Ber e 1 protein: the versatile major allergen from Brazil nut seeds

Alcocer, Marcos; Rundqvist, Louise; Larsson, Göran

doi:10.1007/s10529-011-0831-1

Cited by 23 publications

(20 citation statements)

References 71 publications

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“…It was postulated that these differences were due to the age of children assessed with Cor a 9 specificity decreasing with age and Cor a 14 specificity increasing with age 28, 33. Other 2S albumins have been identified for walnut (Jug r 1),34, 35 cashew (Ana o 3), 36 and Brazil nut (Ber e 1) 37 (Table III). …”

Section: In Vitro Tests For Ige-mediated Food Allergymentioning

confidence: 99%

Making the Most of In Vitro Tests to Diagnose Food Allergy

Santos

Brough

2017

The Journal of Allergy and Clinical Immunology: In Practice

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Various in vitro tests assess different aspects of the underlying immune mechanism of IgE-mediated food allergy. Some can be used for diagnostic purposes; specific IgE to allergen extracts is widely available; specific IgE to allergen components is used in most specialist centers, and the basophil activation test is becoming increasingly used clinically. IgE to allergen peptides, T-cell assays, allergen-specific/total IgE ratios, and allergen-specific IgG4/IgE ratios are currently reserved for research. Different factors can modulate the likelihood of IgE-mediated food allergy of a given allergy test result, namely, the patients' age, ethnicity, previous allergic reaction to the identified food, concomitant atopic conditions, and geographical location, and need to be taken into account when interpreting the allergy test results in the clinic. The importance of the specific food, the clinical resources available, and patient preferences are additional aspects that need to be considered when deciding whether an oral food challenge is required to reach an accurate diagnosis of IgE-mediated food allergy.

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Section: In Vitro Tests For Ige-mediated Food Allergymentioning

confidence: 99%

Making the Most of In Vitro Tests to Diagnose Food Allergy

Santos

Brough

2017

The Journal of Allergy and Clinical Immunology: In Practice

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“…Historically, Ber e 1 has often been used as an example of the unintentional consequences that can occur in genetically modified (GM) crops. Ber e 1 consists of roughly 25% sulfurous amino acids [9], [10] and for this reason its gene was cloned into soybean with the intention of boosting the sulfur content of this leguminous plant. The outcome attracted much media attention since BN-allergic patients showed positive reactions in a skin-prick test (SPT) to the transgenic soybean, but not to the unmodified soybean, making Ber e 1 the first allergen to be transferred from one plant to another [11].…”

Section: Introductionmentioning

confidence: 99%

“…Stored in the hypocotyls of the embryo, wild-type Ber e 1 is posttranslationally cleaved into a small and large subunit that is linked together by four disulfide bonds [10], [12]. In order to perform structural studies, a recombinant Ber e 1 protein was overexpressed in the methylotropic yeast Pichia pastoris [12].…”

Section: Introductionmentioning

confidence: 99%

“…In order to perform structural studies, a recombinant Ber e 1 protein was overexpressed in the methylotropic yeast Pichia pastoris [12]. The recombinant Ber e 1 (rBer e 1) was expressed as a single polypeptide chain, similar to the wt protein, and was shown to contain partial posttranslational processing instead of the total removal of the linker peptide between the small and large subunits as observed in the wt protein [10]. In addition the rBer e 1, when expressed in Pichia pastoris , becomes O-glycosylated.…”

Section: Introductionmentioning

confidence: 99%

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Solution Structure, Copper Binding and Backbone Dynamics of Recombinant Ber e 1–The Major Allergen from Brazil Nut

Rundqvist

Tengel

Zdunek³

et al. 2012

PLoS ONE

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BackgroundThe 2S albumin Ber e 1 is the major allergen in Brazil nuts. Previous findings indicated that the protein alone does not cause an allergenic response in mice, but the addition of components from a Brazil nut lipid fraction were required. Structural details of Ber e 1 may contribute to the understanding of the allergenic properties of the protein and its potential interaction partners.Methodology/Principal FindingsThe solution structure of recombinant Ber e 1 was solved using NMR spectroscopy and measurements of the protein back bone dynamics at a residue-specific level were extracted using 15N-spin relaxation. A hydrophobic cavity was identified in the structure of Ber e 1. Using the paramagnetic relaxation enhancement property of Cu2+ in conjunction with NMR, it was shown that Ber e 1 is able to specifically interact with the divalent copper ion and the binding site was modeled into the structure. The IgE binding region as well as the copper binding site show increased dynamics on both fast ps-ns timescale as well as slower µs-ms timescale.Conclusions/SignificanceThe overall fold of Ber e 1 is similar to other 2S albumins, but the hydrophobic cavity resembles that of a homologous non-specific lipid transfer protein. Ber e 1 is the first 2S albumin shown to interact with Cu2+ ions. This Cu2+ binding has minimal effect on the electrostatic potential on the surface of the protein, but the charge distribution within the hydrophobic cavity is significantly altered. As the hydrophobic cavity is likely to be involved in a putative lipid interaction the Cu2+ can in turn affect the interaction that is essential to provoke an allergenic response.

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“…Although most isoforms have molecular weight of approximately 12 kDa with a high amino acid sequence homology, significant heterogeneity was found (Moreno et al, 2014). Alcocer et al (2012) stated that due to its extremely high content of sulfur amino acids, the allergen fraction has attracted much scientific attention as a target protein in transgenic biotechnology research, studies on processing of plant storage proteins and as an experimental protein in nutritional supplementation experiments. Some studies investigated the addition of Brazil nut protein to other foods such as soy.…”

Section: Brazil Nut Possible Allergies Symptomsmentioning

confidence: 99%

Brazil nut allergy: A review

Ariane¹,

Vildes²

2015

Afr. J. Pharm. Pharmacol.

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Tree nuts and their products are highly nutritive and beneficial to health. On the other hand, some of them can lead to development of allergic reactions, protein intolerance or liver diseases in some groups of consumers. Therefore, it is important to study the risks of tree nuts ingestion as a major issue for food regulators and the pharmaceutical industry safety. A review of surveillance and correlation to possible Brazil nut allergy reactions with effects on consumers and some therapeutic potential was carried out to help in understanding the mechanisms and so preventing damages to sensitive consumer's health.

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Ber e 1 protein: the versatile major allergen from Brazil nut seeds

Cited by 23 publications

References 71 publications

Making the Most of In Vitro Tests to Diagnose Food Allergy

Making the Most of In Vitro Tests to Diagnose Food Allergy

Solution Structure, Copper Binding and Backbone Dynamics of Recombinant Ber e 1–The Major Allergen from Brazil Nut

Brazil nut allergy: A review

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