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

Detalhes bibliográficos
Autor(a) principal: Abram, Debora Moitinho
Data de Publicação: 2020
Outros Autores: Fernandes, Luis Gustavo Romani, Perez-Riverol, Amilcar [UNESP], Regina Brochetto-Braga, Marcia [UNESP], Zollner, Ricardo de Lima
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.3390/toxins12100649
http://hdl.handle.net/11449/209613
Resumo: 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.
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spelling Cross-Reactive Carbohydrate Determinant in Apis mellifera, Solenopsis invicta and Polybia paulista Venoms: Identification of Allergic Sensitization and Cross-ReactivityHymenoptera venom allergycross-reactive carbohydratePolybia paulistabromelainAllergic 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.Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Univ Campinas UNICAMP, Lab Translat Immunol, Med Sch, FCM, Rua Tessalia Vieira Camargo 126, BR-13500 Campinas, SP, BrazilSao Paulo State Univ, Inst Biosci Rio Claro, Inst Biosci Rio Claro, Ctr Study Social Insects,Dept Gen & Appl Biol, BR-13500 Rio Claro, SP, BrazilSao Paulo State Univ, Inst Biosci Rio Claro, Inst Biosci Rio Claro, Ctr Study Social Insects,Dept Gen & Appl Biol, BR-13500 Rio Claro, SP, BrazilCNPq: 455422/2014-1FAPESP: 2019/00729-7CAPES: 02P-4636-2019MdpiUniversidade Estadual de Campinas (UNICAMP)Universidade Estadual Paulista (Unesp)Abram, Debora MoitinhoFernandes, Luis Gustavo RomaniPerez-Riverol, Amilcar [UNESP]Regina Brochetto-Braga, Marcia [UNESP]Zollner, Ricardo de Lima2021-06-25T12:23:53Z2021-06-25T12:23:53Z2020-10-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article18http://dx.doi.org/10.3390/toxins12100649Toxins. Basel: Mdpi, v. 12, n. 10, 18 p., 2020.http://hdl.handle.net/11449/20961310.3390/toxins12100649WOS:000585306600001Web of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengToxinsinfo:eu-repo/semantics/openAccess2021-10-23T19:28:17Zoai:repositorio.unesp.br:11449/209613Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462021-10-23T19:28:17Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Cross-Reactive Carbohydrate Determinant in Apis mellifera, Solenopsis invicta and Polybia paulista Venoms: Identification of Allergic Sensitization and Cross-Reactivity
title Cross-Reactive Carbohydrate Determinant in Apis mellifera, Solenopsis invicta and Polybia paulista Venoms: Identification of Allergic Sensitization and Cross-Reactivity
spellingShingle Cross-Reactive Carbohydrate Determinant in Apis mellifera, Solenopsis invicta and Polybia paulista Venoms: Identification of Allergic Sensitization and Cross-Reactivity
Abram, Debora Moitinho
Hymenoptera venom allergy
cross-reactive carbohydrate
Polybia paulista
bromelain
title_short Cross-Reactive Carbohydrate Determinant in Apis mellifera, Solenopsis invicta and Polybia paulista Venoms: Identification of Allergic Sensitization and Cross-Reactivity
title_full Cross-Reactive Carbohydrate Determinant in Apis mellifera, Solenopsis invicta and Polybia paulista Venoms: Identification of Allergic Sensitization and Cross-Reactivity
title_fullStr Cross-Reactive Carbohydrate Determinant in Apis mellifera, Solenopsis invicta and Polybia paulista Venoms: Identification of Allergic Sensitization and Cross-Reactivity
title_full_unstemmed Cross-Reactive Carbohydrate Determinant in Apis mellifera, Solenopsis invicta and Polybia paulista Venoms: Identification of Allergic Sensitization and Cross-Reactivity
title_sort Cross-Reactive Carbohydrate Determinant in Apis mellifera, Solenopsis invicta and Polybia paulista Venoms: Identification of Allergic Sensitization and Cross-Reactivity
author Abram, Debora Moitinho
author_facet Abram, Debora Moitinho
Fernandes, Luis Gustavo Romani
Perez-Riverol, Amilcar [UNESP]
Regina Brochetto-Braga, Marcia [UNESP]
Zollner, Ricardo de Lima
author_role author
author2 Fernandes, Luis Gustavo Romani
Perez-Riverol, Amilcar [UNESP]
Regina Brochetto-Braga, Marcia [UNESP]
Zollner, Ricardo de Lima
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual de Campinas (UNICAMP)
Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv Abram, Debora Moitinho
Fernandes, Luis Gustavo Romani
Perez-Riverol, Amilcar [UNESP]
Regina Brochetto-Braga, Marcia [UNESP]
Zollner, Ricardo de Lima
dc.subject.por.fl_str_mv Hymenoptera venom allergy
cross-reactive carbohydrate
Polybia paulista
bromelain
topic Hymenoptera venom allergy
cross-reactive carbohydrate
Polybia paulista
bromelain
description 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.
publishDate 2020
dc.date.none.fl_str_mv 2020-10-01
2021-06-25T12:23:53Z
2021-06-25T12:23:53Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.3390/toxins12100649
Toxins. Basel: Mdpi, v. 12, n. 10, 18 p., 2020.
http://hdl.handle.net/11449/209613
10.3390/toxins12100649
WOS:000585306600001
url http://dx.doi.org/10.3390/toxins12100649
http://hdl.handle.net/11449/209613
identifier_str_mv Toxins. Basel: Mdpi, v. 12, n. 10, 18 p., 2020.
10.3390/toxins12100649
WOS:000585306600001
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Toxins
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dc.publisher.none.fl_str_mv Mdpi
publisher.none.fl_str_mv Mdpi
dc.source.none.fl_str_mv Web of Science
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
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