Depletion of IgE-switched B cells may be an efficacious therapy for the treatment of allergic asthma. A humanized
monoclonal IgG1 antibody against the M1 prime segment of human membrane IgE on IgE-switched B cells can reduce
serum IgE by depleting IgE-producing cells. Here we report that removal of the core fucose in the Fc glycan of this
anti-M1 prime antibody increases its binding affinity for human FcγRIII receptors compared to the wildtype antibody. The
enhancement in binding to FcγRIII results in increased antibody potency for the in vitro depletion of IgE-positive cells in
antibody-dependent cell-mediated cytotoxicity assays and for the in vivo reduction of serum IgE in mice reconstituted
with human immune cells. This afucosylated anti-M1 prime antibody is known as quilizumab and is in clinical development
for the treatment of allergic asthma.
Keywords: ADCC, afucosylation, asthma, IgE, quilizumab.
Rights & PermissionsPrintExport