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 language | English |
|---|---|
| Pages (from-to) | 254-260 |
| Number of pages | 7 |
| Journal | Annals of Allergy, Asthma and Immunology |
| Volume | 99 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2007 Jan 1 |
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All Science Journal Classification (ASJC) codes
- Immunology and Allergy
- Immunology
- Pulmonary and Respiratory Medicine
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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 journal › Article
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
PY - 2007/1/1
Y1 - 2007/1/1
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.
UR - http://www.scopus.com/inward/record.url?scp=34548667894&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=34548667894&partnerID=8YFLogxK
U2 - 10.1016/S1081-1206(10)60661-8
DO - 10.1016/S1081-1206(10)60661-8
M3 - Article
C2 - 17910329
AN - SCOPUS:34548667894
VL - 99
SP - 254
EP - 260
JO - Annals of Allergy, Asthma and Immunology
JF - Annals of Allergy, Asthma and Immunology
SN - 1081-1206
IS - 3
ER -