Purification of rabies virus glycoprotein produced inDrosophila melanogasterS2cells: An efficient immunoaffinity method

Autor(es)

Pilatti, Livia ^{[1, 2]} ; Mancini Astray, Renato ^[1] ; Rocca, Mayra Pereira ^[3] ; Barbosa, Flavia Ferreira ^[1] ; Jorge, Soraia Attie Calil ^[1] ; Butler, Michael ^[4] ; de Fatima Pires Augusto, Elisabeth ^[2]

Afiliação do(s) autor(es)

^[1] Butantan Inst, Viral Immunol Lab, Sao Paulo, SP - Brazil

^[2] Fed Univ Sao Paulo UNIFESP, Sci & Technol Inst, Sao Jose Dos Campos, SP - Brazil

^[3] Sao Paulo State Univ UNESP, Med Sch, Botucatu, SP - Brazil

^[4] Natl Inst Biotechnol Res & Training NIBRT, Dublin - Ireland

• Tipo de documento: Artigo Científico
• Fonte: BIOTECHNOLOGY PROGRESS; v. 36, n. 6 AUG 2020.
• Citações Web of Science: 0

Resumo

Most 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 ofDrosophila melanogasterS2 cells. RVGP recovery achieved at least 93%, and characterization analysis showed that the main antigenic proprieties were preserved after purification. (AU)

• Processo FAPESP: 18/10538-1 - Caracterização de antígenos recombinantes e da resposta imune para um novo candidato vacinal contra a raiva
• Beneficiário: Renato Mancini Astray
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 12/24647-0 - Purificação e caracterização da glicoproteína do vírus da raiva produzida pelos sistemas S2 (Drosophila melanogaster) e Semliki Forest Vírus recombinante
• Beneficiário: Renato Mancini Astray
• Modalidade de apoio: Auxílio à Pesquisa - Regular