Sigrid Sjölander

Soybean β‐conglycinin as the main allergen in a patient with food‐dependent exercise‐induced anaphylaxis by tofu: food processing alters pepsin resistance

Background Food‐dependent exercise‐induced anaphylaxis (FDEIA) due to soybeans is a rare disorder. The allergen responsible for FDEIA due to soybeans has not yet been determined.

IgE to Gly m 5 and Gly m 6 is associated with severe allergic reactions to soybean in Japanese children

IgE to Gly m 5 and Gly m 6 is associated with severe allergic reactions to soybean in Japanese children

Evaluation of IgE Antibodies to Recombinant Peanut Allergens in Patients with Reported Reactions to Peanut

Background: Peanut may cause severe reactions in allergic individuals. The objective was to evaluate IgE antibodies to various recombinant (r) peanut and birch pollen allergens in relation to IgE levels to whole peanut extract and severe allergic reactions to peanut. Methods: Seventy-four Swedish peanut-allergic patients (age: 14–61 years) reported previous peanut exposure and associated symptoms using a questionnaire. Their IgE reactivity to peanut, birch pollen and individual allergen components was analyzed using ImmunoCAP®. Results: Of the 48 subjects sensitized to Ara h 1, 2 or 3, 60% had peanut-specific IgE levels >15 kUA/l, while 100% of the subjects without detectable IgE to these allergens had low peanut-specific IgE levels (<10 kUA/l). The levels of IgE to rAra h 8, rBet v 1 and birch pollen were highly correlated (rS = 0.94, p < 0.0001). Fifty-eight patients reported adverse reactions after accidental or deliberate peanut exposure (oral, inhalation or skin) of whom 41 had IgE to rAra h 1, 2 or 3. Symptoms of respiratory distress were associated with sensitization to Ara h 1, 2 or 3 (56 vs. 18%, p < 0.01). Two cases of anaphylaxis were reported among the individuals sensitized to Ara h 1–3. IgE to rAra h 8, rAra h 9, profilin or cross-reactive carbohydrate determinants were not associated with severe symptoms. Conclusions: The results indicate that IgE reactivity to Ara h 1, 2 and 3 is associated with severe reactions after exposure to peanut in Swedish patients.

Wheat allergy in children evaluated with challenge and IgE antibodies to wheat components

Wheat sensitization is common but IgE antibodies (IgE‐abs) to wheat are not predictive of clinical symptoms in children with suspected wheat allergy. Wheat allergen components other than ω‐5 gliadin have not been well studied. Our aim was to characterize the clinical profile and investigate the value of adding measurements of IgE‐abs to wheat components in a group of children with a doctors diagnosed wheat allergy.

Secondary soy allergy in children with birch pollen allergy may cause both chronic and acute symptoms

To cite this article: De Swert LFA, Gadisseur R, Sjölander S, Raes M, Leus J, Van Hoeyveld E. Secondary soy allergy in children with birch pollen allergy may cause both chronic and acute symptoms. Pediatr Allergy Immunol 2011; Doi: 10.1111/j.1399‐3038.2011.01218.x

Two cases of pollen-food allergy syndrome to soy milk diagnosed by skin prick test, specific serum immunoglobulin E and microarray analysis

Oral allergy syndrome to soy milk is classified as a phenotype of pollen‐food allergy syndrome (PFAS). As causative antigens, Gly m 4 (Bet v 1 homolog, 17 kD) and oleosin (23 kD), have been reported. In this study, we report two cases of PFAS to soy milk. Both cases showed positive reactions to soy milk in skin prick tests (SPT) and to Gly m 4 in specific serum immunoglobulin (Ig)E antibody. When we measured specific serum IgE antibody of soy‐related proteins using a new laboratory testing method, microarray analysis, both cases showed a positive reaction for Bet v 1. One case was weakly positive for a soybean protein, β‐conglycinin. Other results for reactivity to soy, peanut, cross‐reactive carbohydrate determinants and profilin were negative. Based on these results, we diagnosed the two cases as PFAS to Gly m 4. We also performed protein microarray analysis and found it useful as a screening test for immediate allergy, such as PFAS.

Increase in pollen sensitization in Swedish adults and protective effect of keeping animals in childhood.

To date, most studies of the ‘allergy epidemic’ have been based on self‐reported data. There is still limited knowledge on time trends in allergic sensitization, especially among adults.

High prevalence of sIgE to Galactose‐α‐1,3‐galactose in rural pre‐Alps area: a cross‐sectional study

High prevalence of sIgE to Galactose--1,3-galactose in rural pre-Alps area : a cross-sectional study

Recognition pattern of kiwi seed storage proteins in kiwifruit-allergic children

To the Editor, The consumption of kiwifruits, both green (Actinidia deliciosa) and golden (Actinidia chinensis), is increasing and so is the allergy (1, 2). The sweeter golden kiwi is believed to be less allergenic due to its low content of actinidin (Act d 1), which is the major allergen in the pulp of green kiwi (3). The major focus on identifying kiwi allergens has been on allergens from the pulp; however, in a European study, the combined diagnostic sensitivity of five pulp allergens plus LTP (Act d 10) from seeds was not more than 65% (2). Recently, two novel allergens were found in seeds from green kiwi – Act d 12 and Act d 13 (4). Both are storage proteins, 11S globulin and 2S albumin, and bind IgE in sera from kiwi-allergic adults (4, 5). Generally, sensitization to storage proteins is linked to severe allergic food reactions. 2S albumin (Act d 13) was identified as a minor allergen in a population of adult Spanish patients where 18% were sensitized (5). Considering the described differences in symptoms between children and adults, where children on average have more severe reactions (6), Act d 13 could be of greater importance in children. Here, the aim was to, for the first time, investigate the sensitization pattern to seed storage proteins from both green and golden kiwifruits among children with kiwi allergy. Five Swedish children (10–17 years of age) being patients at an allergy department in Stockholm, Sweden, were studied. All five reported allergic symptoms within 30 min after kiwi ingestion. Four of the five reported systemic allergic symptoms and the fifth patient had oral allergy symptoms (OAS), the reason why all were considered kiwi-allergic (Table 1). Also, all patients were allergic to additional foods, like egg, milk, wheat, oats, sesame, peanuts, and nuts (Table 1). The children and their caregivers got written information and accepted to donate blood to this case report. Seed storage proteins from ripe green and golden kiwi were purified and characterized using a two-step approach after extraction. First, proteins were extracted from ground seeds in a phosphate buffer at neutral pH, after which they were separated by gel filtration (Superdex 75 pg XK 50/100 column; GE Healthcare, Uppsala, Sweden) and then further separated with anion (HiScreen Capto Q ImpRes column; GE Healthcare, Uppsala, Sweden) or cation (HiScreen Capto SP ImpRes column; GE Healthcare, Uppsala, Sweden) exchange chromatography. Purity of obtained proteins was estimated by SDS-PAGE, analytical gel filtration (Superdex 200 HR 10/30 column; GE Healthcare, Uppsala, Sweden), and mass spectroscopy (EASY-nLC 1000 interfaced by a Nanospray Flex to

A retrospect study into the utility of allergen components in walnut allergy

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