Application of the 16-kDa buckwheat 2 S storage albumin protein for diagnosis of clinical reactivity

Soo Young Choi, Jung Ho Sohn, Yong Won Lee, Eun Kyung Lee, Chein Soo Hong, Jungwon Park

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Background: The 16-kDa protein of buckwheat (BW) has been implicated as a major allergen in BW allergy. Objective: To characterize the 16-kDa allergen and evaluate its clinical significance as an indicator of BW allergy. Methods: Complementary DNA from the 16-kDa allergen was cloned and expressed in Escherichia coli. Allergenicity was confirmed with IgE immunoblotting or with an enzyme-linked immunosorbent assay. The clinical utility of the recombinant protein (r16 kDa) for diagnosis of BW reactivity was evaluated in 18 BW-allergic and in 20 asymptomatic BW-sensitized subjects. Results: The 16-kDa allergen, composed of 127 amino acids, has 50% homology to the reported 8-kDa BW allergen, which belongs to the 2 S storage albumin. The r16-kDa protein can inhibit specific IgE (sIgE) antibody binding to the native BW 16-kDa allergen but minimally inhibited sIgE binding to crude BW extract. Approximately 77.8% of patients with the BW allergy produced sIgE antibodies to the r16-kDa protein, compared with a complete lack of reactivity in the 20 asymptomatic BW-sensitized subjects. The areas of the receiver operating characteristic curves for the skin prick test (mean, 0.93; 95% confidence interval, 0.85 to approximately 1.01; P < .001) and the r16-kDa enzyme-linked immunosorbent assay (mean, 0.93; 95% confidence interval, 0.84 to approximately 1.01; P < .001) were higher than the area of the BW IgE measurement curve determined by ImmunoCAP (a system for assaying serum IgE) (mean, 0.80; 95% confidence interval, 0.66 to approximately 0.94; P = .002). Conclusions: The 16-kDa allergen belongs to the 2 S storage albumin. Measurement of r16-kDa sIgE was more discriminating than measurement of ImmunoCAP sIgE in whole BW extracts for the diagnosis of clinical reactivity to BW.

Original languageEnglish
Pages (from-to)254-260
Number of pages7
JournalAnnals of Allergy, Asthma and Immunology
Volume99
Issue number3
DOIs
Publication statusPublished - 2007 Jan 1

Fingerprint

Fagopyrum
Albumins
Immunoglobulin E
Allergens
Proteins
Hypersensitivity
Confidence Intervals
Enzyme-Linked Immunosorbent Assay
Antibodies
Skin Tests
Complex Mixtures

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Immunology
  • Pulmonary and Respiratory Medicine

Cite this

Choi, Soo Young ; Sohn, Jung Ho ; Lee, Yong Won ; Lee, Eun Kyung ; Hong, Chein Soo ; Park, Jungwon. / Application of the 16-kDa buckwheat 2 S storage albumin protein for diagnosis of clinical reactivity. In: Annals of Allergy, Asthma and Immunology. 2007 ; Vol. 99, No. 3. pp. 254-260.
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abstract = "Background: The 16-kDa protein of buckwheat (BW) has been implicated as a major allergen in BW allergy. Objective: To characterize the 16-kDa allergen and evaluate its clinical significance as an indicator of BW allergy. Methods: Complementary DNA from the 16-kDa allergen was cloned and expressed in Escherichia coli. Allergenicity was confirmed with IgE immunoblotting or with an enzyme-linked immunosorbent assay. The clinical utility of the recombinant protein (r16 kDa) for diagnosis of BW reactivity was evaluated in 18 BW-allergic and in 20 asymptomatic BW-sensitized subjects. Results: The 16-kDa allergen, composed of 127 amino acids, has 50{\%} homology to the reported 8-kDa BW allergen, which belongs to the 2 S storage albumin. The r16-kDa protein can inhibit specific IgE (sIgE) antibody binding to the native BW 16-kDa allergen but minimally inhibited sIgE binding to crude BW extract. Approximately 77.8{\%} of patients with the BW allergy produced sIgE antibodies to the r16-kDa protein, compared with a complete lack of reactivity in the 20 asymptomatic BW-sensitized subjects. The areas of the receiver operating characteristic curves for the skin prick test (mean, 0.93; 95{\%} confidence interval, 0.85 to approximately 1.01; P < .001) and the r16-kDa enzyme-linked immunosorbent assay (mean, 0.93; 95{\%} confidence interval, 0.84 to approximately 1.01; P < .001) were higher than the area of the BW IgE measurement curve determined by ImmunoCAP (a system for assaying serum IgE) (mean, 0.80; 95{\%} confidence interval, 0.66 to approximately 0.94; P = .002). Conclusions: The 16-kDa allergen belongs to the 2 S storage albumin. Measurement of r16-kDa sIgE was more discriminating than measurement of ImmunoCAP sIgE in whole BW extracts for the diagnosis of clinical reactivity to BW.",
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Application of the 16-kDa buckwheat 2 S storage albumin protein for diagnosis of clinical reactivity. / Choi, Soo Young; Sohn, Jung Ho; Lee, Yong Won; Lee, Eun Kyung; Hong, Chein Soo; Park, Jungwon.

In: Annals of Allergy, Asthma and Immunology, Vol. 99, No. 3, 01.01.2007, p. 254-260.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Application of the 16-kDa buckwheat 2 S storage albumin protein for diagnosis of clinical reactivity

AU - Choi, Soo Young

AU - Sohn, Jung Ho

AU - Lee, Yong Won

AU - Lee, Eun Kyung

AU - Hong, Chein Soo

AU - Park, Jungwon

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N2 - Background: The 16-kDa protein of buckwheat (BW) has been implicated as a major allergen in BW allergy. Objective: To characterize the 16-kDa allergen and evaluate its clinical significance as an indicator of BW allergy. Methods: Complementary DNA from the 16-kDa allergen was cloned and expressed in Escherichia coli. Allergenicity was confirmed with IgE immunoblotting or with an enzyme-linked immunosorbent assay. The clinical utility of the recombinant protein (r16 kDa) for diagnosis of BW reactivity was evaluated in 18 BW-allergic and in 20 asymptomatic BW-sensitized subjects. Results: The 16-kDa allergen, composed of 127 amino acids, has 50% homology to the reported 8-kDa BW allergen, which belongs to the 2 S storage albumin. The r16-kDa protein can inhibit specific IgE (sIgE) antibody binding to the native BW 16-kDa allergen but minimally inhibited sIgE binding to crude BW extract. Approximately 77.8% of patients with the BW allergy produced sIgE antibodies to the r16-kDa protein, compared with a complete lack of reactivity in the 20 asymptomatic BW-sensitized subjects. The areas of the receiver operating characteristic curves for the skin prick test (mean, 0.93; 95% confidence interval, 0.85 to approximately 1.01; P < .001) and the r16-kDa enzyme-linked immunosorbent assay (mean, 0.93; 95% confidence interval, 0.84 to approximately 1.01; P < .001) were higher than the area of the BW IgE measurement curve determined by ImmunoCAP (a system for assaying serum IgE) (mean, 0.80; 95% confidence interval, 0.66 to approximately 0.94; P = .002). Conclusions: The 16-kDa allergen belongs to the 2 S storage albumin. Measurement of r16-kDa sIgE was more discriminating than measurement of ImmunoCAP sIgE in whole BW extracts for the diagnosis of clinical reactivity to BW.

AB - Background: The 16-kDa protein of buckwheat (BW) has been implicated as a major allergen in BW allergy. Objective: To characterize the 16-kDa allergen and evaluate its clinical significance as an indicator of BW allergy. Methods: Complementary DNA from the 16-kDa allergen was cloned and expressed in Escherichia coli. Allergenicity was confirmed with IgE immunoblotting or with an enzyme-linked immunosorbent assay. The clinical utility of the recombinant protein (r16 kDa) for diagnosis of BW reactivity was evaluated in 18 BW-allergic and in 20 asymptomatic BW-sensitized subjects. Results: The 16-kDa allergen, composed of 127 amino acids, has 50% homology to the reported 8-kDa BW allergen, which belongs to the 2 S storage albumin. The r16-kDa protein can inhibit specific IgE (sIgE) antibody binding to the native BW 16-kDa allergen but minimally inhibited sIgE binding to crude BW extract. Approximately 77.8% of patients with the BW allergy produced sIgE antibodies to the r16-kDa protein, compared with a complete lack of reactivity in the 20 asymptomatic BW-sensitized subjects. The areas of the receiver operating characteristic curves for the skin prick test (mean, 0.93; 95% confidence interval, 0.85 to approximately 1.01; P < .001) and the r16-kDa enzyme-linked immunosorbent assay (mean, 0.93; 95% confidence interval, 0.84 to approximately 1.01; P < .001) were higher than the area of the BW IgE measurement curve determined by ImmunoCAP (a system for assaying serum IgE) (mean, 0.80; 95% confidence interval, 0.66 to approximately 0.94; P = .002). Conclusions: The 16-kDa allergen belongs to the 2 S storage albumin. Measurement of r16-kDa sIgE was more discriminating than measurement of ImmunoCAP sIgE in whole BW extracts for the diagnosis of clinical reactivity to BW.

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