TY - JOUR
T1 - Isolation and characterization of the mountain cedar (Juniperus ashei) pollen major allergen, Jun a 1
AU - Midoro-Horiuti, Terumi
AU - Goldblum, Randall M.
AU - Kurosky, Alexander
AU - Goetz, David W.
AU - Brooks, Edward G.
PY - 1999
Y1 - 1999
N2 - 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 con-sistent with this proposition.
AB - 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 con-sistent with this proposition.
KW - Allergen
KW - Cha o 1
KW - Chamaecyparis obtusa
KW - Cry j 1
KW - Cryptomeria japonica
KW - Jun a 1
KW - Juniperus ashei
KW - Juniperus sabinoides
KW - Mountain cedar
KW - Pollinosis
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U2 - 10.1016/s0091-6749(99)70331-3
DO - 10.1016/s0091-6749(99)70331-3
M3 - Article
C2 - 10482835
AN - SCOPUS:0032842409
SN - 0091-6749
VL - 104
SP - 608
EP - 612
JO - Journal of Allergy and Clinical Immunology
JF - Journal of Allergy and Clinical Immunology
IS - 3 II
ER -