Reactivity of IgE to the allergen hyaluronidase from Polybia paulista (Hymenoptera, Vespidae) venom

dc.creatorJacomini, DLJ
dc.creatorMoreira, SMG
dc.creatorPereira, FDC
dc.creatorZollner, RD
dc.creatorBraga, MRB
dc.date2014
dc.dateMAY
dc.date2014-07-30T14:19:35Z
dc.date2015-11-26T17:41:08Z
dc.date2014-07-30T14:19:35Z
dc.date2015-11-26T17:41:08Z
dc.date.accessioned2018-03-29T00:22:53Z
dc.date.available2018-03-29T00:22:53Z
dc.identifierToxicon. Pergamon-elsevier Science Ltd, v. 82, n. 104, n. 111, 2014.
dc.identifier0041-0101
dc.identifierWOS:000335281300012
dc.identifier10.1016/j.toxicon.2014.02.016
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/58947
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/58947
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1286922
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionTo date, there are no allergenic extracts or components available in Brazil to diagnosis and treatment of patients with venom allergy from social wasp (Vespidae Family; Polistinae Subfamily) despite of the great number of existing species. We evaluated the immunogenic potential of the Hyal recombinant protein (Pp-Hyal-rec) which was expressed in an insoluble form in comparison with the allergenic native protein (Pp-Hyal-nat) for recognition of immunoglobulin E (IgE).in the serum of allergic patients to venom of the endemic social wasp Polybia paulista from Sao Paulo State, Brazil. Hyal cDNA from the venom of the social wasp P. paulista (Pp-Hyal) (GI: 302201582) was cloned into the expression vector pET-28a in Escherichia coli DE3 (BL21) cells. Solubilization and purification of Pp-Hyal-rec from inclusion bodies were performed using Ni2+ affinity chromatography (Ni-NTA-Agarose) under denaturing conditions. Both the native (Pp-Hyal-nat) and the recombinant (Pp-Hyal-rec) purified allergens were used for Western blotting to assess the levels of Pp-Hyal-IgE specific in the serum of 10 patients exclusively reactive to the venom of the social wasp P. paulista. The immune sera specifically recognized the band corresponding to the Pp-Hyal-rec protein (40 kDa) at a higher intensity than the native allergen (39 kDa). The sera recognized other proteins in P. paulista crude venom extract to a lesser extent, likely corresponding to other venom allergens such as phospholipase (34 kDa), Antigen 5 (25 kDa), and proteases. The recognition pattern of the immune sera to the Pp-Hyal-rec allergen strongly suggests that this recombinant antigen could be used for developing a diagnostic allergy test as well as for specific immunotherapy (IT). (C) 2014 Elsevier Ltd. All rights reserved.
dc.description82
dc.description104
dc.description111
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionUniv Estadual de Campinas-UNICAMP, [2006/54810]
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionFAPESP [2009/51539-1]
dc.descriptionUniv Estadual de Campinas-UNICAMP, [2006/54810]
dc.languageen
dc.publisherPergamon-elsevier Science Ltd
dc.publisherOxford
dc.publisherInglaterra
dc.relationToxicon
dc.relationToxicon
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectPolybia paulista
dc.subjectVenom
dc.subjectAllergen
dc.subjectRecombinant hyaluronidase
dc.subjectImmunoglobulin E (IgE)
dc.subjectCross-immunoreactivity
dc.subjectAntigenic Cross-reactivity
dc.subjectInsect Stings
dc.subjectWasp
dc.subjectImmunotherapy
dc.subjectProtein
dc.subjectHypersensitivity
dc.subjectPurification
dc.subjectPopulation
dc.subjectPrevalence
dc.subjectBee
dc.titleReactivity of IgE to the allergen hyaluronidase from Polybia paulista (Hymenoptera, Vespidae) venom
dc.typeArtículos de revistas


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