Therapeutic anti-IgE antibodies generate distinct functional immune complex signatures

Allergen-containing immune complexes formed by omalizumab or ligelizumab with IgE and IgG show distinct Fc receptor engagement signatures in primary human leukocytes, including composition-dependent functional shifts.

• Why it matters: Therapeutic anti-IgE antibodies are usually evaluated by blocking IgE–FcεRI binding, but how their IgE- and IgG-containing immune complexes behave on immune cells is not well defined.
• What they did: Primary human leukocytes were exposed to binary IgE–IgG and ternary allergen-containing immune complexes made with omalizumab or ligelizumab, and multiplexed focal molography mapped Fc receptor engagement across free versus complexed antibody states.
• The result: Cellular association and activation patterns depended on antibody identity and complex composition, and allergen incorporation reversed the relative IgE–FcεRI neutralization ability and remodeled FcγR binding for the two antibodies.

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