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

Terumi Midoro-Horiuti, R. M. Goldblum, A. Kurosky, D. W. Goetz, E. G. Brooks

Research output: Contribution to journalArticle

46 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)608-612
Number of pages5
JournalJournal of Allergy and Clinical Immunology
Volume104
Issue number3 I
DOIs
StatePublished - 1999

Fingerprint

Pollen
Allergens
Cryptomeria
Immunoglobulin E
Glycoproteins
Amino Acid Sequence
Chamaecyparis
Serum
Cupressus
Juniperus
Protein Sequence Analysis
Concanavalin A
Juniperus ashei jun a 1 protein
Affinity Chromatography
Immunoblotting
Thymidine
Polyacrylamide Gel Electrophoresis
Blood Cells
Salts
Molecular Weight

Keywords

  • Allergen
  • Cha o 1
  • Chamaecyparis obtusa
  • Cry j 1
  • Cryptomeria japonica
  • Jun a 1
  • Juniperus ashei
  • Juniperus sabinoides
  • Mountain cedar
  • Pollinosis

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Cite this

Isolation and characterization of the mountain cedar (Juniperus ashei) pollen major allergen, Jun a 1. / Midoro-Horiuti, Terumi; Goldblum, R. M.; Kurosky, A.; Goetz, D. W.; Brooks, E. G.

In: Journal of Allergy and Clinical Immunology, Vol. 104, No. 3 I, 1999, p. 608-612.

Research output: Contribution to journalArticle

Midoro-Horiuti, Terumi ; Goldblum, R. M. ; Kurosky, A. ; Goetz, D. W. ; Brooks, E. G. / Isolation and characterization of the mountain cedar (Juniperus ashei) pollen major allergen, Jun a 1. In: Journal of Allergy and Clinical Immunology. 1999 ; Vol. 104, No. 3 I. pp. 608-612.
@article{6e2496cd53d54b698ea8aadbc4ccea8d,
title = "Isolation and characterization of the mountain cedar (Juniperus ashei) pollen major allergen, Jun a 1",
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.",
keywords = "Allergen, Cha o 1, Chamaecyparis obtusa, Cry j 1, Cryptomeria japonica, Jun a 1, Juniperus ashei, Juniperus sabinoides, Mountain cedar, Pollinosis",
author = "Terumi Midoro-Horiuti and Goldblum, {R. M.} and A. Kurosky and Goetz, {D. W.} and Brooks, {E. G.}",
year = "1999",
doi = "10.1016/S0091-6749(99)70331-3",
language = "English (US)",
volume = "104",
pages = "608--612",
journal = "Journal of Allergy and Clinical Immunology",
issn = "0091-6749",
publisher = "Mosby Inc.",
number = "3 I",

}

TY - JOUR

T1 - Isolation and characterization of the mountain cedar (Juniperus ashei) pollen major allergen, Jun a 1

AU - Midoro-Horiuti, Terumi

AU - Goldblum, R. M.

AU - Kurosky, A.

AU - Goetz, D. W.

AU - Brooks, E. 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 consistent 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 consistent 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

UR - http://www.scopus.com/inward/record.url?scp=0032842409&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032842409&partnerID=8YFLogxK

U2 - 10.1016/S0091-6749(99)70331-3

DO - 10.1016/S0091-6749(99)70331-3

M3 - Article

C2 - 10482835

AN - SCOPUS:0032842409

VL - 104

SP - 608

EP - 612

JO - Journal of Allergy and Clinical Immunology

JF - Journal of Allergy and Clinical Immunology

SN - 0091-6749

IS - 3 I

ER -