Anti‐IgE treatment: an update

Mapping of the CD23 Binding Site on Immunoglobulin E (IgE) and Allosteric Control of the IgE-FcϵRI Interaction

“…An anti-IgE antibody (omalizumab) is an effective therapy, currently used in the treatment of moderate to severe asthma that is not controlled by corticosteroids. Omalizumab binds to the Cϵ3 domain of IgE and competitively inhibits FcϵRI binding, although its in vivo activity relies on more than just inhibition of this interaction (32). Results presented here demonstrate that IgE is amenable to allosteric inhibition, an approach that may have significant advantages over competitive inhibition (33) and lay the foundation for the development of allosteric modulators of IgE-receptor interactions.…”

A high‐affinity monoclonal anti‐IgE antibody for depletion of IgE and IgE‐bearing cells

“…Immunoglobulin E is a universal target for the therapy of allergic diseases because of its fundamental role in the underlying pathomechanisms. Omalizumab (23, 24), a humanized monoclonal anti‐IgE antibody, which is repeatedly administered subcutaneously at intervals of 2–4 weeks, was the first drug for therapeutic targeting of IgE. Application of Omalizumab proved to induce a reversible, but significant reduction of IgE‐levels and improvement of clinical signs providing clear evidence for the effectiveness of IgE‐targeted therapy (17, 25).…”

The Immunoglobulin E receptor: Expression and regulation

“…By design, omalizumab is unable to bind surface-bound IgE because its epitope is buried within the IgE-Fcε RI complex. This prevents cross-linking and activation of FcεRI complexes by omalizumab and, to date, no significant reports of anaphylaxis have been observed with this therapy [33]. Clinically, omalizumab has been shown to be effective in reducing asthma exacerbations in patients with moderate to severe allergic asthma and allergic rhinitis [34,35••].…”