Characterization of Buckwheat 19-kD Allergen and Its Application for Diagnosing Clinical Reactivity
Background: The 19-kD protein of buckwheat (BW) has been suggested to be a major allergen, but its characteristics and clinical significance are poorly defined. Methods: cDNA of the 19-kD BW allergen was cloned and expressed in Escherichia coli. Allergenicity and cross-allergenicity were confirmed b...
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| Published in | International archives of allergy and immunology Vol. 144; no. 4; pp. 267 - 274 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Basel, Switzerland
Karger
01.01.2007
S. Karger AG |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1018-2438 1423-0097 1423-0097 |
| DOI | 10.1159/000106315 |
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| Abstract | Background: The 19-kD protein of buckwheat (BW) has been suggested to be a major allergen, but its characteristics and clinical significance are poorly defined. Methods: cDNA of the 19-kD BW allergen was cloned and expressed in Escherichia coli. Allergenicity and cross-allergenicity were confirmed by inhibition immunoblotting or by ELISA inhibition. The recombinant (r19-kD) protein was assessed for clinical utility in the diagnosis of BW reactivity in 18 BW-allergic and 19 BW-asymptomatic sensitized subjects using receiver operating characteristic analysis. Results: The 19-kD BW allergen, which is composed of 135 amino acids, has a weak homology to the vicilin-like allergens of cashew (Ana o 1), English walnut (Jug r 2) and 7 S globulin from Sesamum indicum. The r19-kD protein can inhibit sIgE binding to native 19-kD BW allergen. The maximum percentage inhibition of sIgE binding to crude BW extract was 56%. About 83.3% of the BW allergy patients had sIgE bound to r19-kD protein, compared to only 1 of the 19 BW-asymptomatic sensitized subjects. The areas under the receiver operating characteristic curves for the skin prick tests [0.925 (95% confidence interval: 0.839–1.012), p < 0.001] as well as r19-kD protein sIgE ELISAs [0.860 (95% confidence interval: 0.725–0.995), p <0.001] were higher than that of BW sIgE coated allergen particle test results [0.803 (95% confidence interval: 0.661–0.945), p = 0.002]. Conclusions: The 19-kD BW allergen may be the major allergen from BW. For the diagnosis of clinical reactivity to BW, the r19-kD protein sIgE ELISA test was more discriminative than the coated allergen particle sIgE measurement using whole BW extract. |
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| AbstractList | Background: The 19-kD protein of buckwheat (BW) has been suggested to be a major allergen, but its characteristics and clinical significance are poorly defined. Methods: cDNA of the 19-kD BW allergen was cloned and expressed in Escherichia coli. Allergenicity and cross-allergenicity were confirmed by inhibition immunoblotting or by ELISA inhibition. The recombinant (r19-kD) protein was assessed for clinical utility in the diagnosis of BW reactivity in 18 BW-allergic and 19 BW-asymptomatic sensitized subjects using receiver operating characteristic analysis. Results: The 19-kD BW allergen, which is composed of 135 amino acids, has a weak homology to the vicilin-like allergens of cashew (Ana o 1), English walnut (Jug r2) and 7 S globulin from Sesamum indicum. The r19-kD protein can inhibit slgE binding to native 19-kD BW allergen. The maximum percentage inhibition of slgE binding to crude BW extract was 56%. About 83.3% of the BW allergy patients had slgE bound to r19-kD protein, compared to only 1 of the 19 BW-asymptomatic sensitized subjects. The areas under the receiver operating characteristic curves for the skin prick tests [0.925 (95% confidence interval: 0.839-1.012), p < 0.001] as well as r19-kD protein slgE ELISAs [0.860 (95% confidence interval: 0.725-0.995), p < 0.001] were higher than that of BW slgE coated allergen particle test results [0.803 (95% confidence interval: 0.661-0.945), p = 0.002]. Conclusions: The 19-kD BW allergen may be the major allergen from BW. For the diagnosis of clinical reactivity to BW, the r19-kD protein slgE ELISA test was more discriminative than the coated allergen particle slgE measurement using whole BW extract. Background: The 19-kD protein of buckwheat (BW) has been suggested to be a major allergen, but its characteristics and clinical significance are poorly defined. Methods: cDNA of the 19-kD BW allergen was cloned and expressed in Escherichia coli. Allergenicity and cross-allergenicity were confirmed by inhibition immunoblotting or by ELISA inhibition. The recombinant (r19-kD) protein was assessed for clinical utility in the diagnosis of BW reactivity in 18 BW-allergic and 19 BW-asymptomatic sensitized subjects using receiver operating characteristic analysis. Results: The 19-kD BW allergen, which is composed of 135 amino acids, has a weak homology to the vicilin-like allergens of cashew (Ana o 1), English walnut (Jug r 2) and 7 S globulin from Sesamum indicum. The r19-kD protein can inhibit sIgE binding to native 19-kD BW allergen. The maximum percentage inhibition of sIgE binding to crude BW extract was 56%. About 83.3% of the BW allergy patients had sIgE bound to r19-kD protein, compared to only 1 of the 19 BW-asymptomatic sensitized subjects. The areas under the receiver operating characteristic curves for the skin prick tests [0.925 (95% confidence interval: 0.839–1.012), p < 0.001] as well as r19-kD protein sIgE ELISAs [0.860 (95% confidence interval: 0.725–0.995), p <0.001] were higher than that of BW sIgE coated allergen particle test results [0.803 (95% confidence interval: 0.661–0.945), p = 0.002]. Conclusions: The 19-kD BW allergen may be the major allergen from BW. For the diagnosis of clinical reactivity to BW, the r19-kD protein sIgE ELISA test was more discriminative than the coated allergen particle sIgE measurement using whole BW extract. Background: The 19-kD protein of buckwheat (BW) has been suggested to be a major allergen, but its characteristics and clinical significance are poorly defined. Methods: cDNA of the 19-kD BW allergen was cloned and expressed in Escherichia coli. Allergenicity and cross-allergenicity were confirmed by inhibition immunoblotting or by ELISA inhibition. The recombinant (r19-kD) protein was assessed for clinical utility in the diagnosis of BW reactivity in 18 BW-allergic and 19 BW-asymptomatic sensitized subjects using receiver operating characteristic analysis. Results: The 19-kD BW allergen, which is composed of 135 amino acids, has a weak homology to the vicilin-like allergens of cashew (Ana o 1), English walnut (Jug r 2) and 7 S globulin from Sesamum indicum. The r19-kD protein can inhibit sIgE binding to native 19-kD BW allergen. The maximum percentage inhibition of sIgE binding to crude BW extract was 56%. About 83.3% of the BW allergy patients had sIgE bound to r19-kD protein, compared to only 1 of the 19 BW-asymptomatic sensitized subjects. The areas under the receiver operating characteristic curves for the skin prick tests [0.925 (95% confidence interval: 0.839-1.012), p < 0.001] as well as r19-kD protein sIgE ELISAs [0.860 (95% confidence interval: 0.725-0.995), p <0.001] were higher than that of BW sIgE coated allergen particle test results [0.803 (95% confidence interval: 0.661-0.945), p = 0.002]. Conclusions: The 19-kD BW allergen may be the major allergen from BW. For the diagnosis of clinical reactivity to BW, the r19-kD protein sIgE ELISA test was more discriminative than the coated allergen particle sIgE measurement using whole BW extract. [PUBLICATION ABSTRACT] The 19-kD protein of buckwheat (BW) has been suggested to be a major allergen, but its characteristics and clinical significance are poorly defined.BACKGROUNDThe 19-kD protein of buckwheat (BW) has been suggested to be a major allergen, but its characteristics and clinical significance are poorly defined.cDNA of the 19-kD BW allergen was cloned and expressed in Escherichia coli. Allergenicity and cross-allergenicity were confirmed by inhibition immunoblotting or by ELISA inhibition. The recombinant (r19-kD) protein was assessed for clinical utility in the diagnosis of BW reactivity in 18 BW-allergic and 19 BW-asymptomatic sensitized subjects using receiver operating characteristic analysis.METHODScDNA of the 19-kD BW allergen was cloned and expressed in Escherichia coli. Allergenicity and cross-allergenicity were confirmed by inhibition immunoblotting or by ELISA inhibition. The recombinant (r19-kD) protein was assessed for clinical utility in the diagnosis of BW reactivity in 18 BW-allergic and 19 BW-asymptomatic sensitized subjects using receiver operating characteristic analysis.The 19-kD BW allergen, which is composed of 135 amino acids, has a weak homology to the vicilin-like allergens of cashew (Ana o 1), English walnut (Jug r 2) and 7 S globulin from Sesamum indicum. The r19-kD protein can inhibit sIgE binding to native 19-kD BW allergen. The maximum percentage inhibition of sIgE binding to crude BW extract was 56%. About 83.3% of the BW allergy patients had sIgE bound to r19-kD protein, compared to only 1 of the 19 BW-asymptomatic sensitized subjects. The areas under the receiver operating characteristic curves for the skin prick tests [0.925 (95% confidence interval: 0.839-1.012), p < 0.001] as well as r19-kD protein sIgE ELISAs [0.860 (95% confidence interval: 0.725-0.995), p <0.001] were higher than that of BW sIgE coated allergen particle test results [0.803 (95% confidence interval: 0.661-0.945), p = 0.002].RESULTSThe 19-kD BW allergen, which is composed of 135 amino acids, has a weak homology to the vicilin-like allergens of cashew (Ana o 1), English walnut (Jug r 2) and 7 S globulin from Sesamum indicum. The r19-kD protein can inhibit sIgE binding to native 19-kD BW allergen. The maximum percentage inhibition of sIgE binding to crude BW extract was 56%. About 83.3% of the BW allergy patients had sIgE bound to r19-kD protein, compared to only 1 of the 19 BW-asymptomatic sensitized subjects. The areas under the receiver operating characteristic curves for the skin prick tests [0.925 (95% confidence interval: 0.839-1.012), p < 0.001] as well as r19-kD protein sIgE ELISAs [0.860 (95% confidence interval: 0.725-0.995), p <0.001] were higher than that of BW sIgE coated allergen particle test results [0.803 (95% confidence interval: 0.661-0.945), p = 0.002].The 19-kD BW allergen may be the major allergen from BW. For the diagnosis of clinical reactivity to BW, the r19-kD protein sIgE ELISA test was more discriminative than the coated allergen particle sIgE measurement using whole BW extract.CONCLUSIONSThe 19-kD BW allergen may be the major allergen from BW. For the diagnosis of clinical reactivity to BW, the r19-kD protein sIgE ELISA test was more discriminative than the coated allergen particle sIgE measurement using whole BW extract. The 19-kD protein of buckwheat (BW) has been suggested to be a major allergen, but its characteristics and clinical significance are poorly defined. cDNA of the 19-kD BW allergen was cloned and expressed in Escherichia coli. Allergenicity and cross-allergenicity were confirmed by inhibition immunoblotting or by ELISA inhibition. The recombinant (r19-kD) protein was assessed for clinical utility in the diagnosis of BW reactivity in 18 BW-allergic and 19 BW-asymptomatic sensitized subjects using receiver operating characteristic analysis. The 19-kD BW allergen, which is composed of 135 amino acids, has a weak homology to the vicilin-like allergens of cashew (Ana o 1), English walnut (Jug r 2) and 7 S globulin from Sesamum indicum. The r19-kD protein can inhibit sIgE binding to native 19-kD BW allergen. The maximum percentage inhibition of sIgE binding to crude BW extract was 56%. About 83.3% of the BW allergy patients had sIgE bound to r19-kD protein, compared to only 1 of the 19 BW-asymptomatic sensitized subjects. The areas under the receiver operating characteristic curves for the skin prick tests [0.925 (95% confidence interval: 0.839-1.012), p < 0.001] as well as r19-kD protein sIgE ELISAs [0.860 (95% confidence interval: 0.725-0.995), p <0.001] were higher than that of BW sIgE coated allergen particle test results [0.803 (95% confidence interval: 0.661-0.945), p = 0.002]. The 19-kD BW allergen may be the major allergen from BW. For the diagnosis of clinical reactivity to BW, the r19-kD protein sIgE ELISA test was more discriminative than the coated allergen particle sIgE measurement using whole BW extract. |
| Author | Lee, Eun-Kyung Choi, Soo-Young Park, Jung-Won Sohn, Jung-Ho Hong, Chein-Soo Lee, Yong-Won |
| Author_xml | – sequence: 1 givenname: Soo-Young surname: Choi fullname: Choi, Soo-Young – sequence: 2 givenname: Jung-Ho surname: Sohn fullname: Sohn, Jung-Ho – sequence: 3 givenname: Yong-Won surname: Lee fullname: Lee, Yong-Won – sequence: 4 givenname: Eun-Kyung surname: Lee fullname: Lee, Eun-Kyung – sequence: 5 givenname: Chein-Soo surname: Hong fullname: Hong, Chein-Soo – sequence: 6 givenname: Jung-Won surname: Park fullname: Park, Jung-Won |
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| Keywords | Buckwheat allergen Major allergen Clinical reactivity 19-kD allergen Characterization Allergy Immunopathology Immunology Reactivity Buckwheat Diagnosis Allergen |
| Language | English |
| License | Copyright: All rights reserved. No part of this publication may be translated into other languages, reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording, microcopying, or by any information storage and retrieval system, without permission in writing from the publisher. https://www.karger.com/Services/SiteLicenses CC BY 4.0 Copyright 2007 S. Karger AG, Basel. |
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J Allergy Clin Immunol 1999;103:1005-1011.1035987810.1016%2FS0091-6749%2899%2970171-5 Sporik R, Hill D, Hosking C: Specificity of allergen skin testing in predicting positive open food challenges to milk, egg, and peanut in children. Clin Exp Allergy 2000;30:1540-1546.1106956110.1046%2Fj.1365-2222.2000.00928.x Hill D, Hosking C, Reyes-Benito L: Reducing the need for food allergen challenges in young children: a comparison of in vitro with in vivo tests. Clin Exp Allergy 2001;31:1031-1035.1146799310.1046%2Fj.1365-2222.2001.01113.x Yoshioka H, Ohmoto T, Urisu A, Mine Y, Adachi T: Expression and epitope analysis of the major allergenic protein Fag e 1 from buckwheat. J Plant Physiol 2004;161:761-767.1531006410.1016%2Fj.jplph.2004.01.010 Yoshimasu M, Zhang J, Hayakawa S, Mine Y: Electrophoretic and immunochemical characterization of allergenic proteins in buckwheat. Int Arch Allergy Immunol 2000;123:130-136.1106048410.1159%2F000024431 Vila L, Beyer K, Jarvinen K, Chatchatee P, Bardina L, Sampson H: Role of conformational and linear epitopes in the achievement of tolerance in cow's milk allergy. Clin Exp Allergy 2001;31:1599-1606.1167886110.1046%2Fj.1365-2222.2001.01218.x Park J, Kang D, Kim C, KO S, Yun Y, Kim K, et al: Identification and characterization of the major allergens of buckwheat. Allergy 2000;55:1035-1041.1109731310.1034%2Fj.1398-9995.2000.00763.x Davidson A, Passero M, Settipane G: Buckwheat-induced anaphylaxis: a case report. Ann Allergy 1992;69:439-440.1456486 Fujino K, Funatsuki H, Inada M, Shimono Y, Kikuta Y: Expression, cloning, and immunological analysis of buckwheat (Fagopyrum esculentum Moench) seed storage proteins. J Agric Food Chem 2001;49:1825-1829.1130833210.1021%2Fjf0011485 van Ree R: Clinical importance of cross-reactivity in food allergy. Curr Opin Allergy Clin Immunol 2004;4:235-240.1512694810.1097%2F00130832-200406000-00017 Vassilopoulou E, Rigby N, Moreno J, Zuidmeer L, Akkerdaas J, Tassios I, et al: Effect of in vitro gastric and duodenal digestion on the allergenicity of grape lipid transfer protein. J Allergy Clin Immunol 2006;118:473-480.1689077410.1016%2Fj.jaci.2006.04.057 Imai T, Iikura Y: The national survey of immediate type of food allergy. Arerugi 2003;52:1006-1013.14685046 Celik-Bilgili S, Mehl A, Verstege A, Staden U, Nocon M, Beyer K, et al: The predictive value of specific immunoglobulin E levels in serum for the outcome of oral food challenges. Clin Exp Allergy 2005;35:268-273.1578410210.1111%2Fj.1365-2222.2005.02150.x Kashima T, Fukui M, Masuda Y, Chaoe T: A case of acute death taking 'nyan-mien,' Korean buckwheat noodle. Nihon Hoigaku Zasshi 1961;15:391-394.14454135 Rance F, Abbal M, Lauwers-Cances V: Improved screening for peanut allergy by the combined use of skin prick tests and specific IgE assays. J Allergy Clin Immunol 2002;109:1027-1033.1206353610.1067%2Fmai.2002.124775 Akkerdaas J, Wensing M, Asero R, Rivas M, Knulst A, Bolhaar S, et al: IgE binding to pepsin-digested food extracts. Int Arch Allergy Immunol 2005;138:203-208.1620509810.1159%2F000088720 Yamada K, Urisu A, Katami M, Koyama H, Tokuda R, Wada E, et al: IgE-binding activity to enzyme-digested ovomucoid distinguishes between patients with contact urticaria to egg with and without overt symptoms on ingestion. Allergy 2000;55:565-569.1085898910.1034%2Fj.1398-9995.2000.00430.x Park S, Abe K, Kimura M, Urisu A, Yamasaki N: Primary structure and allergenic activity of trypsin inhibitors from the seeds of buckwheat (Fagopyrum esculentum Moench). 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| Snippet | Background: The 19-kD protein of buckwheat (BW) has been suggested to be a major allergen, but its characteristics and clinical significance are poorly... The 19-kD protein of buckwheat (BW) has been suggested to be a major allergen, but its characteristics and clinical significance are poorly defined. cDNA of... The 19-kD protein of buckwheat (BW) has been suggested to be a major allergen, but its characteristics and clinical significance are poorly... |
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| SubjectTerms | Adolescent Adult Allergens - adverse effects Allergens - genetics Allergens - immunology Allergies Amino Acid Sequence Anacardium Antigens, Plant - adverse effects Antigens, Plant - genetics Antigens, Plant - immunology Biological and medical sciences Child DNA, Complementary Double-Blind Method Escherichia coli Fagopyrum - chemistry Fagopyrum - immunology Female Food Hypersensitivity - diagnosis Food Hypersensitivity - immunology Fundamental and applied biological sciences. Psychology Fundamental immunology Grain Humans Immunoglobulin E - blood Immunoglobulin E - immunology Immunology Immunopathology Juglans Male Medical diagnosis Medical sciences Molecular Sequence Data Original Paper Plant Extracts - adverse effects Plant Extracts - immunology Plant Proteins - adverse effects Plant Proteins - genetics Plant Proteins - immunology Proteins Recombinant Proteins - immunology Sarcoidosis. Granulomatous diseases of unproved etiology. Connective tissue diseases. Elastic tissue diseases. Vasculitis Sesamum indicum Skin Tests |
| Title | Characterization of Buckwheat 19-kD Allergen and Its Application for Diagnosing Clinical Reactivity |
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