Sensitization to the major allergen of Brazil nut is correlated with the clinical expression of allergy

National Research Council, Oristany, Sardinia, Italy
Journal of Allergy and Clinical Immunology (Impact Factor: 11.48). 01/1999; 102(6 Pt 1):1021-7. DOI: 10.1016/S0091-6749(98)70341-0
Source: PubMed


Only a few studies have investigated the clinical role of food allergens, especially the relationship between sensitization to a given allergen and occurrence of adverse reactions when eating the relevant food item.
This study evaluated the clinical role of the allergens of Brazil nut by comparing the patterns of IgE binding in sera from 11 patients with anaphylaxis after eating Brazil nuts with those from 10 subjects with no symptoms to this food item. Both groups had specific IgE to Brazil nut.
Allergens in the in-house extract of Brazil nut were identified by SDS-PAGE/immunoblotting, the major allergen was purified by HPLC, and its N-terminal sequence was determined by a protein sequencer.
SDS-PAGE/immunoblotting detected a number of allergenic components with molecular weights ranging from 4 to 58 kd. All sera from symptomatic patients recognized a 9-kd allergen corresponding (as established by amino acid sequencing) to a 2S albumin already described as a major allergen of Brazil nut, whereas the other allergens each bound IgE from less than 50% of sera. No sera from asymptomatic subjects showed IgE binding to the 9-kd allergen, but they did recognize components from 25 to 58 kd, which are minor allergens.
These findings indicate that the allergen underlying clinical reactions to Brazil nut is a 2S albumin of 9 kd and that in vitro reactivity to this allergen identifies subjects who react in vivo to ingestion of this food.

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    • "The prevalence of food allergy is approximately 1-2% in adults and 6-8% in children and most food allergies are mediated by antigen-specific IgE and are characterized as type-I reactions [1]. Cases of severe allergic reactions including anaphylaxis were reported for Brazil nut (Bertholletia excelsa) [2] and the storage protein 2S albumin was identified as allergen and classified as Ber e1. It has gained particular interest as in the early 1990’s it was considered to transfer the gene coding for the Brazil nut 2S albumin by transgenic techniques to soybean in order to improve its nutritional value for animal feed which however never reached the market due to the allergenic nature of the Brazil nut 2S albumin [3]. "
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    ABSTRACT: It is not exactly known why certain food proteins are more likely to sensitize. One of the characteristics of most food allergens is that they are stable to the acidic and proteolytic conditions in the digestive tract. This property is thought to be a risk factor in allergic sensitization. The purpose of the present study was to investigate the contribution of the protein structure of 2S albumin (Ber e1), a major allergen from Brazil nut, on the sensitizing capacity in vivo using an oral Brown Norway rat food allergy model. Disulphide bridges of 2S albumin were reduced and alkylated resulting in loss of protein structure and an increased pepsin digestibility in vitro. Both native 2S albumin and reduced/alkylated 2S albumin were administered by daily gavage dosing (0.1 and 1 mg) to Brown Norway rats for 42 days. Intraperitoneal administration was used as a positive control. Sera were analysed by ELISA and passive cutaneous anaphylaxis. Oral exposure to native or reduced/alkylated 2S albumin resulted in specific IgG1 and IgG2a responses whereas only native 2S albumin induced specific IgE in this model, which was confirmed by passive cutaneous anaphylaxis. This study has shown that the disruption of the protein structure of Brazil nut 2S albumin decreased the sensitizing potential in a Brown Norway rat food allergy model, whereas the immunogenicity of 2S albumin remained preserved. This observation may open possibilities for developing immunotherapy for Brazil nut allergy.
    11/2013; 3(1):36. DOI:10.1186/2045-7022-3-36
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    • "This ability to bind lipid affects the stability of some LTPs and their resistance to hydrolysis (Breiteneder & Mills, 2005; Douliez et al., 2000; Vassilopoulou et al., 2006). The 2S albumin and LTP protein families both include a number of major allergens, including SFA8 from sunflower (Yagami, 2010), Ara h 2 from peanut (Burks et al., 1991) and Ber e 1 from Brazil nut (Pastorello et al., 1998); and LTPs from peach (Pru p 1) (Wijesinha- Bettoni et al., 2010), barley (Wijesinha-Bettoni et al., 2010) apple (Sancho et al., 2005) and grape (Vassilopoulou et al., 2006). "
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    ABSTRACT: In order for a protein to elicit a systemic allergic response it must reach the circulatory system through the intestinal mucosa as a sufficiently large fragment with adequate structural integrity. Sunflower LTP and 2S albumins (SFA8 and three mixed fractions of Alb1 and Alb2) were digested in simulated gastric fluid (SGF) for 2h and the conditions were then changed to mimic the intestinal environment for a further 2h digestion. The effects of phosphatidylcholine (PC) and emulsification on the digestibility of the proteins were investigated. PC protected all of the proteins studied against both gastric and intestinal digestive enzymes but to different extents. Emulsification of SFA8 resulted in strong protection against digestion, which was further enhanced by the presence of PC in the SGF. These results highlight the importance of considering real food structures such as emulsified systems and also the gastrointestinal environment that proteins are exposed to once consumed when assessing allergenicity.
    Food Chemistry 06/2013; 138(4):2374-81. DOI:10.1016/j.foodchem.2012.12.034 · 3.39 Impact Factor
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    • "At this regard, 11S globulins might represent good candidates. Allergenic members of this protein family have been characterized from almond (Pru du 6) [19], hazelnut (Cor a 9) [20,21], peanut (Ara h 3) [22], walnut (Jug r 4) [23], pistachio (Pis v 2) [24], soybean (glycinins G1-G2) [25], Brazil nut (Ber e 2) [26], cashew nut (Ana o 2) [27], sesame seeds (Ses i 6) [28] or pecan (Car i 4) [29]. Some studies have previously shown that 11S globulins are involved in cross-reactivity between coconut and walnut [30], among buckwheat, poppy and hazelnut [31] or between peanut and other different seeds spices [32]. "
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    ABSTRACT: Background The 11S globulin Sin a 2 is a marker to predict severity of symptoms in mustard allergic patients. The potential implication of Sin a 2 in cross-reactivity with tree nuts and peanut has not been investigated so far. In this work, we studied at the IgG and IgE level the involvement of the 11S globulin Sin a 2 in cross-reactivity among mustard, tree nuts and peanut. Methods Eleven well-characterized mustard-allergic patients sensitized to Sin a 2 were included in the study. A specific anti-Sin a 2 serum was obtained in rabbit. Skin prick tests (SPT), enzyme-linked immunosorbent assay (ELISA), immunoblotting and IgG or IgE-inhibition immunoblotting experiments using purified Sin a 2, Sin a 1, Sin a 3, mustard, almond, hazelnut, pistachio, walnut or peanut extracts were performed. Results The rabbit anti-Sin a 2 serum showed high affinity and specificity to Sin a 2, which allowed us to demonstrate that Sin a 2 shares IgG epitopes with allergenic 11S globulins from tree nuts (almond, hazelnut, pistachio and walnut) but not from peanut. All the patients included in the study had positive skin prick test to tree nuts and/or peanut and we subdivided them into two different groups according to their clinical symptoms after ingestion of such allergenic sources. We showed that 11S globulins contain conserved IgE epitopes involved in cross-reactivity among mustard, tree nuts and peanut as well as species-specific IgE epitopes. Conclusions The allergenic 11S globulin Sin a 2 from mustard is involved in cross-reactivity at the IgE level with tree nuts and peanut. Although the clinical relevance of the cross-reactive IgE epitopes present in 11S globulins needs to be investigated in further detail, our results contribute to improve the diagnosis and management of mustard allergic patients sensitized to Sin a 2.
    12/2012; 2(1):23. DOI:10.1186/2045-7022-2-23
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