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Artemisia annua allergen Art an 1 is the primary sensitizing protein found in the pollen of the annual mugwort plant, Artemisia annua. Structurally, it belongs to the defensin-like protein family and is characterized by a cysteine-rich N-terminal domain and a proline-rich C-terminal domain (UniProt: Q84ZX5). This molecule is a major trigger for Type I hypersensitivity reactions, contributing significantly to seasonal allergic rhinitis and asthma in sensitized individuals (PubMed: 25613331). In clinical practice, Art an 1 is utilized in component-resolved diagnosis to distinguish primary sensitization from cross-reactivity with other pollen allergens like Art v 1 from Artemisia vulgaris (PubMed: 28933105). As a therapeutic target, it is the focus of allergen-specific immunotherapy (AIT), where controlled exposure to the allergen aims to modulate the immune system from a Th2-mediated allergic response to a Th1/Treg-mediated tolerant state (PubMed: 30101519). Safety concerns primarily involve the risk of systemic allergic reactions or anaphylaxis during the administration of immunotherapy extracts. The protein's biological function in the plant is likely related to defense against pathogens, given its defensin-like structure. Understanding Art an 1 is crucial for developing standardized extracts for more effective and safer allergy treatments. It is often used as a marker for Artemisia annua pollen exposure in environmental monitoring. Research continues into recombinant versions of Art an 1 to improve the precision of immunotherapy.
Induction of immune tolerance through T-cell desensitization and the production of blocking antibodies such as IgG4
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