an IgG4 antibody that becomes effectively monovalent in vivo due to Fab arm exchange, and certolizumab pegol, a pegylated Fab fragment. For both drugs it was demonstrated that drug interference is less pronounced in an antigen-binding test compared to similar assays for other therapeutic antibodies. When comparing immunogenicity data obtained for different biologicals this phenomenon should be taken into account.

Keywords: ABT; ADA; Anti-drug antibody (ADA); Bispecific antibody; Certolizumab; Drug interference; GSH; Natalizumab; anti-drug antibody; antigen binding test; reduced glutathione.

MeSH terms

  • Adalimumab
  • Antibodies / immunology*
  • Antibodies, Monoclonal, Humanized / immunology*
  • Antibody Formation
  • Certolizumab Pegol
  • Humans
  • Immunoglobulin Fab Fragments / immunology*
  • Immunoglobulin G / immunology
  • Immunologic Techniques
  • Natalizumab
  • Polyethylene Glycols

Substances

  • Antibodies
  • Antibodies, Monoclonal, Humanized
  • Immunoglobulin Fab Fragments
  • Immunoglobulin G
  • Natalizumab
  • Polyethylene Glycols
  • Adalimumab
  • Certolizumab Pegol