Food Allergens—Molecular and Immunological Characteristics

Breiteneder, Heimo; Mills, E. N. Clare

doi:10.1002/9781118744185.ch4

Cited by 5 publications

(4 citation statements)

References 243 publications

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“…The molecular basis for the observed coexisting sensitivities is not yet fully understood, as it remains unclear if they are the result of multiple primary sensitivities or molecular cross-reactivities. Major allergens in peanut and tree nuts belong to a relatively small number of protein families, particularly storage proteins (2S albumins, vicilins, legumins and profilins) [ 7 ], indicating that conserved structures and biological activities play a role in determining or promoting the sensitizing and cross-reactivity properties of proteins [ 29 , 30 ].…”

Section: Resultsmentioning

confidence: 99%

Immunoglobulin E-Binding Pattern of Canadian Peanut Allergic Children and Cross-Reactivity with Almond, Hazelnut and Pistachio

et al. 2020

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Peanut allergic individuals can be both co-sensitized and co-allergic to peanut and tree nuts. At the moment, standard diagnostic approaches do not always allow differentiation between clinically relevant sensitization and nonsignificant cross-reactions, and the responsibility of each allergen remains unclear. The objective of this study was therefore to determine a peanut sensitization profile in a cohort of Canadian peanut allergic children and assess the immunoglobulin E (IgE) molecular cross-reactivity between peanut, almond, hazelnut and pistachio. The specific IgE (sIgE) levels of each patient serum were determined by ImmunoCAP, indirect ELISA and immunoblot to examine their sIgE-binding levels and profiles to peanut proteins. Reciprocal inhibition ELISA and immunoblotting were used to study sIgE cross-reactions between peanut and the selected tree nuts using an adjusted and representative serum pool of the nine allergic patients. The results showed that the prepared peanut and tree nut protein extracts allowed for the detection of the majority of peanut and selected tree nut known allergens. The reciprocal inhibition ELISA experiments showed limited sIgE cross-reactivities between peanut and the studied tree nuts, with peanut being most likely the sensitizing allergen and tree nuts the cross-reactive ones. In the case of hazelnut and pistachio, a coexisting primary sensitization to hazelnut and pistachio was also demonstrated in the serum pool. Reciprocal inhibition immunoblotting further revealed that storage proteins (2S albumin, 7S vicilin and 11S legumin) could possibly account for the observed IgE-cross-reactions between peanut and the studied tree nuts in this cohort of allergic individuals. It also demonstrated the importance of conformational epitopes in the exhibited cross-reactions.

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Section: Resultsmentioning

confidence: 99%

Immunoglobulin E-Binding Pattern of Canadian Peanut Allergic Children and Cross-Reactivity with Almond, Hazelnut and Pistachio

et al. 2020

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“…The heat stability of some protein allergens is considered an important feature for the retention or increase in the allergenicity of some foods after cooking or processing (Breiteneder and Mills 2008). For most proteins, the function is linked to their native folded conformation (Berg et al 2002).…”

Section: Heat Stabilitymentioning

confidence: 99%

Assessment of the potential allergenicity of genetically-engineered food crops

Ladics

2018

Journal of Immunotoxicology

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An extensive safety assessment process exists for genetically-engineered (GE) crops. The assessment includes an evaluation of the introduced protein as well as the crop containing the protein with the goal of demonstrating the GE crop is "as-safe-as" non-GE crops in the food supply. One of the evaluations for GE crops is to assess the expressed protein for allergenic potential. Currently, no single factor is recognized as a predictor for protein allergenicity. Therefore, a weight-of-the-evidence approach, which accounts for a variety of factors and approaches for an overall assessment of allergenic potential, is conducted. This assessment includes an evaluation of the history of exposure and safety of the gene(s) source; protein structure (e.g. amino acid sequence identity to human allergens); stability of the protein to pepsin digestion in vitro; heat stability of the protein; glycosylation status; and when appropriate, specific IgE binding studies with sera from relevant clinically allergic subjects. Since GE crops were first commercialized over 20 years ago, there is no proof that the introduced novel protein(s) in any commercialized GE food crop has caused food allergy.

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“…Additional tree nut allergens are pan-allergens, including LTPs, profilins, and heveins. These are found in a wide variety of pollens, tree nuts, seeds, fruits, and vegetables and are associated with significant IgE-mediated cross-reactivity [63] . Similar to many of the allergens responsible for peanut allergy, many of the proteins responsible for severe reactions to tree nuts (vicilins, legumin-like proteins, LTPs, and heveins) are resistant to proteolysis and denaturation [64,65] .…”

Section: Tree Nut Allergensmentioning

confidence: 99%

“…Seed storage proteins, the major allergens in peanut and tree nuts, are glycosylated proteins that contain disulfide bonds. These features confer stability to the protein structures under conditions of high temperature and extreme pH, such as those occurring during gastric digestion [63] . There is a genetic predisposition to peanut allergy, with a 7% sibling risk, but the apparent increase in prevalence may be attributed to environmental factors [1] .…”

Section: Pathogenesismentioning

confidence: 99%

Peanut and Tree Nut Allergy

Cox

Sicherer²

2015

Food Allergy: Molecular Basis and Clinical Practice

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Allergy to peanut and tree nuts is a major worldwide health concern. The prevalence of these allergies may be increasing, but the reasons for these increases remain unclear. This group of foods accounts for a large proportion of severe and fatal food-allergic reactions. These allergies present most often during childhood but can occur at any age. Resolution is possible but uncommon, and frequent lifetime reactions caused by accidental ingestion are a serious problem. The major allergens of peanut and most tree nuts have been identified, allowing for insights into patient diagnoses, clinical outcomes, and potential future immunotherapies. © 2015 S. Karger AG, Basel Ebisawa M, Ballmer-Weber BK, Vieths S, Wood RA (eds): Food Allergy: Molecular Basis and Clinical Practice.

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Food Allergens—Molecular and Immunological Characteristics

Cited by 5 publications

References 243 publications

Immunoglobulin E-Binding Pattern of Canadian Peanut Allergic Children and Cross-Reactivity with Almond, Hazelnut and Pistachio

Immunoglobulin E-Binding Pattern of Canadian Peanut Allergic Children and Cross-Reactivity with Almond, Hazelnut and Pistachio

Assessment of the potential allergenicity of genetically-engineered food crops

Peanut and Tree Nut Allergy

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