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Can we prevent immunogenicity of human protein drugs?
  1. D W Scott1,
  2. A S De Groot2
  1. 1
    Departments of Surgery and of Microbiology and Immunology, and Center for Vascular and Inflammatory Diseases, University of Maryland School of Medicine, Baltimore, USA
  2. 2
    EpiVax, Inc, and University of Rhode Island, Providence, USA
  1. Correspondence to Dr D W Scott, Departments of Surgery, Microbiology and Immunology, University of Maryland School of Medicine, Center for Vascular and Inflammatory Diseases, 800 West Baltimore St, Baltimore, MD 21201, USA; davscott{at}som.umaryland.edu

Abstract

Monoclonal antibodies have proved to be extremely valuable additions to conventional treatment for rheumatic diseases. However, despite the general trend towards “humanisation”, these drugs remain immunogenic in clinical settings, baffling drug developers. In principle, humanised and fully human monoclonal antibodies are “self” immunoglobulins and should be tolerated. In this overview, the factors that may influence this process, the nature of immunogenicity and methods to analyse and modify potential immunogenicity are discussed. Finally, novel approaches to “re-induce” immunological tolerance to these proteins, including gene therapy and the recognition of unique regulatory epitopes, are outlined.

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Footnotes

  • Funding Research supported by grants from the NIH (RO1 HL061883, RO1 AI035622, RO1DK068343, R43HL08834 and from the Juvenile Diabetes Foundation.

  • Competing interests DWS is on the Scientific Advisory Board of EpiVax, Inc. ASDG is CEO and majority stockholder in EpiVax. This author acknowledges that there is a potential conflict of interest related to her relationship with EpiVax and attests that the work contained in this research report is free of any bias that might be associated with the commercial goals of the company.

  • Provenance and Peer review Not commissioned; externally peer reviewed.

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