Isolation and characterization of the mountain cedar (Juniperus ashei) pollen major allergen, Jun a 1

JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY

卷:104

Article

Midoro-Horiuti, T ; Goldblum, RM ; Kurosky, A ; Goetz, DW ; Brooks, EG

关键词: allergen;    Cha o 1;    Cry j 1;    Chamaecyparis obtusa;    Cryptomeria japonica;    Jun a 1;    Juniperus ashei;    Juniperus sabinoides;    mountain cedar;    pollinosis;   

DOI  :  10.1016/S0091-6749(99)70331-3

来源: Elsevier

【 摘 要 】

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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