Tree Nut Allergens

Roux, Kenneth H.; Teuber, Suzanne S.; Sathe, Shridhar K.

doi:10.1159/000072135

Cited by 170 publications

(111 citation statements)

References 59 publications

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“…Vicilins, also called 7S globulins, comprise one well-known class of storage proteins and can constitute as much as 70±80% of the total seed protein [19,20]. Using the SDS-PAGE electrophoresis method with a reductor agent, it was possible to observe globulins and albumins.…”

Section: Discussionmentioning

confidence: 99%

Obtention of Protein Concentrate and Polyphenols From Macadamia (Macadamia Integrifolia) With Aqueous Extraction Method

Greffa

Lara

Vilcacundo

et al. 2017

Asian J Pharm Clin Res

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Objective: The aim of this study was to obtain protein concentrates from Macadamia using alkaline pH at different pHs of precipitation with water to analyze the protein isolates using the native-polyacrylamide gel electrophoresis (PAGE), sodium dodecyl sulfate-PAGE (SDS-PAGE) electrophoresis, and reversed-phase high-performance liquid chromatography (RP-UHPLC) methods. Methods:Macadamia protein concentrates were obtained using the isoelectric precipitation method at different pHs using water as solvent. Proteins were analyzed using the native-PAGE, SDS-PAGE electrophoresis, and RP-UHPLC methods.Results: A yield of 36.57±0.17 a of protein concentrate of defatted Macadamia flour at pH 6.0 with a 51.564% of protein was obtained using the Dumas method. Polypeptides profile was identified in the 11-63 kDa range. Total polyphenols content was high at pH 5.0 with a value of 367,340 mg gallic acid equivalent equivalents/100 g. Conclusions:Macadamia seed is a good source of proteins. Native-PAGE, SDS-PAGE, and RP-UHPLC are good methods to identify the Macadamia protein isolate in the presence of water.

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Section: Discussionmentioning

confidence: 99%

Obtention of Protein Concentrate and Polyphenols From Macadamia (Macadamia Integrifolia) With Aqueous Extraction Method

Greffa

Lara

Vilcacundo

et al. 2017

Asian J Pharm Clin Res

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“…[12][13][14][15] Seed storage proteins from PNs and TNs are considered the major allergens contributing to the anaphylactic reactions of patients with nut allergy. 15 PN Ara h 2 is recognized as functionally more potent and considered the most clinically important PN allergen. 16 -19 Serum IgE to Ara h 2 is an important predictor of clinical reactivity to PN.…”

Section: Discussionmentioning

confidence: 99%

A retrospective study of peanut and tree nut allergy: Sensitization and correlations with clinical manifestations

2015

Allergy & Rhinology

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Peanut (PN) and tree nut (TN) P eanut (PN) and tree nut (TN) allergies can be severe and account for a relatively high proportion of fatal food-induced anaphylaxis.1,2 These allergies can be lifelong 3 and appear to be increasing in prevalence, especially in children.4,5 The current prevalence of nut allergy (2%) has doubled in the past 10 years. 5PN and TN allergy are a major health concern.6 PN is a legume, the same family as beans such as soy and peas, 7 and is different from TNs. Studies have shown cross-reactive allergen epitopes between PNs and TNs 8,9 but whether this results in clinical cross-reactivity remains unclear. This cohort study investigated the correlation between PN and TN allergy, in terms of clinical allergic manifestations and in vitro sensitization (IVS). METHODSWe conducted a retrospective medical chart review (2003)(2004)(2005)(2006)(2007)(2008)(2009)(2010)(2011)(2012) at the Allergy Clinic at University Hospital of Brooklyn. Cases of children (Ͼ3 years old) and adults who had PN and/or TN allergy (include cashew, walnut, almond, hazelnut, pistachio, or pecan) were reviewed. Presence of concurrent allergic disease including allergic rhinoconjunctivitis, asthma, and atopic dermatitis (AD) was also included in the database. This study was approved by the Institutional Review Board from State University of New York Downstate Medical Center. The data were collected without identifiers, and all of the information was kept confidential.The total number of organ systems involved in clinical reactivity was determined, including dermatologic (urticaria, pruritus, angioedema, swelling, and worsening of AD), respiratory (wheezing, throat tightness, shortness of breath, cough, and tight chest), gastrointestinal (nausea, vomiting, diarrhea, and abdominal pain), and neurological (dizziness and syncope). Degree of IVS was quantified as follows: 0, not reactive (IgE, Ͻ0.35 kU/L); 1, weakly reactive (IgE, 0.35-0.7 kU/L); 2, moderately reactive (IgE, 0.7-3.5 kU/L); 3, highly reactive (HR; IgE, 3.5-17.5 kU/L); 4, very highly reactive (VHR; IgE, 17.6 -100kU/L; Quest Diagnostics, Madison, NJ). For patients with multiple TN sensitivities by serum IgE, the greatest level of sensitivity was used in statistical analysis. Spearman correlation coefficients were generated to determine the relationship between total allergic reaction organ involvement and level of IVS.Statistical data analysis was performed using SAS Version 9.3 software (SAS, Cary, NC). RESULTSOf 1406 charts were reviewed; 76 (5.4% of 1406) patients were identified with self-reported PN or TN allergy.

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“…Ewan (1996) tested 62 patients for cross-reactivity to six nuts: peanut, Brazil nut, almond, hazelnut, walnut, and cashew nut, but did not report the species involved in each treatment. Table based on references (Altenbach et al 1987;Arshad et al 1991;Fernandez et al 1995;Tariq et al 1996;Marinas et al 1998;Moneret-Vautrin et al 1998;Sutherland et al 1999;Teuber and Peterson 1999;Teuber et al 1999Teuber et al , 2003Diaz-Perales et al 2000;Bannon et al 2001;Poltronieri et al 2002;Wang et al 2002;de Leon et al 2003;Roux et al 2003;Asero et al 2004;Lerch et al 2005;Crespo et al 2006;Benito et al 2007;Willison et al 2008;Ahn et al 2009;Breiteneder 2009;Garino et al 2010;Allergen.org 2014). VOLUME 33 (2) Tree Nut Allergenscross-reactivity, though additional comparisons are needed to investigate this hypothesis.…”

Section: Cross-reactivity Is Not Associated With Sequence Similaritymentioning

confidence: 99%

An Evolutionary Perspective on Human Cross-sensitivity to Tree Nut and Seed Allergens

Fisher¹,

Nawrocki²

2015

aliso

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Tree nut allergies are some of the most common and serious allergies in the United States. Patients who are sensitive to nuts or to seeds commonly called nuts are advised to avoid consuming a variety of different species, even though these may be distantly related in terms of their evolutionary history. This is because studies in the literature report that patients often display sensitivity to multiple nut species (crosssensitivity) if they have an existing nut allergy. These reports suggest that cross-sensitivity in patients with nut allergies may be caused by an IgE antibody reacting with epitopes present in the seed proteins of different species (cross-reactivity), for example, if IgE isolated from the serum of a patient were able to bind to both almond and peanut allergens. We hypothesize that allergenic proteins in seeds may have similar amino acid sequences that cause the observed cross-sensitivity. Here, we test the hypothesis that similarity in the protein sequences of allergenic nuts drives cross-sensitivity and cross-reactivity by reconstructing the gene trees of three allergenic seed-storage proteins (vicilin, legumin, and 2S albumin) from species sampled across vascular plants. We generate estimates of their phylogenetic relationships and compare these to the allergen cross-sensitivity and cross-reactivity data that is reported in the literature. In general, evolutionary relationships of the three proteins are congruent with the current understanding of plant species relationships. However, we find little evidence that distantly related nut species reported to be crossreactive share similar vicilin, legumin, or 2S albumin amino acid sequences. Our data thus suggests that features of the proteins other than their amino acid sequences may be driving the cross-reactivity observed during in vitro tests and skin tests. Our results support current treatment guidelines to limit nut and seed consumption if allergies are present in a patient. More studies are necessary to better understand the characteristics of allergenic proteins and patterns of cross-sensitivity in patients who suffer from nut allergies.

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Tree Nut Allergens

Cited by 170 publications

References 59 publications

Obtention of Protein Concentrate and Polyphenols From Macadamia (Macadamia Integrifolia) With Aqueous Extraction Method

Obtention of Protein Concentrate and Polyphenols From Macadamia (Macadamia Integrifolia) With Aqueous Extraction Method

A retrospective study of peanut and tree nut allergy: Sensitization and correlations with clinical manifestations

An Evolutionary Perspective on Human Cross-sensitivity to Tree Nut and Seed Allergens

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