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

Autores
Abrahamyan, Levon G.; Chatel Chaix, Laurent; Ajamian, Lara; Milev, Miroslav P.; Monette, Anne; Clément, Jean François; Song, Rujun; Lehmann, Martin; DesGroseillers, Luc; Laughrea, Michael; Boccaccio, Graciela Lidia; Mouland, Andrew J.
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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: Abrahamyan, Levon G.. Davis Jewish General Hospital; Canadá
Fil: Chatel Chaix, Laurent. Davis Jewish General Hospital; Canadá
Fil: Ajamian, Lara. Mc Gill University; Canadá. Davis Jewish General Hospital; Canadá
Fil: Milev, Miroslav P.. Mc Gill University; Canadá. Davis Jewish General Hospital; Canadá
Fil: Monette, Anne. Mc Gill University; Canadá. Davis Jewish General Hospital; Canadá
Fil: Clément, Jean François. Davis Jewish General Hospital; Canadá
Fil: Song, Rujun. Mc Gill University; Canadá. Davis Jewish General Hospital; Canadá
Fil: Lehmann, Martin. Davis Jewish General Hospital; Canadá
Fil: DesGroseillers, Luc. University Of Montreal; Canadá
Fil: Laughrea, Michael. Mc Gill University; Canadá. Davis Jewish General Hospital; Canadá
Fil: Boccaccio, Graciela Lidia. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina
Fil: Mouland, Andrew J.. Mc Gill University; Canadá. Davis Jewish General Hospital; Canadá
Materia
HIV
Staufen
Stress Granule
capside
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/15285
Acceder
id CONICETDig_551fb9c1bf3261ca5c555b19b652f1dc
oai_identifier_str oai:ri.conicet.gov.ar:11336/15285
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNAAbrahamyan, Levon G.Chatel Chaix, LaurentAjamian, LaraMilev, Miroslav P.Monette, AnneClément, Jean FrançoisSong, RujunLehmann, MartinDesGroseillers, LucLaughrea, MichaelBoccaccio, Graciela LidiaMouland, Andrew J.HIVStaufenStress Granulecapsidehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Human 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: Abrahamyan, Levon G.. Davis Jewish General Hospital; CanadáFil: Chatel Chaix, Laurent. Davis Jewish General Hospital; CanadáFil: Ajamian, Lara. Mc Gill University; Canadá. Davis Jewish General Hospital; CanadáFil: Milev, Miroslav P.. Mc Gill University; Canadá. Davis Jewish General Hospital; CanadáFil: Monette, Anne. Mc Gill University; Canadá. Davis Jewish General Hospital; CanadáFil: Clément, Jean François. Davis Jewish General Hospital; CanadáFil: Song, Rujun. Mc Gill University; Canadá. Davis Jewish General Hospital; CanadáFil: Lehmann, Martin. Davis Jewish General Hospital; CanadáFil: DesGroseillers, Luc. University Of Montreal; CanadáFil: Laughrea, Michael. Mc Gill University; Canadá. Davis Jewish General Hospital; CanadáFil: Boccaccio, Graciela Lidia. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; ArgentinaFil: Mouland, Andrew J.. Mc Gill University; Canadá. Davis Jewish General Hospital; CanadáCompany Of Biologists2010-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/15285Abrahamyan, Levon G.; Chatel Chaix, Laurent; Ajamian, Lara; Milev, Miroslav P.; Monette, Anne; et al.; Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA; Company Of Biologists; Journal Of Cell Science; 123; Pte 3; 2-2010; 369-3831477-9137enginfo:eu-repo/semantics/altIdentifier/url/http://jcs.biologists.org/content/123/3/369.longinfo:eu-repo/semantics/altIdentifier/doi/10.1242/jcs.055897info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:12:08Zoai:ri.conicet.gov.ar:11336/15285instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:12:08.928CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA
title Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA
spellingShingle Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA
Abrahamyan, Levon G.
HIV
Staufen
Stress Granule
capside
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
dc.creator.none.fl_str_mv Abrahamyan, Levon G.
Chatel Chaix, Laurent
Ajamian, Lara
Milev, Miroslav P.
Monette, Anne
Clément, Jean François
Song, Rujun
Lehmann, Martin
DesGroseillers, Luc
Laughrea, Michael
Boccaccio, Graciela Lidia
Mouland, Andrew J.
author Abrahamyan, Levon G.
author_facet Abrahamyan, Levon G.
Chatel Chaix, Laurent
Ajamian, Lara
Milev, Miroslav P.
Monette, Anne
Clément, Jean François
Song, Rujun
Lehmann, Martin
DesGroseillers, Luc
Laughrea, Michael
Boccaccio, Graciela Lidia
Mouland, Andrew J.
author_role author
author2 Chatel Chaix, Laurent
Ajamian, Lara
Milev, Miroslav P.
Monette, Anne
Clément, Jean François
Song, Rujun
Lehmann, Martin
DesGroseillers, Luc
Laughrea, Michael
Boccaccio, Graciela Lidia
Mouland, Andrew J.
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv HIV
Staufen
Stress Granule
capside
topic HIV
Staufen
Stress Granule
capside
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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: Abrahamyan, Levon G.. Davis Jewish General Hospital; Canadá
Fil: Chatel Chaix, Laurent. Davis Jewish General Hospital; Canadá
Fil: Ajamian, Lara. Mc Gill University; Canadá. Davis Jewish General Hospital; Canadá
Fil: Milev, Miroslav P.. Mc Gill University; Canadá. Davis Jewish General Hospital; Canadá
Fil: Monette, Anne. Mc Gill University; Canadá. Davis Jewish General Hospital; Canadá
Fil: Clément, Jean François. Davis Jewish General Hospital; Canadá
Fil: Song, Rujun. Mc Gill University; Canadá. Davis Jewish General Hospital; Canadá
Fil: Lehmann, Martin. Davis Jewish General Hospital; Canadá
Fil: DesGroseillers, Luc. University Of Montreal; Canadá
Fil: Laughrea, Michael. Mc Gill University; Canadá. Davis Jewish General Hospital; Canadá
Fil: Boccaccio, Graciela Lidia. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina
Fil: Mouland, Andrew J.. Mc Gill University; Canadá. Davis Jewish General Hospital; Canadá
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.
publishDate 2010
dc.date.none.fl_str_mv 2010-02
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/15285
Abrahamyan, Levon G.; Chatel Chaix, Laurent; Ajamian, Lara; Milev, Miroslav P.; Monette, Anne; et al.; Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA; Company Of Biologists; Journal Of Cell Science; 123; Pte 3; 2-2010; 369-383
1477-9137
url http://hdl.handle.net/11336/15285
identifier_str_mv Abrahamyan, Levon G.; Chatel Chaix, Laurent; Ajamian, Lara; Milev, Miroslav P.; Monette, Anne; et al.; Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA; Company Of Biologists; Journal Of Cell Science; 123; Pte 3; 2-2010; 369-383
1477-9137
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://jcs.biologists.org/content/123/3/369.long
info:eu-repo/semantics/altIdentifier/doi/10.1242/jcs.055897
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Company Of Biologists
publisher.none.fl_str_mv Company Of Biologists
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1844614025854320640
score 13.070432

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