Clinical importance of cross-reactivity in food allergy

2004 ◽  
Vol 4 (3) ◽  
pp. 235-240 ◽  
Author(s):  
Ronald van Ree
Keyword(s):  
Food Allergy ◽  
Clinical Importance ◽  
Cross Reactivity

scholarly journals Novel Allergen Discovery through Comprehensive De Novo Transcriptomic Analyses of Five Shrimp Species

2020 ◽  
Vol 22 (1) ◽  
pp. 32
Author(s):  
Shaymaviswanathan Karnaneedi ◽  
Roger Huerlimann ◽  
Elecia B. Johnston ◽  
Roni Nugraha ◽  
Thimo Ruethers ◽  
...  
Keyword(s):  
De Novo ◽  
Penaeus Monodon ◽  
Clinical Importance ◽  
Major Allergen ◽  
Cross Reactivity ◽  
Multiple Sequence ◽  
Alpha Tubulin ◽  
Shrimp Species ◽  
Allergen Sources ◽  
Shellfish Allergy

Shellfish allergy affects 2% of the world’s population and persists for life in most patients. The diagnosis of shellfish allergy, in particular shrimp, is challenging due to the similarity of allergenic proteins from other invertebrates. Despite the clinical importance of immunological cross-reactivity among shellfish species and between allergenic invertebrates such as dust mites, the underlying molecular basis is not well understood. Here we mine the complete transcriptome of five frequently consumed shrimp species to identify and compare allergens with all known allergen sources. The transcriptomes were assembled de novo, using Trinity, from raw RNA-Seq data of the whiteleg shrimp (Litopenaeus vannamei), black tiger shrimp (Penaeus monodon), banana shrimp (Fenneropenaeus merguiensis), king shrimp (Melicertus latisulcatus), and endeavour shrimp (Metapenaeus endeavouri). BLAST searching using the two major allergen databases, WHO/IUIS Allergen Nomenclature and AllergenOnline, successfully identified all seven known crustacean allergens. The analyses revealed up to 39 unreported allergens in the different shrimp species, including heat shock protein (HSP), alpha-tubulin, chymotrypsin, cyclophilin, beta-enolase, aldolase A, and glyceraldehyde-3-phosphate dehydrogenase (G3PD). Multiple sequence alignment (Clustal Omega) demonstrated high homology with allergens from other invertebrates including mites and cockroaches. This first transcriptomic analyses of allergens in a major food source provides a valuable resource for investigating shellfish allergens, comparing invertebrate allergens and future development of improved diagnostics for food allergy.

scholarly journals Food allergy: nuts and tree nuts

2006 ◽  
Vol 96 (S2) ◽  
pp. S95-S102 ◽  
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.

scholarly journals 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

2004 ◽  
Vol 385 (1) ◽  
pp. 319-327 ◽  
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.

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

2013 ◽  
Vol 2013 ◽  
pp. 1-12 ◽  
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.

scholarly journals Common food allergens and cross-reactivity

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.

A structural basis for food allergy: the role of cross-reactivity

2008 ◽  
Vol 8 (1) ◽  
pp. 82-86 ◽  
Author(s):  
Rana S Bonds ◽  
Terumi Midoro-Horiuti ◽  
Randall Goldblum
Keyword(s):  
Food Allergy ◽  
Cross Reactivity ◽  
Structural Basis

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

2013 ◽  
Vol 6 ◽  
pp. P139
Author(s):  
Miho Hasegawa ◽  
Takatsugu Komata ◽  
Kiyotake Ogura ◽  
Katsuhito Iikura ◽  
Sakura Sato ◽  
...  
Keyword(s):  
Food Allergy ◽  
Cross Reactivity ◽  
Food Allergens ◽  
Major Food

MILESTONES MARKING THE KNOWLEDGE OF ADVERSE REACTIONS TO FOOD IN THE DECADE OF THE 1980s

PEDIATRICS ◽  
1995 ◽  
Vol 96 (2) ◽  
pp. 380-381
Author(s):  
Betty Miller
Keyword(s):  
Food Allergy ◽  
Adverse Reactions ◽  
Food Additives ◽  
Food Challenge ◽  
Cross Reactivity ◽  
Allergic Reactions ◽  
Double Blind ◽  
Specific Patient ◽  
Clinical Sensitivity ◽  
A Prospective Study

Purpose of the Study. This study outlines the significant advances made to our understanding of adverse reactions to foods and food additives in the last decade. The milestones are listed in order of overall importance and are discussed in depth in the review. 1. Establishing double-blind, placebo-controlled food challenge (DBPCFC) as the "gold-standard" for defining specific patient population to be used in scientific studies. (VanMetre, May, Bock) 2. Recognition of the key role food allergy plays in the pathogenesis of atopic dermatitis. (Sampson, May) 3. Identifying the group of foods most likely to be associated with true allergic reactions. Analysis of DBPCFC in children has shown that 93% of allergic reactions occurred to eight foods (in order of frequency): egg, peanut, milk, soy, tree nuts, crustacean-type shellfish, fish, and wheat. Corn and chocolate allergy was rarely found. (Bock, Sampson, Atkins) 4. Food allergy has a natural history. In a prospective study of 501 children, Bock found that, of 15 cases of allergy proven by DBPCFC in the first year of life, none of the 15 cases was reactive beyond 24 months of age. In contrast, long-term follow-up of patients who have experienced peanut anaphylaxis revealed that clinical sensitivity lasts for at least 14 years. (Bock, Atkins) 5. Food allergy cross-sensitivity (clinical reactivity) does not extend equally to all members of a biologic food family. Although immunologic cross-reactivity between peanut, soy, and other peas/beans could be regularly found in allergic patients, clinically important cross-reactions demonstrated by DBPCFC were rare. (Bernhisel -Broadbent, Sampson)

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