Why are some proteins allergenic? Implications for biotechnology

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Abstract
In recent years, a number of agricultural crops have been developed with recombinant DNA technology. Because the transferred genes code for proteins that are ordinarily not present in these particular foods, there is concern about the potential allergenicity of these new crop varieties. Foods contain many proteins; however, only a small fraction are allergens. Although the structural properties of proteins that cause allergic reactions have not been characterized completely, known food allergens in general have molecular weights between 10 and 70 kDa, stimulate the immune response (induce the production of allergen-specific IgE), and are stable molecules that are resistant to processing, cooking, and digestion. Although any type of food is potentially allergenic, the majority of food allergies are caused by a small group of foods (cows' milk, nuts, legumes, eggs, seafood). Cross-reactivities occur within a given food group and between foods and seemingly unrelated proteins. Even though most transgenic foods are considered safe, biotechnological manipulation can affect crop allergenicity. The safety evaluation of transgenic foods is relatively easy when the allergenicity of the gene sources are known. The recombinant food can be assayed using traditional in vitro inhibition assays. Recently, reduced allergen content of biotechnologically altered rice was shown. In contrast, increased allergenicity was demonstrated in transgenic soybeans after a methionine- and cystine-rich protein from Brazil nuts, identified as a major Brazil nut allergen, was expressed in soybean to increase its content of sulfur-rich amino acids. The most difficult issue regarding transgenic food allergenicity is the effect of transfer of proteins of unknown allergenicity. The challenge is to determine whether these proteins are allergenic as there is no generally accepted, established, definitive procedure to define or predict a protein's allergenicity. Comparing the structures of the transferred protein with known allergens and allergen epitopes could be one approach. Additionally, Th-2 cell stimulation, the production of IL-4, and IgE antibody induction in animal models may help to evaluate the potential allergenicity of a protein. In conclusion, there is no evidence that recombinant proteins in newly developed foods are more allergenic than traditional proteins. The evidence suggests that the vast majority of these proteins will be completely safe for the consumer. The concern is that if a few transgenic foods cause serious allergic reactions, this could undermine the public's confidence in such products. It is essential that proper guidelines are established and tests are developed to assure that this will not occur.