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Cross-Reactive Carbohydrate Determinant in Apis mellifera, Solenopsis invicta and Polybia paulista Venoms: Identification of Allergic Sensitization and Cross-Reactivity

1
Laboratory of Translational Immunology, Medicine School, FCM, University of Campinas (UNICAMP), Rua Tessália Vieira de Camargo, nº 126, 13083-888, Cidade Universitária “Zeferino Vaz”, Campinas SP 13500, Brazil
2
Center for the Study of Social Insects, Department of General and Applied Biology, Institute of Biosciences of Rio Claro, Institute of Biosciences of Rio Claro, São Paulo State University, Rio Claro SP 13500, Brazil
*
Author to whom correspondence should be addressed.
Toxins 2020, 12(10), 649; https://doi.org/10.3390/toxins12100649
Received: 19 August 2020 / Revised: 1 October 2020 / Accepted: 2 October 2020 / Published: 8 October 2020
(This article belongs to the Section Animal Venoms)
Allergic reactions to Hymenoptera venom, which could lead to systemic and even fatal symptoms, is characterized by hypersensitivity reactions mediated by specific IgE (sIgE) driven to venom allergens. Patients multisensitized to sIgE usually recognize more than one allergen in different Hymenoptera species. However, the presence of sIgE directed against Cross-Reactive Carbohydrate Determinant (CCD), which occurs in some allergens from Hymenoptera venom, hampers the identification of the culprit insects. CCD is also present in plants, pollen, fruits, but not in mammals. Bromelain (Brl) extracted from pineapples is a glycoprotein commonly used for reference to sIgE-CCD detection and analysis. In sera of fifty-one Hymenoptera allergic patients with specific IgE ≥ 1.0 KU/L, we assessed by immunoblotting the reactivity of sIgE to the major allergens of Apis mellifera, Polybia paulista and Solenopsis invicta venoms. We also distinguished, using sera adsorption procedures, the cases of CCD cross-reaction using Brl as a marker and inhibitor of CCD epitopes. The presence of reactivity for bromelain (24–28 kDa) was obtained in 43% of the patients, in which 64% presented reactivity for more than one Hymenoptera venom in radioallergosorbent (RAST) tests, and 90% showed reactivity in immunoblot analysis to the major allergens of Apis mellifera, Polybia paulista and Solenopsis invicta venoms. Sera adsorption procedures with Brl lead to a significant reduction in patients’ sera reactivity to the Hymenoptera allergens. Immunoblotting assay using pre- and post-Brl adsorption sera from wasp-allergic patients blotted with non-glycosylated recombinant antigens (rPoly p1, rPoly p5) from Polybia paulista wasp venom showed no change in reactivity pattern of sIgE that recognize allergen peptide epitopes. Our results, using Brl as a marker and CCD inhibitor to test sIgE reactivity, suggest that it could complement diagnostic methods and help to differentiate specific reactivity to allergens’ peptide epitopes from cross-reactivity caused by CCD, which is extremely useful in clinical practice. View Full-Text
Keywords: Keywords; Hymenoptera venom allergy; cross-reactive carbohydrate; Polybia paulista; bromelain Keywords; Hymenoptera venom allergy; cross-reactive carbohydrate; Polybia paulista; bromelain
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Abram, D.M.; Fernandes, L.G.R.; Perez-Riverol, A.; Regina Brochetto-Braga, M.; Zollner, R.L. Cross-Reactive Carbohydrate Determinant in Apis mellifera, Solenopsis invicta and Polybia paulista Venoms: Identification of Allergic Sensitization and Cross-Reactivity. Toxins 2020, 12, 649.

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