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  • Title: Identification and immunologic characterization of an allergen, alliin lyase, from garlic (Allium sativum).
    Author: Kao SH, Hsu CH, Su SN, Hor WT, Chang T WH, Chow LP.
    Journal: J Allergy Clin Immunol; 2004 Jan; 113(1):161-8. PubMed ID: 14713923.
    Abstract:
    BACKGROUND: Garlic (Allium sativum) is one of the most common relishes used in cooking worldwide. Very few garlic allergens have been reported, and garlic allergy has been rarely studied. OBJECTIVE: The aim of the study was to identify allergenic proteins in garlic and to investigate their importance in allergies to other Allium species (leek, shallot, and onion). METHODS: A crude extract of garlic proteins was separated by SDS-PAGE and 2-dimensional electrophoresis; immunoblotting was then performed with the use of individual and pooled sera from patients with garlic allergy, and the major IgE-binding proteins were analyzed by amino acid sequencing and mass spectrometry. The putative allergens were further purified by chromatography; the antigenicity, allergenicity, and IgE-binding cross-reactivity of the purified protein were then studied by immunoblotting, periodate oxidation, skin tests, and IgE-binding inhibition assays. RESULTS: A major allergen, alliin lyase, was identified by mass spectrometry and Edman sequencing and purified to homogeneity through the use of a simple 2-step chromatographic method. Skin tests showed that the purified protein elicited IgE-mediated hypersensitive responses in patients with garlic allergy. Periodate oxidation showed that carbohydrate groups were involved in the antigenicity, allergenicity, and cross-reactivity. Garlic alliin lyase showed strong cross-reactivity with alliin lyases from other Allium species, namely leek, shallot, and onion. CONCLUSIONS: Alliin lyase was found to be a major garlic allergen in a garlic-allergic group of patients in Taiwan. The wide distribution of alliin lyase in Allium suggests it may be a new cross-reactive allergen.
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