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 language | English (US) |
|---|---|
| Pages (from-to) | 7965-7970 |
| Number of pages | 6 |
| Journal | Journal of Agricultural and Food Chemistry |
| Volume | 53 |
| Issue number | 20 |
| DOIs | |
| State | Published - Oct 5 2005 |
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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 journal › Article
}
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 -