Ana o 1, a cashew (Anacardium occidental) allergen of the vicilin seed storage protein family

Wang, Fang; Robotham, Jason M.; Teuber, Suzanne S.; Tawde, Pallavi; Sathe, Shridhar K.; Roux, Kenneth H.

doi:10.1067/mai.2002.125208

Cited by 159 publications

(175 citation statements)

References 35 publications

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“…All three allergens are classified as seed storage proteins. Of patients allergic to cashew nut, 50% (10 of 20 sera) are sensitized to recombinant Ana o 1, 62% (13 of 21 sera) to recombinant Ana o 2 and 81% (21 of 26 sera) to recombinant Ana o 3 determined by Western immunoblotting (14,15,17).…”

Section: Allergensmentioning

confidence: 99%

Systematic review on cashew nut allergy

Valk

Dubois

Wijk

et al. 2014

Allergy

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Recent studies on cashew nut allergy suggest that the prevalence of cashew nut allergy is increasing. Cashew nut consumption by allergic patients can cause severe reactions, including anaphylaxis. This review summarizes current knowledge on cashew nut allergy to facilitate timely clinical recognition and to promote awareness of this emerging food allergy amongst clinicians. The goal of this study is to present a systematic review focused on the clinical aspects of allergy to cashew nut including the characteristics of cashew nut, the prevalence, allergenic components, cross-reactivity, diagnosis and management of cashew nut allergy. The literature search yielded 255 articles of which 40 met our selection criteria and were considered to be relevant for this review. The 40 articles included one prospective study, six retrospective studies and seven case reports. The remaining 26 papers were not directly related to cashew nut allergy. The literature suggests that the prevalence of cashew nut allergy is increasing, although the level of evidence for this is low. A minimal amount of cashew nut allergen may cause a severe allergic reaction, suggesting high potency comparable with other tree nuts and peanuts. Cashew allergy is clearly an underestimated important healthcare problem, especially in children.Although peanut allergy has been on the increase for two decades or more, studies indicate that cashew nut is also becoming an important food allergen (1, 2). The rapid increase in consumption of cashew nuts and the change in eating and cooking habits may be responsible for the increasing significance of cashew nut allergy (2).In this paper, we summarize the relevant information available on epidemiology, allergen components, clinical features, diagnosis, clinical and in vitro cross-sensitization and management of cashew nut allergy. Data sources and literature searchIn our search, we adhered to the methods and procedures of the Preferred Reporting Items for Systematic Reviews and Meta-analyses (PRISMA) guidelines for reporting this systematic review, excluding irrelevant items. Registration number in PROSPERO is CRD42013004047.We used Ovid MEDLINE and EMBASE databases to identify relevant articles using the string: (Anacardi* sensitiv*) OR allerg*): de, ab, ti for EMBASE. We also checked references to relevant articles ('snowballing').We aimed to include studies focused on the clinical aspects of cashew nut allergy. We considered only studies in English. There was no restriction on publication date. Mouse model studies were excluded. Initially, all articles on cashew nut allergy or on cashew nuts were included. Thereafter articles on contact dermatitis, genetics, product labelling, poisoning, detection methods and possible medicinal effects of cashew plants were excluded. Forty of 255 articles found with the literature search (244 articles) and by 'snowballing (11 articles) were considered relevant for the review. Of these 40 articles, one article was a prospective study and six articles were retrospective stu...

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Section: Allergensmentioning

confidence: 99%

Systematic review on cashew nut allergy

Valk

Dubois

Wijk

et al. 2014

Allergy

View full text Add to dashboard Cite

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“…Cashews, like other nuts, contain 3 conserved seed storage proteins that have been characterized as food allergens by the International Union of Immunological Societies (IUIS). These include the 7S vicilin Ana o 1 [16], 11S legumin Ana o 2 [17], and the 2S albumin Ana o 3 [18]. Cashew allergens such as Ana o 1, Ana o 2, and Ana o 3 are resistant to physical and thermal processing methods [19,20].…”

Section: Introductionmentioning

confidence: 99%

Treatment of cashew extracts with Aspergillopepsin reduces IgE binding to cashew allergens

2016

J App Biol Biotech

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Enzymes from Aspergillus fungal species are used in many industrial and pharmaceutical applications. Aspergillus niger and Aspergillus oryzae were cultured on media containing cashew nut flour to identify secreted proteins that may be useful as future food allergen processing enzymes. Mass-spectrometric analysis of secreted proteins and protein bands from SDS-PAGE gels indicated the presence of at least 63 proteins. The majority of these proteins were involved in carbohydrate metabolism, but there were also enzymes involved in lipid and protein metabolism. It is likely that some of these enzymes are specifically upregulated in response to cashew nut protein, and study of these enzymes could aid our understanding of cashew nut metabolism. Aspergillopepsin from A. niger was one of the proteolytic enzymes identified, and 6 distinct peptides were matched to this protein providing 22% coverage of the protein. Cashew extracts were incubated with a commercially available preparation of Aspergillopepsin (Acid Stable Protease, ASP) using simulated gastric fluid conditions to determine if ASP could degrade the protein and lower antibody binding to cashew allergens. Following treatment of cashew extract with ASP, a significant reduction was observed in cashew allergen binding to rabbit anti-cashew IgG using an immunoblot assay and serum IgE antibodies from cashew allergic individuals using competitive ELISA. These findings highlight the possible application of Aspergillopepsin/ASP from A. niger in food processing steps to attenuate cashew nut and other tree nut or peanut allergens.

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“…Wang et al (2002) aligned a newly identified vicilin gene in cashews (Ana o 1) with the peanut vicilin gene (Ara h 1). They found few conserved amino acids, even within IgE-binding epitopes, and hypothesized that protein sequence similarity is not necessarily predictive of allergenicity.…”

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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Ana o 1, a cashew (Anacardium occidental) allergen of the vicilin seed storage protein family

Cited by 159 publications

References 35 publications

Systematic review on cashew nut allergy

Systematic review on cashew nut allergy

Treatment of cashew extracts with Aspergillopepsin reduces IgE binding to cashew allergens

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

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