The Major Soybean Allergen Gly m Bd 28K Induces Hypersensitivity Reactions in Mice Sensitized to Cow’s Milk Proteins

Candreva, Ángela María; Smaldini, Paola Lorena; Curciarello, Renata; Fossati, Carlos A.; Docena, Guillermo Horacio; Petruccelli, Silvana

doi:10.1021/acs.jafc.5b05623

Cited by 23 publications

(25 citation statements)

References 50 publications

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“…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 ).…”

Section: Cross‐reactivity Of Milk Allergensmentioning

confidence: 99%

Bovine Milk Allergens: A Comprehensive Review

Villa

Costa

Oliveira

et al. 2017

Comp Rev Food Sci Food Safe

177

145

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Cow milk allergy is one of the most common food allergies in early childhood and often persists through adult life, forcing an individual to a complete elimination diet. Milk proteins are present in uncounted food products, such as cheese, yogurt, or bakery item, exposing allergic persons to a constant threat. Many efforts have been made to overcome this global problem and to improve the life quality of allergic individuals. First, proper and reliable food labeling is fundamental for consumers, but the verification of its compliance is also needed, which should rely on accurate and sensitive analytical methods to detect milk allergens in processed foods. At the same time, strategies to reduce milk allergenicity, such as immunotherapy or the use of food processing techniques to modify allergen structure, have to be extensively studied. Recent research findings on the applicability of food processing, such as heat treatment, fermentation, or high pressure, have revealed great potential in reducing milk allergenicity. In this review, significant research advances on cow milk allergy are explored, focusing on prevalence, diagnosis, and therapy. Molecular characterization of cow milk allergens and cross-reactivity with other nonbovine milk species are described, as well as the effects of processing, food matrix, and digestibility on milk allergenicity. Additionally, analytical methods for the detection of milk allergens in food are described, from immunoassays and mass spectrometry methods for protein analysis to real-time polymerase chain reaction for DNA analysis.

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Section: Cross‐reactivity Of Milk Allergensmentioning

confidence: 99%

Bovine Milk Allergens: A Comprehensive Review

Villa

Costa

Oliveira

et al. 2017

Comp Rev Food Sci Food Safe

177

145

View full text Add to dashboard Cite

show abstract

“…Furthermore, Candreva et al analyzed the in silico similarity between proteins at the peptide level 5 . Cross‐reactivity between milk and soy proteins has been suggested by other immunologic studies 6 .…”

Section: Introductionmentioning

confidence: 99%

Evaluation of cross‐reactivity between casein components using inhibition assay and in silico analysis

Naito

Matsui²,

Yamada

et al. 2020

Pediatric Allergy Immunology

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Casein (CN), a major allergen for patients with persistent cow's milk (CM) allergy, comprises approximately 80% of CM proteins. 1 Bovine CN is constituted of four components, αs1-, αs2-, β-, and κ-CN, and exists as a micelle with a 30-300 nm diameter. 2 CN is an unfolded phosphoprotein and interacts with calcium phosphate in milk. 3 αs-CN is defined as an insoluble fraction in 0.4 mol/L calcium chloride, while κ-CN is the soluble fraction. β-CN is defined as soluble in 3.3 mol/L urea and insoluble in 1.7 mol/L urea. Bovine αs1-, αs2- ,

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“…Furthermore, Candreva et al analyzed the in silico similarity between proteins at the peptide level. 5 Crossreactivity between milk and soy proteins has been suggested by other immunological studies. 6 Thus, we also employed an in silico analysis at the peptide level using the peptide similarity tool on the Structural Database of Allergenic Proteins (SDAP).…”

Section: Introductionmentioning

confidence: 87%

Evaluation of cross-reactivity between casein components using inhibition assay and in silico analysis

Naito

Matsui²,

Yamada

et al. 2020

Preprint

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Background: We previously reported that the specific IgE levels to αs1-casein (CN) and β-CN in patients with cow's milk allergy decreased with similar dynamics during oral immunotherapy. Therefore, we hypothesized that αs1-and β-CN have strong crossreactivity among CN components, despite the low similarity in the full-length amino acid sequences. Methods: The αs1-, β-, and κ-CN were purified from commercial cow's milk. We recruited 39 patients with cow's milk allergy and the serum IgE levels for each CN component were measured by enzyme-linked immunosorbent assay (ELISA). Cross-reactivity between CN components was investigated by competitive ELISA against αs1-CN. Sequence homology between CN components at the peptide level was calculated using in silico analysis and quantified by the Property Distance (PD) value. Results: The αs1-CN-specific IgE levels exhibited a strong positive correlation with the β-CN-specific IgE (r = 0.945, P < 0.001). Complete competition was observed by β-CN against αs1-CN, suggesting the presence of common epitopes between them. In silico analysis detected 24 peptide sets with PD values lower than 10 between αs1-and β-CN, and 14 sets between αs1-and κ-CN. The amino acid sequences of αs1-(E61-E70) and β-CN (I12-E21) that showed the lowest PD value (5.30) were present in the characteristic sequence known as casein phosphopeptide (CPP). Conclusion: We detected strong cross-reactivity between CN components. Furthermore, we found highly homologous sequences in the CPP region, which contains a core sequence of "SSSEE" with phosphorylated serine residues.

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The Major Soybean Allergen Gly m Bd 28K Induces Hypersensitivity Reactions in Mice Sensitized to Cow’s Milk Proteins

Cited by 23 publications

References 50 publications

Bovine Milk Allergens: A Comprehensive Review

Bovine Milk Allergens: A Comprehensive Review

Evaluation of cross‐reactivity between casein components using inhibition assay and in silico analysis

Evaluation of cross-reactivity between casein components using inhibition assay and in silico analysis

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