Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3

Tom A. Beardslee, Michael G Zeece, Gautam Sarath, John P. Markwell

Research output: Contribution to journalArticle

130 Citations (Scopus)

Abstract

Background: The identification of IgE epitopes for proteins is the first step in understanding the interaction of allergens with the immune system. Proteins from the legume family have shown in vitro cross-reactivity in IgE-binding assays, but this cross-reactivity is rarely clinically significant. Resolution of this discrepancy requires IgE epitope mapping of legume family protein allergens. Methods: We constructed six fusion proteins representing overlapping regions of soybean glycinin G1 acidic chain. These fusion proteins were used in immunoblotting and a novel sandwich ELISA with pooled sera from soy-allergic individuals to reveal a common IgE-binding region. This region was the focus for IgE epitope mapping using overlapping synthetic peptides. Results: Data from the fusion protein experiments revealed an IgE-binding region consisting of residues F192-I265. Analysis of the overlapping synthetic peptides to this region indicated that IgE epitopes to glycinin G1 acidic chain consist of residues G217-V235 and G253-I265. The epitopes identified for glycinin G1 acidic chain are homologous to IgE epitopes previously identified for the peanut allergen Ara h 3 [1]. However, residues identified by alanine scanning in the peanut epitopes as being important for IgE binding are different in the natural soybean epitopes. Conclusions: The IgE epitopes identified for glycinin G1 acidic chain apparently represent an allergenic region of several legume family seed storage proteins. Our findings indicate that the identification of IgE epitopes and structural analysis of legume family proteins will provide valuable information to the study of food allergies.

Original languageEnglish (US)
Pages (from-to)299-307
Number of pages9
JournalInternational Archives of Allergy and Immunology
Volume123
Issue number4
DOIs
StatePublished - Dec 1 2000

Fingerprint

Soybeans
Allergens
Immunoglobulin E
Epitopes
Fabaceae
Proteins
Epitope Mapping
Arachis
glycinin
Seed Storage Proteins
Peptides
Food Hypersensitivity
Immunoblotting
Alanine
Immune System
Enzyme-Linked Immunosorbent Assay

Keywords

  • ELISA
  • Epitope mapping
  • IgE
  • Peanut allergens
  • Soybean allergens

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Cite this

Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3. / Beardslee, Tom A.; Zeece, Michael G; Sarath, Gautam; Markwell, John P.

In: International Archives of Allergy and Immunology, Vol. 123, No. 4, 01.12.2000, p. 299-307.

Research output: Contribution to journalArticle

Beardslee, Tom A. ; Zeece, Michael G ; Sarath, Gautam ; Markwell, John P. / Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3. In: International Archives of Allergy and Immunology. 2000 ; Vol. 123, No. 4. pp. 299-307.
@article{2a4ddf3698cb48d2b5db8e9cc0d5a324,
title = "Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3",
abstract = "Background: The identification of IgE epitopes for proteins is the first step in understanding the interaction of allergens with the immune system. Proteins from the legume family have shown in vitro cross-reactivity in IgE-binding assays, but this cross-reactivity is rarely clinically significant. Resolution of this discrepancy requires IgE epitope mapping of legume family protein allergens. Methods: We constructed six fusion proteins representing overlapping regions of soybean glycinin G1 acidic chain. These fusion proteins were used in immunoblotting and a novel sandwich ELISA with pooled sera from soy-allergic individuals to reveal a common IgE-binding region. This region was the focus for IgE epitope mapping using overlapping synthetic peptides. Results: Data from the fusion protein experiments revealed an IgE-binding region consisting of residues F192-I265. Analysis of the overlapping synthetic peptides to this region indicated that IgE epitopes to glycinin G1 acidic chain consist of residues G217-V235 and G253-I265. The epitopes identified for glycinin G1 acidic chain are homologous to IgE epitopes previously identified for the peanut allergen Ara h 3 [1]. However, residues identified by alanine scanning in the peanut epitopes as being important for IgE binding are different in the natural soybean epitopes. Conclusions: The IgE epitopes identified for glycinin G1 acidic chain apparently represent an allergenic region of several legume family seed storage proteins. Our findings indicate that the identification of IgE epitopes and structural analysis of legume family proteins will provide valuable information to the study of food allergies.",
keywords = "ELISA, Epitope mapping, IgE, Peanut allergens, Soybean allergens",
author = "Beardslee, {Tom A.} and Zeece, {Michael G} and Gautam Sarath and Markwell, {John P.}",
year = "2000",
month = "12",
day = "1",
doi = "10.1159/000053642",
language = "English (US)",
volume = "123",
pages = "299--307",
journal = "International Archives of Allergy and Immunology",
issn = "1018-2438",
publisher = "S. Karger AG",
number = "4",

}

TY - JOUR

T1 - Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3

AU - Beardslee, Tom A.

AU - Zeece, Michael G

AU - Sarath, Gautam

AU - Markwell, John P.

PY - 2000/12/1

Y1 - 2000/12/1

N2 - Background: The identification of IgE epitopes for proteins is the first step in understanding the interaction of allergens with the immune system. Proteins from the legume family have shown in vitro cross-reactivity in IgE-binding assays, but this cross-reactivity is rarely clinically significant. Resolution of this discrepancy requires IgE epitope mapping of legume family protein allergens. Methods: We constructed six fusion proteins representing overlapping regions of soybean glycinin G1 acidic chain. These fusion proteins were used in immunoblotting and a novel sandwich ELISA with pooled sera from soy-allergic individuals to reveal a common IgE-binding region. This region was the focus for IgE epitope mapping using overlapping synthetic peptides. Results: Data from the fusion protein experiments revealed an IgE-binding region consisting of residues F192-I265. Analysis of the overlapping synthetic peptides to this region indicated that IgE epitopes to glycinin G1 acidic chain consist of residues G217-V235 and G253-I265. The epitopes identified for glycinin G1 acidic chain are homologous to IgE epitopes previously identified for the peanut allergen Ara h 3 [1]. However, residues identified by alanine scanning in the peanut epitopes as being important for IgE binding are different in the natural soybean epitopes. Conclusions: The IgE epitopes identified for glycinin G1 acidic chain apparently represent an allergenic region of several legume family seed storage proteins. Our findings indicate that the identification of IgE epitopes and structural analysis of legume family proteins will provide valuable information to the study of food allergies.

AB - Background: The identification of IgE epitopes for proteins is the first step in understanding the interaction of allergens with the immune system. Proteins from the legume family have shown in vitro cross-reactivity in IgE-binding assays, but this cross-reactivity is rarely clinically significant. Resolution of this discrepancy requires IgE epitope mapping of legume family protein allergens. Methods: We constructed six fusion proteins representing overlapping regions of soybean glycinin G1 acidic chain. These fusion proteins were used in immunoblotting and a novel sandwich ELISA with pooled sera from soy-allergic individuals to reveal a common IgE-binding region. This region was the focus for IgE epitope mapping using overlapping synthetic peptides. Results: Data from the fusion protein experiments revealed an IgE-binding region consisting of residues F192-I265. Analysis of the overlapping synthetic peptides to this region indicated that IgE epitopes to glycinin G1 acidic chain consist of residues G217-V235 and G253-I265. The epitopes identified for glycinin G1 acidic chain are homologous to IgE epitopes previously identified for the peanut allergen Ara h 3 [1]. However, residues identified by alanine scanning in the peanut epitopes as being important for IgE binding are different in the natural soybean epitopes. Conclusions: The IgE epitopes identified for glycinin G1 acidic chain apparently represent an allergenic region of several legume family seed storage proteins. Our findings indicate that the identification of IgE epitopes and structural analysis of legume family proteins will provide valuable information to the study of food allergies.

KW - ELISA

KW - Epitope mapping

KW - IgE

KW - Peanut allergens

KW - Soybean allergens

UR - http://www.scopus.com/inward/record.url?scp=0034501229&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034501229&partnerID=8YFLogxK

U2 - 10.1159/000053642

DO - 10.1159/000053642

M3 - Article

VL - 123

SP - 299

EP - 307

JO - International Archives of Allergy and Immunology

JF - International Archives of Allergy and Immunology

SN - 1018-2438

IS - 4

ER -