Artemisia vulgaris nonspecific lipid-transfer protein (Art v 3) (Art v 3)

Artemisia vulgaris nonspecific lipid-transfer protein (Art v 3) is a 12 kDa monomeric, non-glycosylated protein found predominantly in mugwort pollen, characterized by four alpha helices stabilized by four disulfide bridges, conferring high thermal and acid stability[2][1][3]. Art v 3 is a powerful allergen responsible for frequent sensitization and allergic reactions in humans, especially in areas with high mugwort pollen exposure. Sensitization is frequently associated with severe respiratory symptoms (asthma, rhinitis) and is a marker for cross-reactive nsLTP allergy syndromes, which include food allergies to fruits like peach (Pru p 3) and other plant foods, sometimes resulting in anaphylaxis[2][1][4]. Clinically, Art v 3 IgE sensitization is detected in allergic patients using blood tests or allergen chip arrays, and its relevance is established by direct challenge and immunological assays[2][1][3]. No approved pharmacological inhibitors exist for Art v 3; current management relies on allergen avoidance, symptomatic therapy, and potential allergen immunotherapy for desensitization[2][4].

Other names

Mugwort nonspecific lipid-transfer proteinMugwort LTPArtemisia vulgaris lipid-transfer proteinnsLTP mugwortAllergen Art v 3

Allergen immunotherapy: Desensitization via controlled exposure to Art v 3-containing extracts IgE-blocking: Downregulation or competitive inhibition of IgE antibody binding