Functional and biochemical properties of Mal de Río Cuarto virus (Fijivirus, Reoviridae) P9-1 viroplasm protein show further similarities to animal reovirus counterparts

Mal de Río Cuarto virus (MRCV) is a plant virus of the genus Fijivirus within the family Reoviridae that infects several monocotyledonous species and is transmitted by planthoppers in a persistent and propagative manner. Other members of the family replicate in viral inclusion bodies (VIBs) termed v...

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Autores principales: Maroniche, Guillermo Andrés, Mongelli, Vanesa Claudia, Peralta, Andrea Veronica, Distefano, Ana Julia, Llauger, Gabriela, Taboga, Oscar Alberto, Hopp, Horacio Esteban, Del Vas, Mariana
Formato: info:ar-repo/semantics/artículo
Lenguaje:Inglés
Publicado: Elsevier 2023
Materias:
Acceso en línea:http://hdl.handle.net/20.500.12123/15341
https://www.sciencedirect.com/science/article/pii/S0168170210001942
https://doi.org/10.1016/j.virusres.2010.06.010
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author Maroniche, Guillermo Andrés
Mongelli, Vanesa Claudia
Peralta, Andrea Veronica
Distefano, Ana Julia
Llauger, Gabriela
Taboga, Oscar Alberto
Hopp, Horacio Esteban
Del Vas, Mariana
author_browse Del Vas, Mariana
Distefano, Ana Julia
Hopp, Horacio Esteban
Llauger, Gabriela
Maroniche, Guillermo Andrés
Mongelli, Vanesa Claudia
Peralta, Andrea Veronica
Taboga, Oscar Alberto
author_facet Maroniche, Guillermo Andrés
Mongelli, Vanesa Claudia
Peralta, Andrea Veronica
Distefano, Ana Julia
Llauger, Gabriela
Taboga, Oscar Alberto
Hopp, Horacio Esteban
Del Vas, Mariana
author_sort Maroniche, Guillermo Andrés
collection INTA Digital
description Mal de Río Cuarto virus (MRCV) is a plant virus of the genus Fijivirus within the family Reoviridae that infects several monocotyledonous species and is transmitted by planthoppers in a persistent and propagative manner. Other members of the family replicate in viral inclusion bodies (VIBs) termed viroplasms that are formed in the cytoplasm of infected plant and insect cells. In this study, the protein coded by the first ORF of MRCV segment S9 (P9-1) was shown to establish cytoplasmic inclusion bodies resembling viroplasms after transfection of Spodoptera frugiperda insect cells. In accordance, MRCV P9-1 self-associates giving rise to high molecular weight complexes when expressed in bacteria. Strong self-interaction was also evidenced by yeast two-hybrid assays. Furthermore, biochemical characterization showed that MRCV P9-1 bound single stranded RNA and had ATPase activity. Finally, the MRCV P9-1 region required for the formation of VIB-like structures was mapped to the protein carboxy-terminal half. This extensive functional and biochemical characterization of MRCV P9-1 revealed further similarities between plant and animal reovirus viroplasm proteins.
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spelling INTA153412023-09-27T14:23:00Z Functional and biochemical properties of Mal de Río Cuarto virus (Fijivirus, Reoviridae) P9-1 viroplasm protein show further similarities to animal reovirus counterparts Maroniche, Guillermo Andrés Mongelli, Vanesa Claudia Peralta, Andrea Veronica Distefano, Ana Julia Llauger, Gabriela Taboga, Oscar Alberto Hopp, Horacio Esteban Del Vas, Mariana Fijivirus Reovirus ssRNA viruses ATPase ATPasa Mal de Río Cuarto Virus Viroplasm Virus del mal de Río Cuarto Viroplasma Mal de Río Cuarto virus (MRCV) is a plant virus of the genus Fijivirus within the family Reoviridae that infects several monocotyledonous species and is transmitted by planthoppers in a persistent and propagative manner. Other members of the family replicate in viral inclusion bodies (VIBs) termed viroplasms that are formed in the cytoplasm of infected plant and insect cells. In this study, the protein coded by the first ORF of MRCV segment S9 (P9-1) was shown to establish cytoplasmic inclusion bodies resembling viroplasms after transfection of Spodoptera frugiperda insect cells. In accordance, MRCV P9-1 self-associates giving rise to high molecular weight complexes when expressed in bacteria. Strong self-interaction was also evidenced by yeast two-hybrid assays. Furthermore, biochemical characterization showed that MRCV P9-1 bound single stranded RNA and had ATPase activity. Finally, the MRCV P9-1 region required for the formation of VIB-like structures was mapped to the protein carboxy-terminal half. This extensive functional and biochemical characterization of MRCV P9-1 revealed further similarities between plant and animal reovirus viroplasm proteins. Instituto de Biotecnología Fil: Maroniche, Guillermo Andrés. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina Fil: Mongelli, Vanesa Claudia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina Fil: Peralta, Andrea Veronica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina Fil: Distefano, Ana Julia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina Fil: Distefano, Ana Julia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina Fil: Llauger, Gabriela. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina Fil: Llauger, Gabriela. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina Fil: Taboga, Oscar Alberto. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina Fil: Hopp, Horacio Esteban. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina Fil: Hopp, Horacio Esteban. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina Fil: Del Vas, Mariana. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina 2023-09-27T14:18:32Z 2023-09-27T14:18:32Z 2010-09 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://hdl.handle.net/20.500.12123/15341 https://www.sciencedirect.com/science/article/pii/S0168170210001942 1872-7492 https://doi.org/10.1016/j.virusres.2010.06.010 eng info:eu-repo/semantics/restrictedAccess http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) application/pdf Elsevier Virus Research 152 (1-2) : 96-103 (Septiembre 2010)
spellingShingle Fijivirus
Reovirus
ssRNA viruses
ATPase
ATPasa
Mal de Río Cuarto Virus
Viroplasm
Virus del mal de Río Cuarto
Viroplasma
Maroniche, Guillermo Andrés
Mongelli, Vanesa Claudia
Peralta, Andrea Veronica
Distefano, Ana Julia
Llauger, Gabriela
Taboga, Oscar Alberto
Hopp, Horacio Esteban
Del Vas, Mariana
Functional and biochemical properties of Mal de Río Cuarto virus (Fijivirus, Reoviridae) P9-1 viroplasm protein show further similarities to animal reovirus counterparts
title Functional and biochemical properties of Mal de Río Cuarto virus (Fijivirus, Reoviridae) P9-1 viroplasm protein show further similarities to animal reovirus counterparts
title_full Functional and biochemical properties of Mal de Río Cuarto virus (Fijivirus, Reoviridae) P9-1 viroplasm protein show further similarities to animal reovirus counterparts
title_fullStr Functional and biochemical properties of Mal de Río Cuarto virus (Fijivirus, Reoviridae) P9-1 viroplasm protein show further similarities to animal reovirus counterparts
title_full_unstemmed Functional and biochemical properties of Mal de Río Cuarto virus (Fijivirus, Reoviridae) P9-1 viroplasm protein show further similarities to animal reovirus counterparts
title_short Functional and biochemical properties of Mal de Río Cuarto virus (Fijivirus, Reoviridae) P9-1 viroplasm protein show further similarities to animal reovirus counterparts
title_sort functional and biochemical properties of mal de rio cuarto virus fijivirus reoviridae p9 1 viroplasm protein show further similarities to animal reovirus counterparts
topic Fijivirus
Reovirus
ssRNA viruses
ATPase
ATPasa
Mal de Río Cuarto Virus
Viroplasm
Virus del mal de Río Cuarto
Viroplasma
url http://hdl.handle.net/20.500.12123/15341
https://www.sciencedirect.com/science/article/pii/S0168170210001942
https://doi.org/10.1016/j.virusres.2010.06.010
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