Cross-Reactivity Between the Soybean Protein P34 and Bovine Caseins

Abstract

PurposeSoy-based formulas are widely used as dairy substitutes to treat milk allergy patients. However, reactions to soy have been reported in a small proportion of patients with IgE-mediated milk allergies. The aim of this work was to explore whether P34, a mayor soybean allergen, is involved in this cross-reactivity.MethodsIn vitro recognition of P34 was evaluated by immunoblotting, competitive ELISA and basophil activation tests (BAT) using sera from allergic patients. In vivo cross-reactivity was examined using an IgE-mediated milk allergy mouse model.ResultsP34 was recognized by IgE antibodies from the sera of milk allergic patients, casein-specific monoclonal antibodies, and sera from milk-allergic mice. Spleen cells from sensitized mice incubated with milk, soy or P34 secreted IL-5 and IL-13, while IFN-γ remained unchanged. In addition, the cutaneous test was positive with cow's milk proteins (CMP) and P34 in the milk allergy mouse model. Moreover, milk-sensitized mice developed immediate symptoms following sublingual exposure to P34.ConclusionsOur results demonstrate that P34 shares epitopes with bovine casein, which is responsible for inducing hypersensitivity symptoms in milk allergic mice. This is the first report of the in vivo cross-allergenicity of P34.

The effects of whey and soy proteins on growth performance, gastrointestinal digestion, and selected physiological responses in rats

“…21 This suggested some similarity in the IgE epitope sequence and a possible cross reaction of antibodies with two proteins of different species. 22,23 Preparation S did not show the presence of nonsoy proteins. A strong reaction with anti-β-glycinin antibodies (50% cross reactivity level) confirmed that β-glycinin is one of the main proteins in the S preparation ( Fig.…”

Bovine Milk Allergens: A Comprehensive Review

“…Nonetheless, it has been demonstrated that some patients are intolerant to such products, suggesting the cross‐reactivity between soy and cow milk proteins. It was reported that the α‐subunit of beta‐conglycinin (Gly m 5.0101) from the vicilin‐like protein family, the G4 subunit of glycinin (Gly m 6.0401) from legumin‐like proteins, and, more recently, the cysteine protease P34 (Gly m Bd30K) and the globulin P28 (Gly m Bd28K) are involved in cross‐reactivity phenomena with bovine caseins (Rozenfeld and others ; Katz and others ; Smaldini and others ; Curciarello and others ; Candreva and others ; Candreva and others ).…”

Identification of cross-reactive B-cell epitopes between Bos d 9.0101(Bos Taurus ) and Gly m 5.0101 (Glycine max ) by epitope mapping MALDI-TOF MS

“…Curciarello et al. used overlapping 15‐mer peptides and mapped cross‐reactive B cell epitopes in the C‐terminal region .Noteworthy, in this study we have been able to map for the first time B cell epitopes in the entire molecule of Gly m 5.0101 using peptides in solution.…”

“…Fu et al also reported epitope 125-LRRHKNKNPFLFGSNRFE-142 as one of the major IgG-binding region of the Gly m 5.0101 using a pool of plasma from ten piglets [40]. Curciarello et al used overlapping 15-mer peptides and mapped cross-reactive B cell epitopes in the C-terminal region [14].Noteworthy, in this study we have been able to map for the first time B cell epitopes in the entire molecule of Gly m 5.0101 using peptides in solution.…”