Food allergy and anaphylaxis – 2056. Clinical cross-reactivity of major food allergens among children

2017 ◽

Vol 54 (3) ◽

pp. 346

Author(s):

Chhavi Arya ◽

Chetna Jantwal

Keyword(s):

Food Allergy ◽

Food Allergies ◽

Allergic Reactions ◽

Food Allergens ◽

Food Groups ◽

Consumer Protection Act ◽

Major Food ◽

Life Threatening ◽

Major Allergens ◽

Allergen Labeling

Food allergens are the substances present in food that cause food allergy. Human body reactions to food allergens range from mild to severe life threatening anaphylactic shock. At least seventy different foods have been reported to cause allergic reactions and several other foods have been identified which have the potential to provoke allergic reactions. Majority of the identified food allergens are proteins. The Food Allergen Labeling and Consumer Protection Act (FALCPA) identifies eight major food groups i.e. milk, eggs, fish, crustacean shellfish, tree nuts, peanuts, wheat, and soybeans as major allergy causing foods. These eight foods are believed to account for 90 per cent of food allergies and are responsible for most serious reactions to foods. Several studies have been done which identify the major allergens in various foods. The present paper attempts to review the major allergens present in various food.

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Common food allergens and cross-reactivity

Journal of Food Allergy ◽

10.2500/jfa.2020.2.200020 ◽

2020 ◽

Vol 2 (1) ◽

pp. 17-21

Author(s):

Olivia L. Francis ◽

Kathleen Y. Wang ◽

Edwin H. Kim ◽

Timothy P. Moran

Keyword(s):

Food Allergy ◽

Protein Stability ◽

Cross Reactivity ◽

Molecular Characteristics ◽

Food Allergens ◽

Tree Nuts ◽

Heat Stable ◽

Systemic Reactions ◽

Hen’S Egg ◽

Fish And Shellfish

The most clinically relevant food allergens are cow’s milk, hen’s egg, peanut, tree nuts, wheat, soy, fish, shellfish, and seeds. Heat-stable food allergens have molecular characteristics that enhance protein stability and gastrointestinal absorption and thus are more likely to cause systemic reactions on ingestion. In contrast, heat-labile food allergens lack these characteristics and do not typically elicit reactions if sufficiently altered by heat or acid. Immunologic cross-sensitization between food allergens is more common than clinical cross-reactivity. However, certain groups of food allergens, such as tree nuts, fish, and shellfish, are associated with high rates of clinical cross-reactivity. Knowing the rates of clinical cross-reactivity is important when providing guidance to patients with food allergy and families on what foods can be safely added to the diet and what foods should be avoided.

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MECHANISMS OF FOOD ALLERGY CROSS-REACTIVITY FORMING: RESULTS OF RECENT STUDIES

Rossiiskii Allergologicheskii ZHurnal ◽

10.36691/rja1020 ◽

2009 ◽

Vol 6 (6) ◽

pp. 5-11

Author(s):

Ol'ga Sergeevna Fedorova ◽

L M Ogorodova ◽

O S Fedorova ◽

L M Ogorodova

Keyword(s):

Health Care ◽

Food Allergy ◽

Clinical Features ◽

Elimination Diet ◽

Cross Reactivity ◽

Diagnostic Methods ◽

Food Allergens ◽

Significant Interest

The phenomenon of food allergy cross:reactivity presents significant interest for investigators and health care specialists. This review provides an analysis of studies results of clinical features and manifestations mechanisms of cross:reactivity. There are information about the food allergens main classes, estimation of sensitivity of cross:reactivity different diagnostic methods, and principles of elimination diet in the article.

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Faculty Opinions recommendation of Exposure to food allergens through inflamed skin promotes intestinal food allergy through the thymic stromal lymphopoietin-basophil axis.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.718285496.793494494 ◽

2014 ◽

Author(s):

Johann Bauer ◽

Ana Sancho

Keyword(s):

Food Allergy ◽

Thymic Stromal Lymphopoietin ◽

Food Allergens

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Food allergy: nuts and tree nuts

British Journal Of Nutrition ◽

10.1017/bjn20061869 ◽

2006 ◽

Vol 96 (S2) ◽

pp. S95-S102 ◽

Cited By ~ 48

Author(s):

Jesus F. Crespo ◽

John M. James ◽

Consuelo Fernandez-Rodriguez ◽

Julia Rodriguez

Keyword(s):

Food Allergy ◽

Dietary Habits ◽

Storage Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Cross Reactivity ◽

Severe Reaction ◽

Immunological Mechanism ◽

Pathogenesis Related Protein ◽

The Usa

Nuts are a well-defined cause of food allergy, which affect approximately 1 % of the general population in the UK and the USA. There do appear to be differences in the frequency of nut allergy between different countries because of different dietary habits and cooking procedures. For example, in the USA and France, peanuts are one of the most frequent causes of food allergy, but in other countries, it seems to be less common. Genetic factors, in particular, appear to play a role in the development of peanut allergy. While the majority of nut allergens are seed storage proteins, other nut allergens are profilins and pathogenesis-related protein homologues, considered as panallergens because of their widespread distribution in plants. The presence of specific IgE antibodies to several nuts is a common clinical finding, but the clinical relevance of this cross-reactivity is usually limited. Allergic reactions to nuts appear to be particularly severe, sometimes even life-threatening, and fatal reactions following their ingestion have been documented. Food allergy is diagnosed by identifying an underlying immunological mechanism (i.e. allergic testing), and establishing a causal relationship between food ingestion and symptoms (i.e. oral challenges). In natural history investigations carried out in peanut-allergic children, approximately 20 % of the cases outgrew their allergy or developed oral tolerance. The treatment of nut allergies should include patient and family education about avoiding all presentations of the food and the potential for a severe reaction caused by accidental ingestion. Patients and families should be instructed how to recognise early symptoms of an allergic reaction and how to treat severe anaphylaxis promptly.

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Molecular basis of pollen-related food allergy: identification of a second cross-reactive IgE epitope on Pru av 1, the major cherry (Prunus avium) allergen

Biochemical Journal ◽

10.1042/bj20040842 ◽

2004 ◽

Vol 385 (1) ◽

pp. 319-327 ◽

Cited By ~ 36

Author(s):

Regina WICHE ◽

Michaela GUBESCH ◽

Herbert KÖNIG ◽

Kay FÖTISCH ◽

Andreas HOFFMANN ◽

...

Keyword(s):

Food Allergy ◽

Amino Acid ◽

Prunus Avium ◽

Protein Structures ◽

Cross Reactivity ◽

Type I ◽

Binding Region ◽

Leukaemia Cell Line ◽

Bet V 1 ◽

Ige Binding

Birch (Betula verrucosa) pollen-associated food allergy is a well-characterized syndrome, which is due to the cross-reactivity of IgE antibodies to homologous allergens in various foods. One crossreacting area on the major birch pollen allergen Bet v 1 and its homologue in cherry (Prunus avium) Pru av 1 has already been identified. This is the so-called ‘P-loop’ region, which encompasses amino acid residues around position 45 and is found on the two virtually identical tertiary protein structures. We tried to determine an additional IgE cross-reacting patch on Pru av 1 and Bet v 1. The putative IgE-binding region on Pru av 1 was localized with a mAb (monoclonal antibody) that was generated against Bet v 1, and cross-reacts with several Bet v 1 homologues in food and inhibits the binding of patients' IgE to Pru av 1. mAb reactivity pattern was analysed and amino acid positions 28 and 108 of Pru av 1 were selected and mutated by site-directed mutagenesis. The Pru av 1 mutants were produced as recombinant proteins and characterized for their folding, mAb- and IgE-binding capacity and allergenic potency with a cellular assay using the humanized rat basophilic leukaemia cell line RBL-25/30. Amino acid position 28 is involved in a second major IgE-binding region on Pru av 1 and probably on Bet v 1. The identification of this second major IgE-binding region is an essential prerequisite to understand the phenomenon of cross-reactivity and its clinical consequences, and to produce hypoallergenic proteins for an improved immunotherapy of type I allergy.

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Allergenic Characterization of New Mutant Forms of Pru p 3 as New Immunotherapy Vaccines

Clinical and Developmental Immunology ◽

10.1155/2013/385615 ◽

2013 ◽

Vol 2013 ◽

pp. 1-12 ◽

Cited By ~ 6

Author(s):

C. Gómez-Casado ◽

M. Garrido-Arandia ◽

P. Gamboa ◽

N. Blanca-López ◽

G. Canto ◽

...

Keyword(s):

Food Allergy ◽

Ex Vivo ◽

Binding Capacity ◽

Cross Reactivity ◽

T Cell Epitopes ◽

Native Form ◽

Ige Binding ◽

Pru P 3

Nowadays, treatment of food allergy only considered the avoidance of the specific food. However, the possibility of cross-reactivity makes this practice not very effective. Immunotherapy may exhibit as a good alternative to food allergy treatment. The use of hypoallergenic molecules with reduced IgE binding capacity but with ability to stimulate the immune system is a promising tool which could be developed for immunotherapy. In this study, three mutants of Pru p 3, the principal allergen of peach, were produced based on the described mimotope and T cell epitopes, by changing the specific residues to alanine, named asPru p 3.01, Pru p 3.02, andPru p 3.03.Pru p 3.01showed very similar allergenic activity as the wild type byin vitroassays. However,Pru p 3.02andPru p 3.03presented reduced IgE binding with respect to the native form, byin vitro,ex vivo,and in vivo assays. In addition,Pru p 3.03had affected the IgG4 binding capacity and presented a random circular dichroism, which was reflected in the nonrecognition by specific antibodies anti-Pru p 3. Nevertheless, bothPru p 3.02andPru p 3.03maintained the binding to IgG1 and their ability to activate T lymphocytes. Thus,Pru p 3.02andPru p 3.03could be good candidates for potential immunotherapy in peach-allergic patients.

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