Fusing a protein to a stable portion of an antibody structure confers a longer circulating half-life to the protein, thus increasing its therapeutic benefits. The classic example is etanercept (Enbrel), a soluble p75-Fc dimer that blocks the action of TNF-a, the fusion being between p75, the TNF-a type II receptor (the TNF binding domain), and the Fc portion of human IgG (Mohler et al. 1993). More recently, we have collaborated with Zymogenetics on TACI-Ig. This is a fusion protein between the extracellular portion of the TACI receptor and the Fc portion ofhuman immunoglobulin G. Since this protein inhibits Blys (B lymphocyte stimulating factor), APRIL (a proliferation-inducing ligand) and heterotrimers, it might have greater clinical potential than an antibody (Dillon et al. 2006). It is currently in clinical studies for SLE, RA and hematological malignancies.
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