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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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
Lenguaje:	Inglés
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
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paperaa:paper_00219533_v123_n3_p369_Abrahamyan
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spelling	paperaa:paper_00219533_v123_n3_p369_Abrahamyan2023-06-12T16:43:02Z Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA J. Cell Sci. 2010;123(3):369-383 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. 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 Human immunodeficiency virus 1 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. Fil:Boccaccio, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2010 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion application/pdf eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00219533_v123_n3_p369_Abrahamyan
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
language	Inglés
orig_language_str_mv	eng
topic	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 Human immunodeficiency virus 1
spellingShingle	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 Human immunodeficiency virus 1 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. Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA
topic_facet	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 Human immunodeficiency virus 1
description	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.
format	Artículo Artículo publishedVersion
author	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.
author_facet	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.
author_sort	Abrahamyan, L.G.
title	Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA
title_short	Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA
title_full	Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA
title_fullStr	Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA
title_full_unstemmed	Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA
title_sort	novel staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of hiv-1 genomic rna
publishDate	2010
url	http://hdl.handle.net/20.500.12110/paper_00219533_v123_n3_p369_Abrahamyan
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Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA

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