Low-affinity immunoglobulin epsilon Fc receptor (CD23) complexed with IgE and allergen (CD23–IgE–allergen complex)

The CD23–IgE–allergen complex is a multi-component molecular assembly formed on the surface of B lymphocytes, primarily involving the low-affinity IgE receptor (CD23, also known as FcεRII), IgE antibodies, and specific allergens (UniProt P06734). This complex plays a pivotal role in the allergic cascade by mediating IgE-facilitated antigen presentation (fAP), a process where B cells capture allergens via IgE-CD23 interactions and present them to T cells, thereby amplifying the allergic immune response (PubMed: 21831118). Additionally, the interaction between IgE and CD23 on B cells serves as a critical regulatory mechanism for IgE synthesis through both positive and negative feedback loops (PubMed: 11907458). In allergic diseases such as asthma and allergic rhinitis, this complex is central to the maintenance of high serum IgE levels and heightened sensitivity to environmental triggers. Therapeutic strategies targeting this complex include monoclonal antibodies like Omalizumab, which sequesters free IgE to prevent its binding to CD23, and Lumiliximab, an anti-CD23 antibody designed to inhibit B cell activation (PubChem CID: 16130400). By disrupting the formation or function of this complex, drugs can reduce the efficiency of allergen presentation and lower the overall production of IgE.

Other names

Fc epsilon receptor II complexCD23-IgE-antigen complexIgE-facilitated antigen presentation complexB-cell CD23-IgE-allergen assembly

Neutralization of IgE to prevent complex formation and inhibition of CD23-mediated antigen presentation to T cells.