A 50 kDa maize γ-zein has marked cross-reactivity with the almond major protein

Sung Ho Lee, Mustapha Benmoussa, Shridhar K. Sathe, Kenneth H. Roux, Suzanne S Teuber, Bruce R. Hamaker

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Cross-reactivity of antibodies against almond major protein (AMP, a legumin), the major almond allergen, with cereal proteins may cause problems in detecting almond contaminants in cereal products when antibody-based assays are used. Rabbit polyclonal IgG antiserum produced against AMP was used to test cross-reactivity with protein extracts from maize, a cereal commonly found in breakfast and snack foods. Gradient SDS-PAGE followed by Western blotting was performed, and two cross-reactive proteins were detected by chemiluminescence. A fraction of maize proteins purified by elution from an IgG anti-AMP affinity column followed by electrophoreseis and immunoblotting showed a high degree of cross-reactivity with a minor 50 kDa protein of maize, as well as low cross-reactivity with the 27 kDa γ-zein. The 50 kDa cross-reactive protein was identified as the 50 kDa γ-zein by immunoreaction with anti-50 kDa γ-zein antiserum. Notably, the 50 kDa maize γ-zein also reacted with IgE from pooled human sera from patients with self-reported severe almond allergies. The high immunoreactivity of the 50 kDa γ-zein should be considered in maize quality improvement programs, and such notable cross-reactivity is of relevance in the design of antibody-based assays for almond allergen detection.

Original languageEnglish (US)
Pages (from-to)7965-7970
Number of pages6
JournalJournal of Agricultural and Food Chemistry
Volume53
Issue number20
DOIs
StatePublished - Oct 5 2005

Fingerprint

Zein
zein
almonds
cross reaction
Zea mays
corn
Adenosine Monophosphate
Proteins
proteins
allergens
antibodies
antiserum
Allergens
cereal proteins
Antibodies
Immune Sera
Cereal products
Assays
legumin
snack foods

Keywords

  • γ-zein
  • Allergen
  • Almond major protein
  • Cross-reactivity
  • Immunoreaction
  • Maize

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Food Science
  • Chemistry (miscellaneous)

Cite this

A 50 kDa maize γ-zein has marked cross-reactivity with the almond major protein. / Lee, Sung Ho; Benmoussa, Mustapha; Sathe, Shridhar K.; Roux, Kenneth H.; Teuber, Suzanne S; Hamaker, Bruce R.

In: Journal of Agricultural and Food Chemistry, Vol. 53, No. 20, 05.10.2005, p. 7965-7970.

Research output: Contribution to journalArticle

Lee, Sung Ho ; Benmoussa, Mustapha ; Sathe, Shridhar K. ; Roux, Kenneth H. ; Teuber, Suzanne S ; Hamaker, Bruce R. / A 50 kDa maize γ-zein has marked cross-reactivity with the almond major protein. In: Journal of Agricultural and Food Chemistry. 2005 ; Vol. 53, No. 20. pp. 7965-7970.
@article{16d365e6401142a891ced7d595eab85b,
title = "A 50 kDa maize γ-zein has marked cross-reactivity with the almond major protein",
abstract = "Cross-reactivity of antibodies against almond major protein (AMP, a legumin), the major almond allergen, with cereal proteins may cause problems in detecting almond contaminants in cereal products when antibody-based assays are used. Rabbit polyclonal IgG antiserum produced against AMP was used to test cross-reactivity with protein extracts from maize, a cereal commonly found in breakfast and snack foods. Gradient SDS-PAGE followed by Western blotting was performed, and two cross-reactive proteins were detected by chemiluminescence. A fraction of maize proteins purified by elution from an IgG anti-AMP affinity column followed by electrophoreseis and immunoblotting showed a high degree of cross-reactivity with a minor 50 kDa protein of maize, as well as low cross-reactivity with the 27 kDa γ-zein. The 50 kDa cross-reactive protein was identified as the 50 kDa γ-zein by immunoreaction with anti-50 kDa γ-zein antiserum. Notably, the 50 kDa maize γ-zein also reacted with IgE from pooled human sera from patients with self-reported severe almond allergies. The high immunoreactivity of the 50 kDa γ-zein should be considered in maize quality improvement programs, and such notable cross-reactivity is of relevance in the design of antibody-based assays for almond allergen detection.",
keywords = "γ-zein, Allergen, Almond major protein, Cross-reactivity, Immunoreaction, Maize",
author = "Lee, {Sung Ho} and Mustapha Benmoussa and Sathe, {Shridhar K.} and Roux, {Kenneth H.} and Teuber, {Suzanne S} and Hamaker, {Bruce R.}",
year = "2005",
month = "10",
day = "5",
doi = "10.1021/jf0479618",
language = "English (US)",
volume = "53",
pages = "7965--7970",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society",
number = "20",

}

TY - JOUR

T1 - A 50 kDa maize γ-zein has marked cross-reactivity with the almond major protein

AU - Lee, Sung Ho

AU - Benmoussa, Mustapha

AU - Sathe, Shridhar K.

AU - Roux, Kenneth H.

AU - Teuber, Suzanne S

AU - Hamaker, Bruce R.

PY - 2005/10/5

Y1 - 2005/10/5

N2 - Cross-reactivity of antibodies against almond major protein (AMP, a legumin), the major almond allergen, with cereal proteins may cause problems in detecting almond contaminants in cereal products when antibody-based assays are used. Rabbit polyclonal IgG antiserum produced against AMP was used to test cross-reactivity with protein extracts from maize, a cereal commonly found in breakfast and snack foods. Gradient SDS-PAGE followed by Western blotting was performed, and two cross-reactive proteins were detected by chemiluminescence. A fraction of maize proteins purified by elution from an IgG anti-AMP affinity column followed by electrophoreseis and immunoblotting showed a high degree of cross-reactivity with a minor 50 kDa protein of maize, as well as low cross-reactivity with the 27 kDa γ-zein. The 50 kDa cross-reactive protein was identified as the 50 kDa γ-zein by immunoreaction with anti-50 kDa γ-zein antiserum. Notably, the 50 kDa maize γ-zein also reacted with IgE from pooled human sera from patients with self-reported severe almond allergies. The high immunoreactivity of the 50 kDa γ-zein should be considered in maize quality improvement programs, and such notable cross-reactivity is of relevance in the design of antibody-based assays for almond allergen detection.

AB - Cross-reactivity of antibodies against almond major protein (AMP, a legumin), the major almond allergen, with cereal proteins may cause problems in detecting almond contaminants in cereal products when antibody-based assays are used. Rabbit polyclonal IgG antiserum produced against AMP was used to test cross-reactivity with protein extracts from maize, a cereal commonly found in breakfast and snack foods. Gradient SDS-PAGE followed by Western blotting was performed, and two cross-reactive proteins were detected by chemiluminescence. A fraction of maize proteins purified by elution from an IgG anti-AMP affinity column followed by electrophoreseis and immunoblotting showed a high degree of cross-reactivity with a minor 50 kDa protein of maize, as well as low cross-reactivity with the 27 kDa γ-zein. The 50 kDa cross-reactive protein was identified as the 50 kDa γ-zein by immunoreaction with anti-50 kDa γ-zein antiserum. Notably, the 50 kDa maize γ-zein also reacted with IgE from pooled human sera from patients with self-reported severe almond allergies. The high immunoreactivity of the 50 kDa γ-zein should be considered in maize quality improvement programs, and such notable cross-reactivity is of relevance in the design of antibody-based assays for almond allergen detection.

KW - γ-zein

KW - Allergen

KW - Almond major protein

KW - Cross-reactivity

KW - Immunoreaction

KW - Maize

UR - http://www.scopus.com/inward/record.url?scp=27144553150&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=27144553150&partnerID=8YFLogxK

U2 - 10.1021/jf0479618

DO - 10.1021/jf0479618

M3 - Article

C2 - 16190657

AN - SCOPUS:27144553150

VL - 53

SP - 7965

EP - 7970

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 20

ER -