Major Betulaceae PR-10 allergens (PR-10 allergens)

Major Betulaceae PR-10 allergens, with Bet v 1 as the prototypical member, are a group of proteins found in the pollen of trees in the Betulaceae family (e.g., birch, alder, hazel) that are responsible for triggering Type I hypersensitivity reactions (UniProt P15494) [1]. These proteins belong to the Pathogenesis-Related protein family 10 and possess a characteristic fold consisting of a seven-stranded antiparallel beta-sheet and three alpha-helices, forming a large internal cavity for ligand binding (PubMed: 18331744) [2]. In sensitized individuals, allergen-specific IgE antibodies recognize and bind to specific epitopes on these proteins, leading to the cross-linking of FcεRI receptors on mast cells and basophils and the subsequent release of inflammatory mediators (WHO/IUIS Allergen Nomenclature) [3]. This interaction is the primary driver of allergic rhinitis and can lead to pollen-food allergy syndrome due to the high structural homology between Bet v 1 and PR-10 proteins in various plant-derived foods like apples and hazelnuts (PubMed: 25210005) [4]. Therapeutic strategies focus on modulating the interaction between these allergens and allergen-specific IgE, either through allergen immunotherapy (AIT) to induce tolerance or through the use of monoclonal antibodies like Omalizumab that sequester IgE (FDA: Itulazax Label; DrugBank: DB00043) [5, 6].

Other names

Bet v 1-like proteinsBirch pollen allergensPathogenesis-related protein family 10Major birch allergenMajor Betulaceae PR-10 allergens binding allergen-specific IgE

Allergen immunotherapy (AIT) induces the production of allergen-specific IgG4 blocking antibodies that compete with IgE for binding to the PR-10 allergens, thereby preventing the activation of mast cells and basophils. Anti-IgE therapy (e.g., Omalizumab) binds to the Fc region of free IgE, preventing its interaction with the high-affinity IgE receptor (FcεRI) on effector cells.