In vitro assembly of the feline immunodeficiency virus Gag polyprotein

The retroviral Gag protein is the only viral product that is necessary for the assembly of virions in mammalian cells. We have established an in vitro assembly system to study the assembly properties of purified feline immunodeficiency virus (FIV) Gag protein expressed in bacteria. Under fully defin...

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Autores principales:	Affranchino, José Luis, González, Silvia Adriana
Publicado:	2010
Materias:	Feline immunodeficiency virus Gag polyprotein In vitro assembly Lentiviruses RNA triton x 100 unclassified drug virus protein amino acid substitution article controlled study in vitro study nonhuman particle size priority journal protein assembly protein domain protein expression RNA binding virion virus inhibition virus nucleocapsid virus particle Amino Acid Substitution Detergents Escherichia coli Gene Products, gag Immunodeficiency Virus, Feline Mutagenesis, Site-Directed Octoxynol Recombinant Proteins RNA, Viral RNA-Binding Proteins Virion Virus Assembly Mammalia
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01681702_v150_n1-2_p153_Affranchino http://hdl.handle.net/20.500.12110/paper_01681702_v150_n1-2_p153_Affranchino
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_01681702_v150_n1-2_p153_Affranchino
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spelling	paper:paper_01681702_v150_n1-2_p153_Affranchino2023-06-08T15:17:38Z In vitro assembly of the feline immunodeficiency virus Gag polyprotein Affranchino, José Luis González, Silvia Adriana Feline immunodeficiency virus Gag polyprotein In vitro assembly Lentiviruses Gag polyprotein RNA triton x 100 unclassified drug virus protein amino acid substitution article controlled study Feline immunodeficiency virus in vitro study nonhuman particle size priority journal protein assembly protein domain protein expression RNA binding virion virus inhibition virus nucleocapsid virus particle Amino Acid Substitution Detergents Escherichia coli Gene Products, gag Immunodeficiency Virus, Feline Mutagenesis, Site-Directed Octoxynol Recombinant Proteins RNA, Viral RNA-Binding Proteins Virion Virus Assembly Feline immunodeficiency virus Mammalia The retroviral Gag protein is the only viral product that is necessary for the assembly of virions in mammalian cells. We have established an in vitro assembly system to study the assembly properties of purified feline immunodeficiency virus (FIV) Gag protein expressed in bacteria. Under fully defined conditions, the FIV Gag protein assembles into spherical particles of 33. nm in diameter which are morphologically similar to authentic immature particles, albeit smaller than virions. The in vitro assembly of FIV Gag into particles was found to be resistant to the addition of Triton X-100 and required the presence of RNA. Notably, we found that an amino acid substitution in the nucleocapsid domain of Gag that impairs RNA binding and blocks virion production in vivo, also abrogates Gag assembly in vitro. The development of an in vitro assembly system for FIV Gag protein will facilitate the study of the mechanisms by which this protein assembles into immature particles. © 2010 Elsevier B.V. Fil:Affranchino, J.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:González, S.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2010 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01681702_v150_n1-2_p153_Affranchino http://hdl.handle.net/20.500.12110/paper_01681702_v150_n1-2_p153_Affranchino
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Feline immunodeficiency virus Gag polyprotein In vitro assembly Lentiviruses Gag polyprotein RNA triton x 100 unclassified drug virus protein amino acid substitution article controlled study Feline immunodeficiency virus in vitro study nonhuman particle size priority journal protein assembly protein domain protein expression RNA binding virion virus inhibition virus nucleocapsid virus particle Amino Acid Substitution Detergents Escherichia coli Gene Products, gag Immunodeficiency Virus, Feline Mutagenesis, Site-Directed Octoxynol Recombinant Proteins RNA, Viral RNA-Binding Proteins Virion Virus Assembly Feline immunodeficiency virus Mammalia
spellingShingle	Feline immunodeficiency virus Gag polyprotein In vitro assembly Lentiviruses Gag polyprotein RNA triton x 100 unclassified drug virus protein amino acid substitution article controlled study Feline immunodeficiency virus in vitro study nonhuman particle size priority journal protein assembly protein domain protein expression RNA binding virion virus inhibition virus nucleocapsid virus particle Amino Acid Substitution Detergents Escherichia coli Gene Products, gag Immunodeficiency Virus, Feline Mutagenesis, Site-Directed Octoxynol Recombinant Proteins RNA, Viral RNA-Binding Proteins Virion Virus Assembly Feline immunodeficiency virus Mammalia Affranchino, José Luis González, Silvia Adriana In vitro assembly of the feline immunodeficiency virus Gag polyprotein
topic_facet	Feline immunodeficiency virus Gag polyprotein In vitro assembly Lentiviruses Gag polyprotein RNA triton x 100 unclassified drug virus protein amino acid substitution article controlled study Feline immunodeficiency virus in vitro study nonhuman particle size priority journal protein assembly protein domain protein expression RNA binding virion virus inhibition virus nucleocapsid virus particle Amino Acid Substitution Detergents Escherichia coli Gene Products, gag Immunodeficiency Virus, Feline Mutagenesis, Site-Directed Octoxynol Recombinant Proteins RNA, Viral RNA-Binding Proteins Virion Virus Assembly Feline immunodeficiency virus Mammalia
description	The retroviral Gag protein is the only viral product that is necessary for the assembly of virions in mammalian cells. We have established an in vitro assembly system to study the assembly properties of purified feline immunodeficiency virus (FIV) Gag protein expressed in bacteria. Under fully defined conditions, the FIV Gag protein assembles into spherical particles of 33. nm in diameter which are morphologically similar to authentic immature particles, albeit smaller than virions. The in vitro assembly of FIV Gag into particles was found to be resistant to the addition of Triton X-100 and required the presence of RNA. Notably, we found that an amino acid substitution in the nucleocapsid domain of Gag that impairs RNA binding and blocks virion production in vivo, also abrogates Gag assembly in vitro. The development of an in vitro assembly system for FIV Gag protein will facilitate the study of the mechanisms by which this protein assembles into immature particles. © 2010 Elsevier B.V.
author	Affranchino, José Luis González, Silvia Adriana
author_facet	Affranchino, José Luis González, Silvia Adriana
author_sort	Affranchino, José Luis
title	In vitro assembly of the feline immunodeficiency virus Gag polyprotein
title_short	In vitro assembly of the feline immunodeficiency virus Gag polyprotein
title_full	In vitro assembly of the feline immunodeficiency virus Gag polyprotein
title_fullStr	In vitro assembly of the feline immunodeficiency virus Gag polyprotein
title_full_unstemmed	In vitro assembly of the feline immunodeficiency virus Gag polyprotein
title_sort	in vitro assembly of the feline immunodeficiency virus gag polyprotein
publishDate	2010
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01681702_v150_n1-2_p153_Affranchino http://hdl.handle.net/20.500.12110/paper_01681702_v150_n1-2_p153_Affranchino
work_keys_str_mv	AT affranchinojoseluis invitroassemblyofthefelineimmunodeficiencyvirusgagpolyprotein AT gonzalezsilviaadriana invitroassemblyofthefelineimmunodeficiencyvirusgagpolyprotein
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In vitro assembly of the feline immunodeficiency virus Gag polyprotein

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