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Allergenic proteins from Ligustrum vulgare (common privet) pollen are a group of plant proteins that elicit IgE-mediated allergic responses in sensitized individuals and are a recognized cause of respiratory allergies, particularly allergic rhinitis and asthma, worldwide[1][2][3][5]. The principal characterized allergen is Lig v 1, a member of the Ole e 1-like protein family, but several additional proteins (including profilin, enolase, ATP synthase subunits, and polygalacturonase) have been identified as potential allergens[2][4][6]. These proteins are found in privet pollen, which is prevalent in ornamental plantings and can provoke symptoms in sensitive people upon inhalation. Ligustrum pollen proteins are notable for cross-reactivity with other Oleaceae species such as olive, lilac, and ash, complicating both diagnosis and sensitization patterns[2][5]. While not classical therapeutic drug targets (hence "false" for is_target), they are medically important as the basis for diagnostic tests and emerging allergen-specific immunotherapies[2].
Not applicable for classical drugs; When used as immunotherapy (allergen-specific immunotherapy): exposure induces immune tolerance, reducing allergic symptoms; Mechanism for individual allergenic proteins: triggers IgE-mediated hypersensitivity
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