Pistachio Allergy-Prevalence and In vitro Cross-Reactivity with Other Nuts

Noorbakhsh, Reihaneh; Mortazavi, Seyed Ali; Sankian, Mojtaba; Shahidi, Fakhri; Tehrani, Mohsen; Azad, Farahzad Jabbari; Behmanesh, Fatemeh; Varasteh, Abdolreza

doi:10.2332/allergolint.10-oa-0222

Cited by 43 publications

(41 citation statements)

References 22 publications

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“…SDS-PAGE profile of TSPPN reveals 5 major protein bands with approximate molecular weights of 56, 31, 26, 24, and 13 kDa ( Figure 1). This protein profile was consistent with those obtained by Noorbakhsh et al (2011). According to Shokraii and Esen (1988), majority of the proteins from pistachio nut are globulins amounting to 66.0%, followed by albumins, glutelins, and prolamins, amounting to 25.0, 7.3, and 2.0%, respectively.…”

Section: Resultssupporting

confidence: 88%

Extraction And Characterization of Bioactive Peptides Derived from the Hydrolysates of Total Soluble Proteins of Pistachio Nuts (Pistacia vera L.)

Dumandan

Angelica

Belina-Aldemita

et al. 2014

KIMIKA

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This study explored the potential of pistachio nut (Pistacia vera L.) total soluble proteins to release bioactive peptides exhibiting angiotensin-converting enzyme (ACE) inhibition, antioxidative, and antibacterial activities. The total soluble proteins were extracted from the ground, defatted nut using 0.010 M phosphate buffered saline, pH 6.8. The extracted proteins were hydrolyzed at different time intervals using trypsin and chymotrypsin. Hydrolysates of the total soluble proteins at 24 h digestion time exhibited the highest ACE-inhibition activity of 76.67 ± 0.10% and 70.83 ± 0.00% for chymotrypsin and trypsin digestion, respectively. The 24 h enzymatic hydrolysates were further fractionated in RP-HPLC using a C18 Vydac column. The C1 fraction from the 24 h chymotryptic hydrolysates and T2 from the 24 h tryptic hydrolysates exhibited the highest ACEinhibition activities with an IC50 value of 147.7 ± 0.8 and 148.7 ± 0.6 µg/mL, respectively. The 24 h chymotryptic and tryptic hydrolysates also exhibited a DPPH radical scavenging activity of 83.7 ± 1.1% (EC50 = 356.5 ± 1.0 μg/mL) and 80.4 ± 0.2% (EC50 = 402.7 ± 1.1 μg/mL), respectively. The hydroxyl radical scavenging activities of the 24 h chymotryptic and tryptic hydrolysates were found to be 22.8 ± 1.0 and 16.6 ± 3.7%, respectively. However, the 24 h tryptic and chymotryptic hydrolysates did not exhibit any antibacterial activity against the gram-negative Escherichia coli and grampositive Staphylococcus aureus. Therefore, the total soluble proteins of pistachio nuts were found to contain peptides exhibiting ACE-inhibition and antioxidative activities upon hydrolysis with trypsin and chymotrypsin.

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Section: Resultssupporting

confidence: 88%

Extraction And Characterization of Bioactive Peptides Derived from the Hydrolysates of Total Soluble Proteins of Pistachio Nuts (Pistacia vera L.)

Dumandan

Angelica

Belina-Aldemita

et al. 2014

KIMIKA

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“…A high degree of serological cross-reactivity has been established between cashew nut and pistachio (Pis v 1, Pis v 2 and Pis v 3) by sIgE-inhibition tests. This may be explained by the highly conserved primary and three-dimensional structure of these allergen homologue pairs, present in both cashew nut and pistachio (18)(19)(20)(21)(22) (2,3,19,22,(25)(26)(27). Sensitization against cashew nut allergy seems to be a primary sensitization rather than a cross-reaction between cashew nuts and pollens.…”

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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“…Cross-sensitisation between cashew and other tree nuts, such as hazelnut and walnut has been reported at IgE level [12-15] as well as at T-cell level [16, 17] where mostly Ana o 1 and Ana o 2 acted as cross-reacting allergens [16]. Amongst Anacardiaceae members, allergic cross-reactivity between pistachio and cashew nut is well recognised [12, 15, 18-21] and avoidance of both nuts is advised in case of a confirmed cashew nut allergy [22].…”

Section: Introductionmentioning

confidence: 99%

“…Amongst Anacardiaceae members, allergic cross-reactivity between pistachio and cashew nut is well recognised [12, 15, 18-21] and avoidance of both nuts is advised in case of a confirmed cashew nut allergy [22]. The strong phylogenetic relationship between cashew and pistachio nut is reflected by the high amino acid similarity and conserved three-dimensional regions between the cashew nut and pistachio seed storage allergens Ana o 1/Pis v 3 (7S vicilin), Ana o 2/Pis v 2 (11S legumin), and Ana o 3/Pis v 1 (2S albumin) with a similarity of 78, 80, and 70%, respectively [15, 20, 23]. …”

Section: Introductionmentioning

confidence: 99%

IgE Cross-Reactivity of Cashew Nut Allergens

Bastiaan‐Net

Reitsma

Cordewener

et al. 2018

Int Arch Allergy Immunol

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Background: Allergic sensitisation towards cashew nut often happens without a clear history of eating cashew nut. IgE cross-reactivity between cashew and pistachio nut is well described; however, the ability of cashew nut-specific IgE to cross-react to common tree nut species and other Anacardiaceae, like mango, pink peppercorn, or sumac is largely unknown. Objectives: Cashew nut allergic individuals may cross-react to foods that are phylogenetically related to cashew. We aimed to determine IgE cross-sensitisation and cross-reactivity profiles in cashew nut-sensitised subjects, towards botanically related proteins of other Anacardiaceae family members and related tree nut species. Method: Sera from children with a suspected cashew nut allergy (n = 56) were assessed for IgE sensitisation to common tree nuts, mango, pink peppercorn, and sumac using dot blot technique. Allergen cross-reactivity patterns between Anacardiaceae species were subsequently examined by SDS-PAGE and immunoblot inhibition, and IgE-reactive allergens were identified by LC-MS/MS. Results: From the 56 subjects analysed, 36 were positive on dot blot for cashew nut (63%). Of these, 50% were mono-sensitised to cashew nuts, 19% were co-sensitised to Anacardiaceae species, and 31% were co-sensitised to tree nuts. Subjects co-sensitised to Anacardiaceae species displayed a different allergen recognition pattern than subjects sensitised to common tree nuts. In pink peppercorn, putative albumin- and legumin-type seed storage proteins were found to cross-react with serum of cashew nut-sensitised subjects in vitro. In addition, a putative luminal binding protein was identified, which, among others, may be involved in cross-reactivity between several Anacardiaceae species. Conclusions: Results demonstrate the in vitro presence of IgE cross-sensitisation in children towards multiple Anacardiaceae species. In this study, putative novel allergens were identified in cashew, pistachio, and pink peppercorn, which may pose factors that underlie the observed cross-sensitivity to these species. The clinical relevance of this widespread cross-sensitisation is unknown.

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Pistachio Allergy-Prevalence and In vitro Cross-Reactivity with Other Nuts

Cited by 43 publications

References 22 publications

Extraction And Characterization of Bioactive Peptides Derived from the Hydrolysates of Total Soluble Proteins of Pistachio Nuts (Pistacia vera L.)

Extraction And Characterization of Bioactive Peptides Derived from the Hydrolysates of Total Soluble Proteins of Pistachio Nuts (Pistacia vera L.)

Systematic review on cashew nut allergy

IgE Cross-Reactivity of Cashew Nut Allergens

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