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International Immunology, Vol. 15, No. 7, pp. 789-796, July 2003
© 2003 Japanese Society for Immunology

FEATURED ARTICLE OF THE MONTH

Specific depletion of autoreactive B lymphocytes by a recombinant fusion protein in vitro and in vivo

Marcel Zocher1,3, Patrick A. Baeuerle1, Torsten Dreier1 and Antonio Iglesias2,3

1 Micromet AG, 81477 Munich, Germany 2 Neuroimmunology Section, Max Planck Institute for Neurobiology, 82152 Martinsried, Germany 3 Present address: F. Hoffmann-LaRoche, Roche Center for Medical Genomics, PRGT, 4070 Basel, Switzerland

Correspondence to: P. A. Baeuerle; E-mail: patrick.baeuerle{at}micromet.de
Transmitting editor: T. Hünig

Antigen-specific B cells are key players in many autoimmune diseases through the production of autoreactive antibodies that can cause severe tissue damage and malfunction. We have designed and expressed a fusion protein, referred to as MOG–Fc, composed of the extracellular Ig-like domain of human myelin oligodendrocyte glycoprotein (MOG) and the CH2 and CH3 domains of the human IgG1 heavy chain. The dimerized fusion protein was capable of mediating cytotoxicity against a MOG-reactive hybridoma line in vitro. Likewise, MOG–Fc significantly reduced the number of circulating MOG-reactive B cells in an anti-MOG Ig heavy chain knock-in mouse model. Our study shows that autoantigen-reactive B lymphocytes can be efficiently and selectively eliminated by an autoantigen Fc{gamma}1 fusion protein in vitro as well as in vivo. Such fusion proteins may provide a platform for the development of highly selective therapeutic approaches.

Keywords: autoantibodies, autoimmunity, fusion protein, myelin oligodendrocyte glycoprotein


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