|Helm, Ricki - UAMS,LRCH, LITTLE ROCK,AR|
|Cockrell, Gael - UAMS,LRCH, LITTLE ROCK,AR|
|Connaughton, Cathie - UAMS,LRCH, LITTLE ROCK,AR|
|Sampson, Hugh - MT.SINAI MED SCH,NEW YORK|
|Bannon, Gary - UAMS,LRCH, LITTLE ROCK,AR|
|Beilinson, Vadim - PURDUE UNIV, BCHM|
|Burks, A - UAMS,LRCH, LITTLE ROCK,AR|
Submitted to: International Archives of Allergy and Immunology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: July 21, 2000
Publication Date: N/A
Interpretive Summary: Food allergies are becoming increasingly important as new foods enter the human food chain. Soy products have a history of eliciting allergic responses in a small but expanding proportion of the population. Sensitivity to soybean products generally involves gastrointestinal disturbances, but they generally become less severe as individuals mature. The research described in this communication is focused on the identification major soybean allergens to which individuals sensitive to soy products react. The allergen described in the communication is called glycinin. Because it is a seed storage protein, it is one of the most prevalent proteins in the seed. In this study, sites on soybean glycinin were identified where immunoglobulins from patients allergic to soybean bind. The information will aid scientists who are interested in either developing seeds that lack the allergen, or whose goal is to develop a means to desensitize individuals to soy products.
Technical Abstract: Individuals develop allergic sensitivity to glycinin, the most prevalent soybean seed storage protein. The objectives of this study were to:1) characterize specific B-cell epitopes on glycinin; 2) determine if any amino acid in each of the epitopes was critical to IgE binding, and 3) identify location in a three dimensional model of G2 glycinin. Eleven linear epitopes, representing 15 amino acid peptide sequences in G2 glycinin, bound IgE from patients allergic to soybean products. The epitopes were distributed asymmetrically on the surface of G2 trimers. The non-random distribution of IgE binding sites provides new insight about the organization of trimers in 11S complexes.