Molecular Cloning and Characterization of Hazel Pollen Protein (70 kD) as a Luminal Binding Protein (BiP): A Novel Cross-Reactive Plant Allergen

Gruehn, Sabine; Suphioglu, Cenk; O’Hehir, Robyn E; Volkmann, Dieter

doi:10.1159/000070924

Cited by 33 publications

(26 citation statements)

References 25 publications

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“…The absence of vicilin-sIgE in these patients could explain the observed low co-sensitisation to other tree nuts, as Ana o 1 is deemed to be the responsible cross-reactive factor between different tree nuts [12-16]. Surprisingly, ribulose-1,5-bisphosphate carboxylase oxygenase (rubisco) in cashew nut, pistachio and pink peppercorn protein fractions was specifically detectable by this patient group I. Additionally, for these same patients peptide homologs of the cross-reactive luminal BiP from C. avellana pollen [46] were recovered from the ca. 73–76 kDa IgE-reactive protein bands in cashew and pistachio nut.…”

Section: Discussionmentioning

confidence: 96%

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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Section: Discussionmentioning

confidence: 96%

IgE Cross-Reactivity of Cashew Nut Allergens

Bastiaan‐Net

Reitsma

Cordewener

et al. 2018

Int Arch Allergy Immunol

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“…The presence of luminal-binding protein Cor a 10, which was described as minor allergen in hazel pollen, has not been shown for birch or other Fagales species [21]. In the single reference [21] on this type of allergen, a probable cross-reactivity to a 70-kDa band in birch extract was indicated, which thus does not disprove the suggested group formation. Furthermore, the relevance of this protein family as allergens appears to be very limited.…”

Section: Tree Pollenmentioning

confidence: 96%

“…Birch pollen extract completely inhibited human IgE binding to alder, hornbeam and oak, whereas the reverse inhibition of IgE binding to birch pollen extract by the mentioned extracts was incomplete [15]. The presence of luminal-binding protein Cor a 10, which was described as minor allergen in hazel pollen, has not been shown for birch or other Fagales species [21]. In the single reference [21] on this type of allergen, a probable cross-reactivity to a 70-kDa band in birch extract was indicated, which thus does not disprove the suggested group formation.…”

Section: Tree Pollenmentioning

confidence: 99%

The Principle of Homologous Groups in Regulatory Affairs of Allergen Products – A Proposal

Lorenz

Lüttkopf

May

et al. 2008

Int Arch Allergy Immunol

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Among other legal regulations, the Note for Guidance on Allergen Products CPMP/BWP/243/96 released by the European Medicines Agency provides regulatory instructions regarding the quality of allergen extracts for diagnostic or therapeutic purposes. The current revision of this guideline intends to transform the so-called ‘principle of taxonomic families’ to the ‘principle of homologous groups’. According to this concept, the data of one allergen extract demonstrating stability, efficacy and safety can, to a limited extent, be extrapolated to other allergen extracts belonging to the same homologous groups. The present work proposes the formation of homologous groups for pollen species and animal-derived materials on the basis of similar biochemical composition and homology/cross-reactivity of allergens or allergen sources. Some tree pollen species could be assigned to three different homologous groups, some weed pollen species to one homologous group and numerous grass pollen species to one homologous group on condition that data rely on single defined representative species. A homologous group for mites is limited to the Dermatophagoides species and the grouping of vertebrate-derived materials such as dander could be possible under restrictions. The criteria for the formation of the proposed homologous groups are illustrated in detail to provide an opportunity for extending existing homologous groups by further species in case of new insights in allergens and cross-reactivity of allergen sources. In this way, the concept of homologous groups could serve as a dynamic tool in the regulation of allergen products.

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“…43 Luminal binding protein (BiP) is a highly conserved hazel pollen allergen (Cor a 10), which functions as a chaperone during protein synthesis, and is reported to be a cross-reactive pollen allergen. 44 BiP also shares a high degree of sequence homology to heat shock protein 70 (Hsp70), which has been reported as an allergen in many fungi. 45,46 Oxygen evolving enhancer protein was a prominent allergen in our analysis; however, there are no studies in the literature that currently report this protein to be an allergen.…”

Section: Discussionmentioning

confidence: 99%