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  • Title: Isolation and characterization of the mountain cedar (Juniperus ashei) pollen major allergen, Jun a 1.
    Author: Midoro-Horiuti T, Goldblum RM, Kurosky A, Goetz DW, Brooks EG.
    Journal: J Allergy Clin Immunol; 1999 Sep; 104(3 Pt 1):608-12. PubMed ID: 10482835.
    Abstract:
    BACKGROUND: Cedar pollens are important causes of seasonal allergic disease in diverse geographic areas. OBJECTIVE: A major allergen from mountain cedar (Juniperus ashei) pollen, termed Jun a 1, was isolated and characterized. METHODS: Water-soluble pollen glycoproteins were extracted, salt precipitated, and purified with use of concanavalin A affinity chromatography or HPLC. The purified fractions were characterized by SDS-PAGE, immunoblotting, and N-terminal amino acid sequence analysis. Binding of allergen-specific IgE from the sera of cedar-hypersensitive patients was detected by ELISA and antigen-specific responses of peripheral blood T cells by tritiated thymidine incorporation. RESULTS: The major extractable cedar pollen glycoprotein had a molecular weight and N-terminal amino acid sequence that was similar to that of the major allergen Cha o 1, from Japanese cypress (Chamaecyparis obtusa), and Cry j 1, from Japanese cedar (Cryptomeria japonica). IgE from cedar-hypersensitive patients' sera bound to the isolated glycoprotein. CONCLUSION: The predominance of Jun a 1 in the soluble proteins of mountain cedar pollen and its high degree of homology with Cha o 1 and Cry j 1 make it likely to be the major allergen of this pollen. Amino acid sequence conservation also makes Jun a 1 a potential target for cross-reactivity between these pollen allergens. The observed reactivity of IgE from the sera of Japanese cedar-sensitive patients with Jun a 1 is consistent with this proposition.
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