Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA

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Human immunodeficiency virus type 1 (HIV-1) Gag selects for and mediates genomic RNA (vRNA) encapsidation into progeny virus particles. The host protein, Staufen1 interacts directly with Gag and is found in ribonucleoprotein (RNP) complexes containing vRNA, which provides evidence that Staufen1 play...

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Detalles Bibliográficos
Autores principales: Abrahamyan, L.G., Chatel-Chaix, L., Ajamian, L., Milev, M.P., Monette, A., Clément, J.-F., Song, R., Lehmann, M., DesGroseillers, L., Laughrea, M., Boccaccio, G., Mouland, A.J.
Formato: Artículo publishedVersion
Publicado: 2010
Materias:
AIDS
HIV-1
Intracellular traffic
Ribonucleoprotein
RNA encapsidation
SHRNP
sIRNA
Staufen1
Staufen1 HIV-1-dependent RNP
Virus-host interaction
Gag protein
genomic RNA
ribonucleoprotein
Staufen 1 ribonucleoprotein
unclassified drug
virus RNA
article
cell granule
cell level
cell stress
cellular distribution
controlled study
human
human cell
Human immunodeficiency virus 1
nonhuman
oxidative stress
polysome
priority journal
protein assembly
protein depletion
protein function
protein localization
virion
virus capsid
virus cell interaction
virus expression
Blotting, Western
Cell Line
Cytoplasmic Granules
Cytoskeletal Proteins
gag Gene Products, Human Immunodeficiency Virus
Hela Cells
Humans
Immunoprecipitation
In Situ Hybridization, Fluorescence
Models, Biological
Protein Binding
Reverse Transcriptase Polymerase Chain Reaction
Ribonucleoproteins
RNA, Viral
RNA-Binding Proteins
Virus Assembly
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00219533_v123_n3_p369_Abrahamyan
http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00219533_v123_n3_p369_Abrahamyan_oai
Aporte de:
Repositorio Digital de la Universidad de Buenos Aires (UBA) de Universidad de Buenos Aires
Descripción
Sumario:Human immunodeficiency virus type 1 (HIV-1) Gag selects for and mediates genomic RNA (vRNA) encapsidation into progeny virus particles. The host protein, Staufen1 interacts directly with Gag and is found in ribonucleoprotein (RNP) complexes containing vRNA, which provides evidence that Staufen1 plays a role in vRNA selection and encapsidation. In this work, we show that Staufen1, vRNA and Gag are found in the same RNP complex. These cellular and viral factors also colocalize in cells and constitute novel Staufen1 RNPs (SHRNPs) whose assembly is strictly dependent on HIV-1 expression. SHRNPs are distinct from stress granules and processing bodies, are preferentially formed during oxidative stress and are found to be in equilibrium with translating polysomes. Moreover, SHRNPs are stable, and the association between Staufen1 and vRNA was found to be evident in these and other types of RNPs. We demonstrate that following Staufen1 depletion, apparent supraphysiologic-sized SHRNP foci are formed in the cytoplasm and in which Gag, vRNA and the residual Staufen1 accumulate. The depletion of Staufen1 resulted in reduced Gag levels and deregulated the assembly of newly synthesized virions, which were found to contain several-fold increases in vRNA, Staufen1 and other cellular proteins. This work provides new evidence that Staufen1-containing HIV-1 RNPs preferentially form over other cellular silencing foci and are involved in assembly, localization and encapsidation of vRNA.

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