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

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade de São Paulo (USP)-
Autor(es): dc.contributorButantan Institute-
Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.contributorNational Institute for Biotechnology Research and Training (NIBRT)-
Autor(es): dc.creatorPilatti, Livia-
Autor(es): dc.creatorMancini Astray, Renato-
Autor(es): dc.creatorRocca, Mayra Pereira [UNESP]-
Autor(es): dc.creatorBarbosa, Flavia Ferreira-
Autor(es): dc.creatorJorge, Soraia Attie Calil-
Autor(es): dc.creatorButler, Michael-
Autor(es): dc.creatorde Fátima Pires Augusto, Elisabeth-
Data de aceite: dc.date.accessioned2022-02-22T00:26:41Z-
Data de disponibilização: dc.date.available2022-02-22T00:26:41Z-
Data de envio: dc.date.issued2020-12-11-
Data de envio: dc.date.issued2020-12-11-
Data de envio: dc.date.issued2019-12-31-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1002/btpr.3046-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/199182-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/199182-
Descrição: dc.descriptionMost 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.-
Descrição: dc.descriptionScience and Technology Institute Federal University of São Paulo (UNIFESP)-
Descrição: dc.descriptionViral Immunology Laboratory Butantan Institute-
Descrição: dc.descriptionMedical School São Paulo State University (UNESP)-
Descrição: dc.descriptionNational Institute for Biotechnology Research and Training (NIBRT)-
Descrição: dc.descriptionMedical School São Paulo State University (UNESP)-
Idioma: dc.languageen-
Relação: dc.relationBiotechnology Progress-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectDrosophila melanogaster S2 cells-
Palavras-chave: dc.subjectimmunoaffinity purification-
Palavras-chave: dc.subjectinsect cells-
Palavras-chave: dc.subjectrabies virus glycoprotein-
Título: dc.titlePurification of rabies virus glycoprotein produced in Drosophila melanogaster S2 cells: An efficient immunoaffinity method-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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