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At least 19 recordsLinked to original sources
PubMed2003

Update on wheat hypersensitivity.

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.

Allergens↗
PubMedDate not supplied

Hypersensitivity to wheat flour in bakers.

Eleven bakers and 4 pastry cooks with hypersensitivity to wheat flour underwent skin tests to flours (wheat, barley, rye, oats), pollens (wheat, barley, rye, oats, grasses), mites (dermatophagoides pteronyssinus, dermatophagoides farinae), molds (alternaria, aspergillus) and weeds (parietaria judaica). The levels of serum immunoglobulins (IgG, IgA, IgM and IgE) were studied and the values of specific IgE (RAST) in the presence of wheat flour and the histamine release test for wheat flour, grass pollens, mites, molds and weeds were assessed. All the patients underwent a nasal challenge test to wheat flour. The results demonstrated the existence of cross reactions between the extracts of barley and rye flour with wheat flour (15/15) as well as between the pollens of cereals and cereal flours. The levels of specific IgE (PRU greater than .35) and the percentages of histamine release (greater than 10%) were positive in 14/15 cases. The nasal challenge test was positive for all the 15 patients under study. Of the patients studied, 11 received immunotherapy for periods ranging from 12 to 18 months. Of these patients, 9/11 continued working in the same occupation whereas the 2 who left their jobs in the industry corresponded to the cases of severe asthma which were polysensitized (flour, mites, molds).

Adult↗
PubMed2006

Study of IgE antigenic relationships in hypersensitivity to hydrolyzed wheat proteins and wheat-dependent exercise-induced anaphylaxis.

BACKGROUND: Wheat is involved in different forms of respiratory, food and contact allergy. The IgE of patients generally reacts with various flour proteins. It is not known if antigenic relationships could explain some of these reactions and if proteins could be involved in different pathologies. METHODS: Two sera were selected as representative of patients with either wheat-dependent exercise-induced anaphylaxis (WDEIA) or hypersensitivity to hydrolyzed wheat proteins (HHWP). Their IgE specificity was studied with wheat, barley and rye proteins, using immunoblot, and immunoblot inhibition with recombinant gamma-3 hordein. This protein was chosen for its cross-reactivity with omega-5 gliadin, a major allergen in WDEIA. RESULTS: The IgE from both sera strongly reacted with natural and recombinant gamma-3 hordein but displayed different patterns of reactivity with wheat, barley and rye proteins. Those from the WDEIA patient showed expected reactions with omega-5 gliadin, gamma-35 and gamma-75 secalins, but also with wheat low-molecular-weight glutenin subunits (LMW-GS), and not with C hordeins. On the contrary, IgE from a HHWP patient reacted with C hordeins, various omega gliadins, and gamma-75 secalin, but very weakly with gamma-35 secalin and LMW-GS. Recombinant gamma-3 hordein inhibited strongly but not totally the WDEIA patient's IgE binding to prolamins. No such inhibition could be observed for the HHWP patient's IgE. CONCLUSIONS: At least part of the reactions of prolamins with the IgE from the WDEIA patient was due to antigenic homologies. The occurrence of cross-reacting carbohydrates was unlikely. These common IgE epitopes were not involved in the pathology of the HHWP patient.

Adult↗
PubMed1995

Immunologic cross-reactivity among cereal grains and grasses in children with food hypersensitivity.

BACKGROUND: Because of a lack of clinical data from food challenges, allergists often recommend dietary restriction of all cereal grains in patients with sensitivity to at least one grain. OBJECTIVES: The purposes of this study were to assess the degree of intrabotanical cross-reactivity among cereal grains and related grasses, to better define the prevalence of multiple grain hypersensitivity, and to define the protein fractions associated with wheat hypersensitivity. METHODS: One hundred forty-five patients evaluated by food challenges and skin prick tests were divided into three groups: group 1, cereal grain and grass allergies; group 2, wheat allergy alone; and group 3, grass allergy alone. Fifteen patients were further selected from groups 1 to 3. Sodium dodecylsulfate--polyacrylamide gel electrophoresis and immunoblot analyses were performed on six grains and four related grasses with sera from these patients. RESULTS: Only 21% of patients had symptomatic reactivity as determined by food challenge; 80% had reactivity to only one grain. As determined by immunoblot analyses, patients in groups 1 and 2 showed extensive cross-reactivity (within each group) among grains but little cross-reactivity among grasses, whereas patients in group 3 showed cross-reactivity between the grains and grasses. Patients with wheat allergy had specific IgE binding to wheat fractions 47 kd and 20 kd, bands not recognized by patients with grass allergy. CONCLUSIONS: Clinically insignificant cross-reactivity exists among cereal grains and grasses; therefore, elimination of all grains from the diet of a patient with grain allergy is unwarranted. Further purification and characterization of the 47 kd and 20 kd wheat fractions is needed to provide more specific in vitro testing.

Adolescent↗
PubMed1990

Specific inhibition of lignification breaks hypersensitive resistance of wheat to stem rust.

When highly resistant wheat (Triticum aestivum L.) varieties are infected by an avirulent race of the stem rust fungus (Puccinia graminis Pers. f. sp. tritici Erics. and E. Henn.), penetrated host cells undergo rapid necrotization. This hypersensitive cell death is correlated with cellular lignification which efficiently restricts further fungal growth. Three competitive inhibitors of phenylalanine ammonia-lyase, the first enzyme of the general phenylpropanoid pathway and, thus, of lignin biosynthesis, namely alpha-aminooxyacetate, alpha-aminooxy-beta-phenylpropionic acid, and (1-amino-2-phenylethyl)phosphonic acid, and two highly specific irreversible suicide inhibitors of the lignification-specific enzyme cinnamyl-alcohol dehydrogenase, namely N(O-aminophenyl)sulfinamoyl-tertiobutyl acetate and N(O-hydroxyphenyl)sulfinamoyl-tertiobutyl acetate, were applied to genetically resistant wheat plants prior to inoculation with stem rust. Treatment with any of these inhibitors decreased the frequency of lignified necrotic host cells and concomitantly led to increased fungal growth. The cinnamyl-alcohol dehydrogenase inhibitors were generally more effective than the phenylalanine ammonia-lyase inhibitors, occasionally allowing some sporulation to occur on the resistant wheat leaves. These results clearly point to a causal relationship between the formation of lignin precursors and the resistance of wheat to stem rust.

Journal Article↗
PubMed2001

Syringolin reprograms wheat to undergo hypersensitive cell death in a compatible interaction with powdery mildew.

We had previously isolated and characterized syringolin A, one of the molecular determinants secreted by Pseudomonas syringae pv syringae that is perceived by nonhost plant species such as rice. Here, we show that syringolin A is recognized by wheat and that it induces the accumulation of gene transcripts and increases protection against powdery mildew when applied before inoculation. Moreover, syringolin A essentially eradicates powdery mildew from infected wheat if applied after inoculation. This curative effect is accompanied by the induction of cell death and the reactivation of pathogenesis-related genes whose transcript levels initially accumulate after powdery mildew inoculation but then decline during the later course of infection. Because syringolin A has no fungicidal activity against a variety of fungi and its action on wheat cannot be mimicked by the fungicide cyprodinil, syringolin A is hypothesized to counteract the suppression of host defense reactions imposed by the pathogen on the colonized cells.

Cell Death↗
PubMed1995

Identification of crossreacting wheat, rye, barley and soya flour allergens using sera from individuals with wheat-induced asthma.

We have conducted radio allergosorbent test (RAST), competitive RAST inhibition, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting using sera from patients with wheat-induced asthma to investigate the immunological relationship between wheat, rye, barley and soya, and to identify common proteins between these flours. RAST showed strong associations between the levels of specific IgE to wheat flour and those of rye and barley flour. Competitive RAST inhibition showed that wheat, rye, barley and soya flours contained crossreacting proteins, in decreasing concentrations. Wheat, rye and barley flours had similar protein profiles on gel electrophoresis. Soya flour contained a number of high molecular weight proteins not present in the other cereals. Western blotting using sera from 21 wheat flour hypersensitive individuals identified a large number of allergens in the different flours. Proteins of 69, 33, 26, 21 and 12 kDa were identified as major wheat flour allergens. Rye flour proteins of 21 and 12 kDa, and barley flour proteins of 69, 52 and 10 kDa were the major allergens identified by serum from wheat hypersensitive individuals. The major common protein of soya and wheat flour had a molecular weight of 21 kDa. The majority of crossreacting allergens identified between the different flours have molecular weights similar to those of known flour enzymes or enzyme inhibitors.

Allergens↗
PubMed2006

Hydrolysed wheat proteins present in cosmetics can induce immediate hypersensitivities.

Cosmetics containing hydrolysed wheat proteins (HWP) can induce rare but severe allergic reactions. 9 patients, all females without common wheat allergy, but with contact urticaria to such cosmetics, were studied. 6 of them also experienced generalized urticaria or anaphylaxis to foods containing HWP. All patients had low to moderate levels of immunoglobulin (Ig)E specific of wheat flour (f4) or gluten (f79). Their sensitivity to HWP and their tolerance to unmodified wheat proteins extracted from grains were confirmed using skin tests. Immunoblotting analyses showed that IgE from all patients reacted with almost all HWP tested. Reactions generally occurred with large random peptide aggregates. IgE reacted also with unmodified grain proteins, which contrasted with skin tests results. They reacted always with salt soluble proteins but variably with gluten proteins. No reaction occurred with gliadins in patients without associated immediate hypersensitivity to food containing HWP. These results show the role of hydrolysis on the allergenicity of wheat proteins, both through skin or digestive routes. At least part of the epitopes involved is pre-existing in unmodified wheat proteins. The aggregation of peptide bearing these epitopes and others created by hydrolysis, along with the increased solubility and the route of exposure, are possible factors of the allergenicity of HWP.

Adult↗
PubMed1985

Skin test and RAST responses to wheat and common allergens and respiratory disease in bakers.

Interrelationships between skin and humoral tests for immediate hypersensitivity to wheat and indicators of respiratory disease were examined in 176 male bakers. Skin tests were assessed by measuring the diameter of the weal resulting from prick innoculation of allergen extract and circulating allergen-specific IgE by radioallergosorbent test (RAST). Fifteen per cent of subjects showed positive skin-prick test responses to wheat extracts. These subjects demonstrated an increased prevalence of respiratory symptoms and of measurable bronchial responsiveness to methacholine. Thirty per cent of subjects had positive skin test responses to common allergens but negative responses to whole wheat. Compared to subjects with no positive skin test responses they had an increased prevalence of bronchial responsiveness to methacholine but a similar prevalence of respiratory symptoms. There was a significant association between skin test responses to whole wheat and skin test responses to common allergens suggesting that bakers with pre-existing sensitivity to common allergens are at increased risk of developing wheat flour sensitization. There was no significant difference between skin-prick test and RAST responses to wheat, water-soluble wheat protein and common allergens. Both tests showed similar relationships with indices of respiratory disease. The associations between skin test and RAST responses to wheat extracts and indices of respiratory disease was stronger for the water-soluble wheat proteins than for other wheat grain extracts. These results suggest that immediate hypersensitivity to wheat flour is important in the development of non-specific bronchial hyperreactivity in bakers and that the water-soluble fractions of wheat flour are the most important allergenic components.(ABSTRACT TRUNCATED AT 250 WORDS)

Adolescent↗
PubMed2001

The wheat cDNA LCT1 generates hypersensitivity to sodium in a salt-sensitive yeast strain.

Salinity affects large areas of agricultural land, and all major crop species are intolerant to high levels of sodium ions. The principal route for Na(+) uptake into plant cells remains to be identified. Non-selective ion channels and high-affinity potassium transporters have emerged as potential pathways for Na(+) entry. A third candidate for Na(+) transport into plant cells is a low-affinity cation transporter represented by the wheat protein LCT1, which is known to be permeable for a wide range of cations when expressed in yeast (Saccharomyces cerevisiae). To investigate the role of LCT1 in salt tolerance we have used the yeast strain G19, which is disrupted in the genes encoding Na(+) export pumps and as a result displays salt sensitivity comparable with wheat. After transformation with LCT1, G19 cells became hypersensitive to NaCl. We show that LCT1 expression results in a strong decrease of intracellular K(+)/Na(+) ratio in G19 cells due to the combined effect of enhanced Na(+) accumulation and loss of intracellular K(+). Na(+) uptake through LCT1 was inhibited by K(+) and Ca(2+) at high concentrations and the addition of these ions rescued growth of LCT1-transformed G19 on saline medium. LCT1 was also shown to mediate the uptake of Li(+) and Cs(+). Expression of two mutant LCT1 cDNAs with N-terminal truncations resulted in decreased Ca(2+) uptake and increased Na(+) tolerance compared with expression of the full-length LCT1. Our findings strongly suggest that LCT1 represents a molecular link between Ca(2+) and Na(+) uptake into plant cells.

Adaptation, Physiological↗
PubMed2003

[Diarrhea as manifestation of allergic diseases. The difficult search for the allergen].

Allergy is a very uncommon cause of diarrhoea. Other mechanisms, medical diseases and infections, psychological and pseudoallergic reactions, intolerance reactions, and enzyme defects/deficiency, and many other conditions are much more common. If food allergy is strongly suspected diagnosis may be difficult, even for allergologists, as it requires a mosaic of history, skin and in vitro tests, diagnostic diet, and even provocation tests. It is important to recognise diarrhoea "accompanying" allergic urticaria and anaphylactic reactions as part of the symptomatology of the primary dermatological or allergic disease and to refer the patient to the appropriate specialist.

Adult↗
PubMed2005

Different profiles of wheat antigens are recognised by patients suffering from coeliac disease and IgE-mediated food allergy.

BACKGROUND: Dietary intake of wheat can cause two distinct immunologically mediated diseases with severe gastrointestinal manifestations, coeliac disease (CD) and IgE-mediated food allergy. The pathomechanisms underlying these diseases are different, but the profile of the target antigens in wheat has not been compared for the two diseases. METHODS: We compared IgA- and IgE-reactive antigens in wheat using sera from patients with coeliac disease (n = 35) and food allergy to wheat (n = 16) by one- and two-dimensional immunoblotting. Furthermore, the IgG subclass (IgG1-IgG4) reactivity to wheat antigens was studied by enzyme-linked immunosorbent assay. RESULTS: IgA antibodies from CD patients and IgE antibodies from allergic patients recognised distinct profiles of wheat antigens. Furthermore, the IgG subclass responses to wheat antigens were different in CD and wheat-allergic patients. CONCLUSION: This study thus demonstrates that wheat contains antigens/epitopes which are preferentially recognised by CD patients, whereas others elicit IgE-mediated food allergy. This finding suggests that the nature of a food antigen may influence the quality of the pathological immune response in the gut and has implications for the diagnosis and therapy of hypersensitivity to wheat.

Adolescent↗
PubMed1997

Identification of the major water/salt insoluble wheat proteins involved in cereal hypersensitivity.

BACKGROUND: Several studies have investigated water/salt soluble proteins which comprise 50% of the proteins in wheat. The remaining 50% of wheat proteins, are water/salt insoluble proteins of which there is limited information on their role in cereal hypersensitivity. OBJECTIVES: To investigate the allergenicity of the water/salt insoluble gliadin and glutenin proteins (prolamins). METHODS: RAST, electrophoresis and Western blotting were used to identify water/salt insoluble wheat allergens. Competitive RAST inhibition was conducted to investigate cross-reactivity between prolamins and water/salt soluble wheat proteins. RESULTS: Specific IgE to alpha-gliadin and to total glutenins were detected in all sera. IgE to beta-, gamma-, fast omega-, and slow omega-gliadin were present in lower numbers of sera. Prolamin allergens of 90-11 kDa were identified by immunoblotting. Water/salt soluble proteins crossreacted with alpha-gliadin and total glutenins. CONCLUSIONS: Individuals who are hypersensitive to water/salt soluble wheat proteins produce specific IgE to water/salt insoluble wheat proteins. Western blotting has shown that gliadins, glutenins and proteins with similar molecular weights as the endogenous water/salt soluble wheat enzyme inhibitors are important allergens. Alpha and fast omega- are the most allergenic gliadins. The water/salt insoluble proteins share cross-reacting epitopes with water/salt soluble proteins. These data show that the numbers of proteins involved in the development of cereal hypersensitivity is greater than previously believed and that the development of specific IgE to alpha-gliadin may in part depend on the presence of cross-reacting antibodies to water/salt soluble flour allergens.

Antibodies, Blocking↗