Abstract:The presence of sIgE-omega-5-gliadin-ab is related to the reaction level to wheat challenge outcome in wheat-sensitized children. The sIgE-omega-5-gliadin-ab was found to be associated with a strong convincing history of wheat allergy also in those cases when oral food challenge was avoided. The sIgE-omega-5-gliadin-ab level may serve as a marker for clinical reactivity in wheat-sensitized individuals.
“…This is in agreement with the findings among Finnish as well Japanese subjects [8,11]. We cannot, however, confirm the findings of Tokuda et al [28] that the basophil response to ω-5 gliadin predicted wheat allergy in children.…”
Section: Discussionsupporting
confidence: 49%
“…Among the gliadins, ω-5 gliadin (Tri a 19) was identified as a major allergen of wheat-dependent, exercise-induced anaphylaxis (WDEIA) as well as in immediate reactions to ingested wheat in children [8,9,10]. IgE-Ab to ω-5 gliadin correlate better with challenge outcome compared to IgE-Ab to wheat [11,12] and can be useful when monitoring tolerance development over time [13]. …”
Background: Wheat is a common food causing allergy which has implications on the quality of life. The diagnosis of IgE-mediated wheat allergy is based on the clinical history and presence of IgE antibodies (IgE-Ab) in skin or blood, and the results of an oral food challenge which is time consuming and associated with risks. An improved diagnostic workup is needed for wheat allergy. The objective was to examine the relationship between wheat challenge, CD-sens and IgE-Ab to related allergens in wheat-allergic children and investigate if a combination of different markers could enhance the prediction of challenge outcome. Method: Twenty-four children (aged 1-15 years) with a wheat allergy diagnosis underwent an open wheat challenge. CD-sens and IgE-Ab to wheat, hydrolyzed wheat protein (HWP), ω-5 gliadin and timothy grass were analyzed and related to the challenge outcome. Results: A positive challenge was seen in 12/24 children. Children reacting to the challenge had higher IgE-Ab concentrations to wheat, ω-5 gliadin and HWP (p < 0.01) and a tendency to higher wheat CD-sens values (p = 0.08) than nonreacting children. Combining wheat CD-sens >150 and IgE-Ab to wheat >20 kUA/l, or ω-5 gliadin >0.1 kUA/l predicted the challenge outcome in 83% of the patients. Most children with IgE-Ab to wheat also had IgE-Ab to timothy. Seven of 9 challenge-positive children had a positive CD-sens to HWP and IgE-Ab to HWP >8 kUA/l. Conclusion: Combining CD-sens and IgE-Ab to wheat or wheat components could be useful in the diagnosis and follow-up of wheat-allergic children.
“…This is in agreement with the findings among Finnish as well Japanese subjects [8,11]. We cannot, however, confirm the findings of Tokuda et al [28] that the basophil response to ω-5 gliadin predicted wheat allergy in children.…”
Section: Discussionsupporting
confidence: 49%
“…Among the gliadins, ω-5 gliadin (Tri a 19) was identified as a major allergen of wheat-dependent, exercise-induced anaphylaxis (WDEIA) as well as in immediate reactions to ingested wheat in children [8,9,10]. IgE-Ab to ω-5 gliadin correlate better with challenge outcome compared to IgE-Ab to wheat [11,12] and can be useful when monitoring tolerance development over time [13]. …”
Background: Wheat is a common food causing allergy which has implications on the quality of life. The diagnosis of IgE-mediated wheat allergy is based on the clinical history and presence of IgE antibodies (IgE-Ab) in skin or blood, and the results of an oral food challenge which is time consuming and associated with risks. An improved diagnostic workup is needed for wheat allergy. The objective was to examine the relationship between wheat challenge, CD-sens and IgE-Ab to related allergens in wheat-allergic children and investigate if a combination of different markers could enhance the prediction of challenge outcome. Method: Twenty-four children (aged 1-15 years) with a wheat allergy diagnosis underwent an open wheat challenge. CD-sens and IgE-Ab to wheat, hydrolyzed wheat protein (HWP), ω-5 gliadin and timothy grass were analyzed and related to the challenge outcome. Results: A positive challenge was seen in 12/24 children. Children reacting to the challenge had higher IgE-Ab concentrations to wheat, ω-5 gliadin and HWP (p < 0.01) and a tendency to higher wheat CD-sens values (p = 0.08) than nonreacting children. Combining wheat CD-sens >150 and IgE-Ab to wheat >20 kUA/l, or ω-5 gliadin >0.1 kUA/l predicted the challenge outcome in 83% of the patients. Most children with IgE-Ab to wheat also had IgE-Ab to timothy. Seven of 9 challenge-positive children had a positive CD-sens to HWP and IgE-Ab to HWP >8 kUA/l. Conclusion: Combining CD-sens and IgE-Ab to wheat or wheat components could be useful in the diagnosis and follow-up of wheat-allergic children.
“…It seems obvious as the ω-5 gliadin fractions act as the main allergens in WDEIA [18,[32][33][34]. However, ω-5 can be also active in other wheat allergies [21,35]. Hence, we could expect the detection of ω-5 by at least some of the sera tested.…”
Skoczowski A, Obtułowicz K, Czarnobilska E, Dyga W, Mazur M, Stawoska I, Waga J. Antibody reactivity in patients with IgE-mediated wheat allergy to various subunits and fractions of gluten and non-gluten proteins from ω-gliadin-free wheat genotypes. Ann Agric Environ Med. 2017; 24(2): 229-236. doi: 10.5604/12321966.1233572 Abstract Introduction and objective. Gluten proteins (gliadins and glutenins) are polymorphic wheat storage proteins of allergenic properties. Significant differences in chemical composition between both protein groups allow to expect highly specific immunological response of individual subunits and fractions in reactions with IgE sera of people allergic to wheat. The aim of these studies was to identify and characterize the most allergenic gluten proteins (GP) and nongluten proteins (NGP) occurred in two closely related wheat hybrid genotypes. Materials and method. 3xC and 3xN wheat hybrids, which differ strongly in regard of gliadin composition, were analyzed. Seven people manifesting different symptoms of wheat allergy donated sera for the experiment. The technique of immunoblotting after SDS-PAGE was used for identification of allergenic subunits and fractions among GP and NGP. Immunologically active protein bands were visualized by chemiluminescence. Results. Great variation of immunodetection spectra was observed. Results of immunoblotting showed LMW glutenins to be of highest, gliadins of medium, while NGP of lowest allergenicity for selected patients. The 43-kDa and 47-kDa LMW glutenin subunits, 40-kDa and 43-kDa γ-gliadin fractions and 49-kDa NGP can be considered as the most immunoreactive among all protein bands separated by SDS-PAGE. Conclusion. The observed differentiation of immunodetection spectra allows to model highly specific IgE-binding profiles of allergenic wheat proteins attributed to individual patients with symptoms of gluten intolerance. Highly immunoreactive subunits and fractions among GP and NGP were identified. The observed immunoreactivity of 49 kDa NGP is worth to emphasize, as it has never been reported as wheat allergenic protein before.
“…The low sensitization rates (as estimated by specific IgE) to most identified allergens associated with this disease, together with the limited number of patients studied in each case [9][10][11][12][13], and the reported variability in sensitization patterns [14], have probably retarded the development of such molecular panel. In contrast, specific IgE to co-5 gliadin has been proposed as a useful tool for diagnosis of wheatdependant exercise-induced anaphylaxis and wheat food allergy [31,32]. Tri a 14, an abundant LTP in wheat seeds, has been recently identified by in vitro and in vivo methods as a major allergen associated with baker's asthma in Spanish patients [16].…”
Summary
Background
Baker's asthma is an important occupational allergic disease. Wheat lipid transfer protein (LTP) Tri a 14 is a major allergen associated with wheat allergy. No panel of wheat recombinant allergens for component‐resolved diagnosis of baker's asthma is currently available.
Objective
To evaluate the potential role of recombinant Tri a 14 as a novel tool for the diagnosis of baker's asthma, and to test the heat and proteolytic resistance of the wheat LTP allergen.
Methods
A cDNA encoding Tri a 14 was isolated and sequenced, the recombinant allergen produced in Pichia pastoris and purified by chromatographic methods. Physicochemical and immunological comparison of the natural and recombinant forms of Tri a 14 was carried out by N‐terminal amino acid sequencing, matrix‐assisted laser desorption/ionization mass spectrometry, circular dichroism (CD) analysis, IgE immunodetection, and specific IgE determination and ELISA‐inhibition assays using a pool or individual sera from 26 patients with baker's asthma. Thermal denaturation and simulated gastrointestinal digestion of both Tri a 14 forms were checked by spectroscopic and electrophoretic methods, respectively, and biological activity by basophil activation test (BAT).
Results
Natural and recombinant Tri a 14 were similarly folded, as indicated by their nearly identical CD spectra and heat denaturation profiles. A high interclass correlation coefficient (0.882) was found between specific IgE levels to both Tri a 14 proteins in individual sera from baker's asthma patients, but a slightly lower IgE‐binding potency of rTri a 14 was detected by ELISA‐inhibition assays. Natural and recombinant Tri a 14 elicited positive BAT in two and one out of three patients, respectively. Heat denaturation profiles and simulated gastrointestinal digestion assays indicated that Tri a 14 displayed a high heat and digestive proteolytic resistance, comparable to those of peach Pru p 3, the model food allergen of the LTP family.
Conclusions
Recombinant Tri a 14 is a potential tool for baker's asthma diagnosis, based on its physicochemical and immunological similarity with its natural counterpart. Wheat Tri a 14 shows a high thermal stability and resistance to gastrointestinal digestion.
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