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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Formato: | Artículo |
Lenguaje: | Inglés |
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Universidad de Belgrano - Facultad de Ciencias Exactas y Naturales - Proyectos de Investigación
2014
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Acceso en línea: | http://repositorio.ub.edu.ar/handle/123456789/2711 |
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I36-R142-123456789-2711 |
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institution |
Universidad de Belgrano |
institution_str |
I-36 |
repository_str |
R-142 |
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Repositorio Institucional - Universidad de Belgrano (UB) |
language |
Inglés |
topic |
Gag polyprotein Feline immunodeficiency virus In vitro assembly Lentiviruses Los lentivirus In vitro montaje poliproteína Gag virus de la inmunodeficiencia felina |
spellingShingle |
Gag polyprotein Feline immunodeficiency virus In vitro assembly Lentiviruses Los lentivirus In vitro montaje poliproteína Gag virus de la inmunodeficiencia felina Affranchino, José L. González, Silvia A. In vitro assembly of the feline immunodeficiency virus Gag polyprotein |
topic_facet |
Gag polyprotein Feline immunodeficiency virus In vitro assembly Lentiviruses Los lentivirus In vitro montaje poliproteína Gag virus de la inmunodeficiencia felina |
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. |
format |
Article |
author |
Affranchino, José L. González, Silvia A. |
author_facet |
Affranchino, José L. González, Silvia A. |
author_sort |
Affranchino, José L. |
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 |
publisher |
Universidad de Belgrano - Facultad de Ciencias Exactas y Naturales - Proyectos de Investigación |
publishDate |
2014 |
url |
http://repositorio.ub.edu.ar/handle/123456789/2711 |
work_keys_str_mv |
AT affranchinojosel invitroassemblyofthefelineimmunodeficiencyvirusgagpolyprotein AT gonzalezsilviaa invitroassemblyofthefelineimmunodeficiencyvirusgagpolyprotein |
bdutipo_str |
Repositorios |
_version_ |
1764820529223565314 |