Background: The increasing number of applications of sweet lupins in food is paralleled by an increase in immunoglobulin E (IgE)-mediated allergic reactions to lupin proteins. In particular, lupin allergy seems to appear in patients with an existing peanut allergy. In the present study, IgE-binding studies towards fractionated lupin seed proteins, and peanut and almond proteins were performed using sera from patients with confirmed lupin allergy. Methods:Immunoblotting and indirect ELISA were performed to investigate IgE binding to protein extracts. ELISA inhibition experiments were performed to investigate the presence of cross-reactive allergens in the protein extracts. Results: Immunoblotting and ELISA experiments demonstrated IgE binding to all lupin conglutins (α, β, γ and δ) as well as to peanut and almond proteins, with a unique IgE-binding profile for each patient. High IgE binding to α-conglutin was observed and IgE from the majority of patients similarly recognized two proteins within the α-conglutin-containing fraction, 40 and 43 kDa in size. Inhibition ELISA experiments showed that preincubation of sera with lupin conglutins, peanut and almond resulted in decreased IgE binding to lupin flour. Conclusions: Overall, these results indicate that α-, β-, γ- and δ-conglutins are candidate allergens in lupin and suggest a particularly strong allergenicity of α-conglutins. Furthermore, the results indicate the presence of cross-reactive allergens in lupin, peanut and almond.

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Background: Food-processing techniques may induce changes in fish protein immunogenicity. Allergens from >100 fish species have been identified, but little is known on the effects of processing on fish protein immunogenicity. Methods: IgE binding of sera of patients allergic to fresh and processed (smoked, salted/sugar-cured, canned, lye-treated and fermented) cod, haddock, salmon, trout, tuna, mackerel and herring and of hydrolysates based on salmon and whiting was investigated using immunoblot and inhibition ELISA. Results: Parvalbumin oligomers were identified using monoclonal and polyclonal antibodies. IgE binding was seen in most sera at 12–14 kDa (parvalbumin), and at 17–60 kDa for all fish except tuna. Changes in IgE binding appeared to reflect altered parvalbumin monomers and oligomers. Smoked haddock, salmon and mackerel had increased IgE binding and novel bands at 30 kDa. Chemically processed cod, salmon, trout and pickled herring had reduced or abolished IgE binding. The serum of 1 subject, however, had increased IgE binding to these products and also inhibition of binding by both fish hydrolysates to their constituent fish species. Conclusion: Process-induced changes in fish protein immunogenicity were more dependent on process rather than species, although individual responses varied. Changes in the allergenicity of a product may depend on the net effect of processing on parvalbumin oligomerization patterns, which may also vary in different species. Chemical processes generally caused loss in IgE-binding activity, though sensitization may occur to modified or degraded rather than intact peptides as shown by increased binding by chemically processed fish and hydrolysates in 1 subject. The clinical significance of these findings remains to be established.

Hen's egg white protein is a major cause of food allergy, and a considerable number of countries have introduced labeling directions for processed food products. To control compliance with these regulations, analytical assays for the detection of egg in manufactured foods have been developed. In this study, we have tested the performance of 3 commercially available kits for quantitative egg analysis using 6 model heat-processed foods. The 3 assays worked well under standard conditions with soluble egg white proteins, but only the kit using a denaturing-reducing extraction buffer detected egg in complex heat-treated food matrixes. The differently extracted food samples were further used to evaluate the stability and allergenicity of the egg white allergens ovalbumin, ovomucoid, ovotransferrin, and lysozyme with polyclonal anti-egg antibodies and sera of 6 patients with egg allergy. It could be shown that differences in egg protein extractability have a significant impact on the interpretation of study results.

Children with sensitization to lupin are not likely to have a clinical lupin allergy. Avoidance of lupin on the basis of lupin sensitization or peanut allergy would lead to unnecessarily strict diets. Food challenge is currently necessary to diagnose lupin allergy.