![]() Since most sera with reactivity to shrimp allergens were also reactive to crab and cockroach allergens, 15 sera were then chosen for the analysis of cross-reactivity among shrimp, crab, and cockroach serum samples by the quantitative-competitive inhibition tests. The serum was then used for the IgE immunoblotting to determine the extent of the inhibition of immunoblotting.ĪReaction types: i6, cockroach d1, dust mite ( Dermatophagoides pteronyssinus) d2, dust mite ( Dermatophagoides farinae) e1, cat dander e5, dog dander h1, house dust f23, crab f24, shrimp m1, Penicillium spp. For the inhibition of immunoblotting, the serum was also prebound with ImmunoCAP these allergens are cross-reactive to the examined allergen. The molecular weights of the proteins were estimated according to the description in each lot of strips by using relative mobility of molecular weight markers. After three washes, the color of the protein bands with reaction to serum IgE was developed by adding substrate reagent. The strip was then washed three times and incubated with enzyme-labeled anti-IgE for 30 min. According to the procedures of the AlaBLOT specific IgE allergen strips test, the diluted serum (50 μl in 500 μl) was added onto the strip, followed by incubation for 2 h at room temperature. The AlaBLOT specific IgE allergen strips (Diagnostic Products Co., Los Angeles, Calif.) were used to identify the serum IgE-reactive allergens by immunochemical means. The results allow us to understand the prevalence of immunosimilarity among examined allergens. Then, the sera with cross-reactivity were further analyzed by immunoblotting. As a control, other atopic sera with multiple IgE reactivities to dust mites, house dust, and dog dander were also examined for the immunosimilarity by quantitative-competitive inhibition tests. ![]() First, the atopic sera with the multiple IgE reactivity to cockroach, crab, and shrimp were chosen for the analysis of cross-reactivity with quantitative-competitive inhibition tests. Since the serum IgE with the reactivity to multiple allergens is commonly seen in clinical patients ( 6), we wanted to characterize the immunosimilarity among allergens. Furthermore, the investigation of atopic infants revealed that human milk whey protein and cow milk β-lactoglobulin not only share the epitope for IgE binding in vitro but also cause the atopic reaction in vivo ( 5). Calcium-involved carbohydrate-containing IgE epitopes also play a role in the cross-reactivity among several species of fish ( 3, 10). In addition, the tropomyosin in cockroach was identified as a major allergen with potential cross-reactivity with mite and shrimp allergens ( 12, 13, 19). Many species of grass pollen, latex, and fruit allergens share their immunological similarities with glycoprotein ( 2, 7- 9, 16, 21). In particular, the cross-reactivity among allergens has been documented ( 1). To avoid the allergen from environment exactly, the allergen for an atopic individual should be identified by the measurement of the specific IgE in serum with suspicious allergens. Family and twin studies have shown that both genetic and environmental factors are involved in the atopic reaction ( 14, 20). These results allow us to detect the cross-reactivity for atopic IgE against multiple allergens.Ītopic allergy, the most widespread immunologic disorder in human, is characterized by the increased and persistent level of immunoglobulin E (IgE) in serum ( 4, 11, 18). Furthermore, the results of immunoblotting are consistent with those of quantitative-competitive inhibition tests. The result shows that the competitive inhibition of IgE binding between shrimp and crab allergens is higher than those between either shrimp and cockroach or between crab and cockroach. The quantitative-competitive inhibition tests and the immunoblotting were applied to analyze the immunosimilarity among examined allergens. The present study analyzes whether the serum IgE with multiple reactivity is due to the presence of unique IgE against the common epitope shared by different allergens or the presence of multiple IgEs against different epitopes on different allergens. However, if IgE from the serum of an allergic patient exhibits reactivity to multiple allergens, it would cause a problem. For the purposes of allergen avoidance and immunotherapy, the measurement of specific IgE is widely applied in clinical laboratories. The existence of specific immunoglobulin E (IgE) allows us to determine the allergens that cause the allergic disease.
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