The causal role of immunoglobulin E (IgE) in triggering the cascade of bioc
hemical events leading to allergic disease is well established. Treatments
that selectively inhibit IgE activity are a logical approach in managing th
e allergic response. One such strategy utilizes rhuMAb-E25, a recombinant h
umanized IgG, monoclonal anti-IgE antibody, which binds to IgE. This anti-I
gE antibody binds at the same epitope site of IgE that binds to Fc epsilon
RI and is thus non-anaphylactogenic. By binding to IgE and removing it via
immune complex formation, the pool of IgE available to interact with mast c
ells and basophils is thereby reduced and the allergic response is attenuat
ed. The clinical safety and efficacy of rhuMAb-E25 demonstrated in phase II
studies of allergic asthma will be outlined. (C) 2000 Elsevier Science B.V
. All rights reserved.