A simplified strategy to package foreign proteins into baculovirus occlusion bodies without engineering the viral genome

Polyhedron envelope protein (PEP) is the major component of the calyx that surrounds the baculovirus occlusion body (OB). PEP has been associated with the stabilization and resistance of polyhedra in the environment. Due to the abundant levels of PEP in OBs, we decided to use this protein as a fusio...

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Detalles Bibliográficos
Autores principales: Fabre, María Laura, Masson, Tomás, Haase, Santiago, Ferrelli, María Leticia, Romanowski, Víctor
Formato: Articulo Preprint
Lenguaje:Inglés
Publicado: 2020
Materias:
Biología
AgMNPV
AcMNPV
Polyhedron envelope protein (PEP)
UFLAg-286
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/120503
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-120503
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Biología
AgMNPV
AcMNPV
Polyhedron envelope protein (PEP)
UFLAg-286
spellingShingle Biología
AgMNPV
AcMNPV
Polyhedron envelope protein (PEP)
UFLAg-286
Fabre, María Laura
Masson, Tomás
Haase, Santiago
Ferrelli, María Leticia
Romanowski, Víctor
A simplified strategy to package foreign proteins into baculovirus occlusion bodies without engineering the viral genome
topic_facet Biología
AgMNPV
AcMNPV
Polyhedron envelope protein (PEP)
UFLAg-286
description Polyhedron envelope protein (PEP) is the major component of the calyx that surrounds the baculovirus occlusion body (OB). PEP has been associated with the stabilization and resistance of polyhedra in the environment. Due to the abundant levels of PEP in OBs, we decided to use this protein as a fusion partner to redirect foreign proteins to baculovirus polyhedra. In this study we developed a strategy that involves the generation of a monoclonal transformed insect cell line expressing a protein of interest fused to the the Anticarsia gemmatalis multiple nucleopolyhedrovirus (AgMNPV) N-terminus of PEP that enables the packaging of foreign proteins into the OBs without generating a recombinant baculovirus. This proved to be an efficient platform that could be exploited to improve wild type baculovirus for their use as bioinsecticides without facing the concerns of releasing genetically modified DNA to the environment and bypassing the associated regulatory issues. We demonstrated, using immunological, proteomic and microscopy techniques, that the envelope of AgMNPV OBs can effectively trap chimeric proteins in an infected insect cell line expressing AgMNPV PEP fused to the enhanced green fluorescent protein (eGFP). Furthermore, packaging of chimeric PEP also took place with heterologous OBs such as those of Autographa californica multiple nucleopolyhedrovirus (AcMNPV), another group I alphabaculovirus.
format Articulo
Preprint
author Fabre, María Laura
Masson, Tomás
Haase, Santiago
Ferrelli, María Leticia
Romanowski, Víctor
author_facet Fabre, María Laura
Masson, Tomás
Haase, Santiago
Ferrelli, María Leticia
Romanowski, Víctor
author_sort Fabre, María Laura
title A simplified strategy to package foreign proteins into baculovirus occlusion bodies without engineering the viral genome
title_short A simplified strategy to package foreign proteins into baculovirus occlusion bodies without engineering the viral genome
title_full A simplified strategy to package foreign proteins into baculovirus occlusion bodies without engineering the viral genome
title_fullStr A simplified strategy to package foreign proteins into baculovirus occlusion bodies without engineering the viral genome
title_full_unstemmed A simplified strategy to package foreign proteins into baculovirus occlusion bodies without engineering the viral genome
title_sort simplified strategy to package foreign proteins into baculovirus occlusion bodies without engineering the viral genome
publishDate 2020
url http://sedici.unlp.edu.ar/handle/10915/120503
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