Immunoglobulin E (IgE) complexed with Cryptomeria japonica allergens (Cry j 1 and Cry j 2) on Fc epsilon RI (IgE-Cryj-FcεRI complex)

The target represents the molecular complex formed when Japanese cedar pollen allergens, specifically Cry j 1 (a pectate lyase) and Cry j 2 (a polygalacturonase), bind to allergen-specific Immunoglobulin E (IgE) antibodies (Yasueda et al., 1983, J Allergy Clin Immunol). These IgE molecules are anchored to the high-affinity IgE receptor (Fc epsilon RI) located on the surface of effector cells such as mast cells and basophils (Galli et al., 2008, Nature). When multiple Cry j 1 or Cry j 2 epitopes cross-link these IgE-Fc epsilon RI complexes, it triggers a signaling cascade leading to the degranulation of the cells and the release of inflammatory mediators like histamine and leukotrienes (Galli et al., 2008, Nature). This process is the primary driver of Japanese cedar pollinosis, a prevalent form of allergic rhinitis in Japan (Okubo et al., 2020, Allergol Int). Therapeutic strategies targeting this complex include the use of anti-IgE monoclonal antibodies like omalizumab, which sequester free IgE to prevent its binding to the receptor, and allergen-specific immunotherapy (AIT), which uses standardized extracts to induce immunological tolerance (Normansell et al., 2014, Cochrane Database Syst Rev; Okubo et al., 2020, Allergol Int). Additionally, small molecule inhibitors targeting downstream signaling components, such as Spleen Tyrosine Kinase (SYK), are explored to prevent the cellular response following allergen binding (Riccaboni et al., 2010, Drug Discov Today).

Other names

Japanese cedar pollen allergen-IgE complexCry j 1-IgE-FcεRI complexCry j 2-IgE-FcεRI complexSensitized mast cell/basophil IgE complex

Inhibition of IgE-Fc epsilon RI binding, neutralization of free IgE, or induction of allergen-specific immune tolerance