Genetic modification removes an immunodominant allergen from soybean

Eliot M Herman, Ricki M. Helm, Rudolf Jung, Anthony J. Kinney

Research output: Contribution to journalArticle

237 Citations (Scopus)

Abstract

The increasing use of soybean (Glycine max) products in processed foods poses a potential threat to soybean-sensitive food-allergic individuals. In vitro assays on soybean seed proteins with sera from soybean-sensitive individuals have immunoglobulin E reactivity to abundant storage proteins and a few less-abundant seed proteins. One of these low abundance proteins, Gly m Bd 30 K, also referred to as P34, is in fact a major (i.e. immunodominant) soybean allergen. Although a member of the papain protease superfamily, Gly m Bd 30 K has a glycine in the conserved catalytic cysteine position found in all other cysteine proteases. Transgene-induced gene silencing was used to prevent the accumulation of Gly m Bd 30 K protein in soybean seeds. The Gly m Bd 30 K-silenced plants and their seeds lacked any compositional, developmental, structural, or ultrastructural phenotypic differences when compared with control plants. Proteomic analysis of extracts from transgenic seed detected the suppression of Gly m Bd 30 K-related peptides but no other significant changes in polypeptide pattern. The lack of a collateral alteration of any other seed protein in the Gly m Bd 30 K-silenced seeds supports the presumption that the protein does not have a role in seed protein processing and maturation. These data provide evidence for substantial equivalence of composition of transgenic and non-transgenic seed eliminating one of the dominant allergens of soybean seeds.

Original languageEnglish (US)
Pages (from-to)36-43
Number of pages8
JournalPlant Physiology
Volume132
Issue number1
DOIs
StatePublished - May 1 2003
Externally publishedYes

Fingerprint

allergens
genetic engineering
Soybeans
Allergens
Seeds
soybeans
seeds
Soybean Proteins
Proteins
proteins
genetically modified organisms
immunoglobulin E
Food
Peptides
Papain
Cysteine Proteases
papain
cysteine proteinases
Gene Silencing
gene silencing

ASJC Scopus subject areas

  • Plant Science

Cite this

Genetic modification removes an immunodominant allergen from soybean. / Herman, Eliot M; Helm, Ricki M.; Jung, Rudolf; Kinney, Anthony J.

In: Plant Physiology, Vol. 132, No. 1, 01.05.2003, p. 36-43.

Research output: Contribution to journalArticle

Herman, Eliot M ; Helm, Ricki M. ; Jung, Rudolf ; Kinney, Anthony J. / Genetic modification removes an immunodominant allergen from soybean. In: Plant Physiology. 2003 ; Vol. 132, No. 1. pp. 36-43.
@article{7e3527daf9f44b65ae50b1fdb8be21a9,
title = "Genetic modification removes an immunodominant allergen from soybean",
abstract = "The increasing use of soybean (Glycine max) products in processed foods poses a potential threat to soybean-sensitive food-allergic individuals. In vitro assays on soybean seed proteins with sera from soybean-sensitive individuals have immunoglobulin E reactivity to abundant storage proteins and a few less-abundant seed proteins. One of these low abundance proteins, Gly m Bd 30 K, also referred to as P34, is in fact a major (i.e. immunodominant) soybean allergen. Although a member of the papain protease superfamily, Gly m Bd 30 K has a glycine in the conserved catalytic cysteine position found in all other cysteine proteases. Transgene-induced gene silencing was used to prevent the accumulation of Gly m Bd 30 K protein in soybean seeds. The Gly m Bd 30 K-silenced plants and their seeds lacked any compositional, developmental, structural, or ultrastructural phenotypic differences when compared with control plants. Proteomic analysis of extracts from transgenic seed detected the suppression of Gly m Bd 30 K-related peptides but no other significant changes in polypeptide pattern. The lack of a collateral alteration of any other seed protein in the Gly m Bd 30 K-silenced seeds supports the presumption that the protein does not have a role in seed protein processing and maturation. These data provide evidence for substantial equivalence of composition of transgenic and non-transgenic seed eliminating one of the dominant allergens of soybean seeds.",
author = "Herman, {Eliot M} and Helm, {Ricki M.} and Rudolf Jung and Kinney, {Anthony J.}",
year = "2003",
month = "5",
day = "1",
doi = "10.1104/pp.103.021865",
language = "English (US)",
volume = "132",
pages = "36--43",
journal = "Plant Physiology",
issn = "0032-0889",
publisher = "American Society of Plant Biologists",
number = "1",

}

TY - JOUR

T1 - Genetic modification removes an immunodominant allergen from soybean

AU - Herman, Eliot M

AU - Helm, Ricki M.

AU - Jung, Rudolf

AU - Kinney, Anthony J.

PY - 2003/5/1

Y1 - 2003/5/1

N2 - The increasing use of soybean (Glycine max) products in processed foods poses a potential threat to soybean-sensitive food-allergic individuals. In vitro assays on soybean seed proteins with sera from soybean-sensitive individuals have immunoglobulin E reactivity to abundant storage proteins and a few less-abundant seed proteins. One of these low abundance proteins, Gly m Bd 30 K, also referred to as P34, is in fact a major (i.e. immunodominant) soybean allergen. Although a member of the papain protease superfamily, Gly m Bd 30 K has a glycine in the conserved catalytic cysteine position found in all other cysteine proteases. Transgene-induced gene silencing was used to prevent the accumulation of Gly m Bd 30 K protein in soybean seeds. The Gly m Bd 30 K-silenced plants and their seeds lacked any compositional, developmental, structural, or ultrastructural phenotypic differences when compared with control plants. Proteomic analysis of extracts from transgenic seed detected the suppression of Gly m Bd 30 K-related peptides but no other significant changes in polypeptide pattern. The lack of a collateral alteration of any other seed protein in the Gly m Bd 30 K-silenced seeds supports the presumption that the protein does not have a role in seed protein processing and maturation. These data provide evidence for substantial equivalence of composition of transgenic and non-transgenic seed eliminating one of the dominant allergens of soybean seeds.

AB - The increasing use of soybean (Glycine max) products in processed foods poses a potential threat to soybean-sensitive food-allergic individuals. In vitro assays on soybean seed proteins with sera from soybean-sensitive individuals have immunoglobulin E reactivity to abundant storage proteins and a few less-abundant seed proteins. One of these low abundance proteins, Gly m Bd 30 K, also referred to as P34, is in fact a major (i.e. immunodominant) soybean allergen. Although a member of the papain protease superfamily, Gly m Bd 30 K has a glycine in the conserved catalytic cysteine position found in all other cysteine proteases. Transgene-induced gene silencing was used to prevent the accumulation of Gly m Bd 30 K protein in soybean seeds. The Gly m Bd 30 K-silenced plants and their seeds lacked any compositional, developmental, structural, or ultrastructural phenotypic differences when compared with control plants. Proteomic analysis of extracts from transgenic seed detected the suppression of Gly m Bd 30 K-related peptides but no other significant changes in polypeptide pattern. The lack of a collateral alteration of any other seed protein in the Gly m Bd 30 K-silenced seeds supports the presumption that the protein does not have a role in seed protein processing and maturation. These data provide evidence for substantial equivalence of composition of transgenic and non-transgenic seed eliminating one of the dominant allergens of soybean seeds.

UR - http://www.scopus.com/inward/record.url?scp=0038523728&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0038523728&partnerID=8YFLogxK

U2 - 10.1104/pp.103.021865

DO - 10.1104/pp.103.021865

M3 - Article

C2 - 12746509

AN - SCOPUS:0038523728

VL - 132

SP - 36

EP - 43

JO - Plant Physiology

JF - Plant Physiology

SN - 0032-0889

IS - 1

ER -