PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 12840704

Update on wheat hypersensitivity.

Kati Palosuo
View original source ↗Export metadata ↓

Abstract

PURPOSE OF REVIEW: Wheat is among the six foods responsible for approximately 90% of food allergies in children, and in recent years wheat has been increasingly recognized as a cause of food-dependent, exercise-induced anaphylaxis. Wheat flour is an important cause of baker's asthma, a well-known occupational respiratory allergy to inhaled flour. This review outlines the diverse clinical manifestations of IgE-mediated wheat hypersensitivity and summarizes recent advances in characterization of clinically significant allergens. RECENT FINDINGS: Only a few of the numerous wheat proteins recognized by IgE of sensitized individuals have been characterized at the molecular level. Characterized allergens causing baker's asthma include several water/salt-soluble wheat proteins, however sensitization patterns show a great degree of individual variation. The insoluble gliadins have been implicated in IgE-mediated allergy to ingested wheat, and omega-5 gliadin has been identified as a major allergen in wheat-dependent, exercise-induced anaphylaxis. The presence of IgE to purified omega-5 gliadin in children was highly predictive of immediate clinical symptoms on oral wheat challenge. SUMMARY: Diagnostic skin prick and in-vitro tests measuring sensitization against water/salt-soluble wheat proteins have poor predictive values. Quantification of gliadin-specific IgE in serum or skin prick testing with gliadin could serve as an additional tool in the diagnostic work-up of allergy to ingested wheat.

Explore related subjects

AllergensAnaphylaxisAntibody SpecificityCross ReactionsFlourHumansImmunoglobulin EWheat HypersensitivityJournal ArticleReview

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Kati Palosuo. 2003. Update on wheat hypersensitivity.. https://doi.org/10.1097/00130832-200306000-00009

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2004

Effect of technological processing on the allergenicity of mangoes (Mangifera indica L.).

In parallel with the rising popularity of exotic fruits in Europe, allergy against mango is of increasing importance. Because mangoes are also consumed as processed products such as chutneys or beverages, the influences of different process conditions on their allergenicity were investigated. Mango purees and nectars were manufactured at small pilot-plant scale, and the allergenic potencies of the resulting intermediate and final products were determined by means of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), immunoblotting and inhibitive enzyme allergosorbent tests (EAST-inhibition), using a pool serum of 9 individuals with manifest mango allergy. The mango allergens were shown to be very stable during technological processing. Irrespective of enzymatic matrix decomposition, mechanical tissue disintegration and heating during peeling, mash treatment, and pasteurization, significant loss of allergenicity could not be observed in the extracts of mango purees and nectars derived thereof. These results were confirmed by analogous investigation of commercial mango drinks and nectars. Hence, conventional mango processing into pulp-containing products typical for this species obviously does not allow complete elimination of the allergenic potency.

Allergens↗
PubMed2004

Development of a real-time PCR and a sandwich ELISA for detection of potentially allergenic trace amounts of peanut (Arachis hypogaea) in processed foods.

Hidden allergens in food products are, especially for peanut-allergic consumers, a serious problem because even low amounts (approximately 200 microg) of peanut can elicit allergic reactions. Undeclared peanut traces can be found in processed food products, because contaminations with peanut during production processes are frequent. To minimize the risk of such cross-contaminations, it is necessary to develop sensitive analytical methods for the detection of hidden allergens in foods. For this approach we developed two peanut-specific assays based on the detection of peanut protein by specific antibodies (sandwich ELISA) and by the detection of peanut-specific DNA (part of the coding region of Ara h 2) by a real-time PCR. Both tests did not show any cross-reactivity with 22 common food ingredients (cereals, nuts, legumes), and the limit of detection is <10 ppm peanut in processed foods. Thirty-three random samples of food products were tested for the presence of peanut to compare both assay types with each other and to evaluate the percentage of foods on the German market that are contaminated with peanut traces. We found that four products (13.3%) without peanut in the list of ingredients contained peanut protein in a range from 1 to 74 ppm peanut protein and that the results of both tests correlated well. The real-time PCR was able to detect one more positive sample than the sandwich ELISA. In conclusion, both assays are sensitive and specific tools for the detection of hidden allergens in processed foods.

Allergens↗
PubMed2004

Maillard reaction and enzymatic browning affect the allergenicity of Pru av 1, the major allergen from cherry (Prunus avium).

The influence of thermal processing and nonenymatic as well as polyphenoloxidase-catalyzed browning reaction on the allergenicity of the major cherry allergen Pru av 1 was investigated. After thermal treatment of the recombinant protein rPru av 1 in the absence or presence of carbohydrates, SDS-PAGE, enzyme allergosorbent tests, and inhibition assays revealed that thermal treatment of rPru av 1 alone did not show any influence on the IgE-binding activity of the protein at least for 30 min, thus correlating well with the refolding of the allergen in buffer solution as demonstrated by CD spectroscopic experiments. Incubation of the protein with starch and maltose also showed no effect on IgE-binding activity, whereas reaction with glucose and ribose and, even more pronounced, with the carbohydrate breakdown products glyceraldehyde and glyoxal induced a strong decrease of the IgE-binding capacity of rPru av 1. In the second part of the study, the effect of polyphenoloxidase-catalyzed oxidation of polyphenols on food allergen activity was investigated. Incubation of rPru av 1 with epicatechin in the presence of tyrosinase led to a drastic decrease in IgE-binding activity of the protein. Variations of the phenolic compound revealed caffeic acid and epicatechin as the most active inhibitors of the IgE-binding activity of rPru av 1, followed by catechin and gallic acid, and, finally, by quercetin and rutin, showing significantly lower activity. On the basis of these data, reactive intermediates formed during thermal carbohydrate degradation as well as during enzymatic polyphenol oxidation are suggested as the active chemical species responsible for modifying nucleophilic amino acid side chains of proteins, thus inducing an irreversible change in the tertiary structure of the protein and resulting in a loss of conformational epitopes of the allergen.

Allergens↗