Purification of rabies virus glycoprotein produced in Drosophila melanogaster S2 cells: An efficient immunoaffinity method

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dc.contributor.authorPilatti, Livia
dc.contributor.authorMancini Astray, Renato
dc.contributor.authorRocca, Mayra Pereira [UNESP]
dc.contributor.authorBarbosa, Flavia Ferreira
dc.contributor.authorJorge, Soraia Attie Calil
dc.contributor.authorButler, Michael
dc.contributor.authorde Fátima Pires Augusto, Elisabeth
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionButantan Institute
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionNational Institute for Biotechnology Research and Training (NIBRT)
dc.date.accessioned2020-12-12T01:32:57Z
dc.date.available2020-12-12T01:32:57Z
dc.date.issued2020-01-01
dc.description.abstractMost rabies vaccines are based on inactivated virus, which production process demands a high level of biosafety structures. In the past decades, recombinant rabies virus glycoprotein (RVGP) produced in several expression systems has been extensively studied to be used as an alternative vaccine. The immunogenic characteristics of this protein depend on its correct conformation, which is present only after the correct post-translational modifications, typically performed by animal cells. The main challenge of using this protein as a vaccine candidate is to keep its trimeric conformation after the purification process. We describe here a new immunoaffinity chromatography method using a monoclonal antibody for RVGP Site II for purification of recombinant rabies virus glycoprotein expressed on the membrane of Drosophila melanogaster S2 cells. RVGP recovery achieved at least 93%, and characterization analysis showed that the main antigenic proprieties were preserved after purification.en
dc.description.affiliationScience and Technology Institute Federal University of São Paulo (UNIFESP)
dc.description.affiliationViral Immunology Laboratory Butantan Institute
dc.description.affiliationMedical School São Paulo State University (UNESP)
dc.description.affiliationNational Institute for Biotechnology Research and Training (NIBRT)
dc.description.affiliationUnespMedical School São Paulo State University (UNESP)
dc.identifierhttp://dx.doi.org/10.1002/btpr.3046
dc.identifier.citationBiotechnology Progress.
dc.identifier.doi10.1002/btpr.3046
dc.identifier.issn1520-6033
dc.identifier.issn8756-7938
dc.identifier.scopus2-s2.0-85088783947
dc.identifier.urihttp://hdl.handle.net/11449/199182
dc.language.isoeng
dc.relation.ispartofBiotechnology Progress
dc.sourceScopus
dc.subjectDrosophila melanogaster S2 cells
dc.subjectimmunoaffinity purification
dc.subjectinsect cells
dc.subjectrabies virus glycoprotein
dc.titlePurification of rabies virus glycoprotein produced in Drosophila melanogaster S2 cells: An efficient immunoaffinity methoden
dc.typeArtigo
unesp.author.orcid0000-0003-4306-5413[1]
unesp.author.orcid0000-0002-6983-5298[2]
unesp.author.orcid0000-0001-9380-1023[5]
unesp.author.orcid0000-0002-4907-3652[6]
unesp.author.orcid0000-0003-0417-5580[7]

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