Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling

Autores
El Mekdad, Hala; Boutant, Emmanuel; Karnib, Hassan; Biedma, Marina Elizabeth; Sharma, Kamal Kant; Malytska, Iuliia; Laumond, Géraldine; Roy, Marion; Réal, Eléonore; Paillart, Jean Christophe; Moog, Christiane; Darlix, Jean Luc; Mély, Yves; de Rocquigny, Hugues
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Background: In HIV-1 infected cells, the integrated viral DNA is transcribed by the host cell machinery to generate the full length HIV-1 RNA (FL RNA) that serves as mRNA encoding for the Gag and GagPol precursors. Virion formation is orchestrated by Gag, and the current view is that a specific interaction between newly made Gag molecules and FL RNA initiates the process. This in turn would cause FL RNA dimerization by the NC domain of Gag (GagNC). However the RNA chaperoning activity of unprocessed Gag is low as compared to the mature NC protein. This prompted us to search for GagNC co-factors. Results: Here we report that RPL7, a major ribosomal protein involved in translation regulation, is a partner of Gag via its interaction with the NC domain. This interaction is mediated by the NC zinc fingers and the N- and C-termini of RPL7, respectively, but seems independent of RNA binding, Gag oligomerization and its interaction with the plasma membrane. Interestingly, RPL7 is shown for the first time to exhibit a potent DNA/RNA chaperone activity higher than that of Gag. In addition, Gag and RPL7 can function in concert to drive rapid nucleic acid hybridization. Conclusions: Our results show that GagNC interacts with the ribosomal protein RPL7 endowed with nucleic acid chaperone activity, favoring the notion that RPL7 could be a Gag helper chaperoning factor possibly contributing to the start of Gag assembly.
Fil: El Mekdad, Hala. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; Francia
Fil: Boutant, Emmanuel. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; Francia
Fil: Karnib, Hassan. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Biedma, Marina Elizabeth. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Estudios Inmunológicos y Fisiopatológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Estudios Inmunológicos y Fisiopatológicos; Argentina. Université de Strasbourg; Francia. Inserm; Francia
Fil: Sharma, Kamal Kant. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; Francia
Fil: Malytska, Iuliia. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Laumond, Géraldine. Université de Strasbourg; Francia. Inserm; Francia
Fil: Roy, Marion. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Réal, Eléonore. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; Francia
Fil: Paillart, Jean Christophe. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; Francia
Fil: Moog, Christiane. Université de Strasbourg; Francia. Inserm; Francia
Fil: Darlix, Jean Luc. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Mély, Yves. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia
Fil: de Rocquigny, Hugues. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia
Materia
CHAPERONE ACTIVITY
GAG
HIV
INTERACTION
NUCLEOCAPSID
RPL7
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/57847
Acceder
id CONICETDig_b5be400c77e804b8e00ce7acc1e9acc7
oai_identifier_str oai:ri.conicet.gov.ar:11336/57847
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodelingEl Mekdad, HalaBoutant, EmmanuelKarnib, HassanBiedma, Marina ElizabethSharma, Kamal KantMalytska, IuliiaLaumond, GéraldineRoy, MarionRéal, EléonorePaillart, Jean ChristopheMoog, ChristianeDarlix, Jean LucMély, Yvesde Rocquigny, HuguesCHAPERONE ACTIVITYGAGHIVINTERACTIONNUCLEOCAPSIDRPL7https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Background: In HIV-1 infected cells, the integrated viral DNA is transcribed by the host cell machinery to generate the full length HIV-1 RNA (FL RNA) that serves as mRNA encoding for the Gag and GagPol precursors. Virion formation is orchestrated by Gag, and the current view is that a specific interaction between newly made Gag molecules and FL RNA initiates the process. This in turn would cause FL RNA dimerization by the NC domain of Gag (GagNC). However the RNA chaperoning activity of unprocessed Gag is low as compared to the mature NC protein. This prompted us to search for GagNC co-factors. Results: Here we report that RPL7, a major ribosomal protein involved in translation regulation, is a partner of Gag via its interaction with the NC domain. This interaction is mediated by the NC zinc fingers and the N- and C-termini of RPL7, respectively, but seems independent of RNA binding, Gag oligomerization and its interaction with the plasma membrane. Interestingly, RPL7 is shown for the first time to exhibit a potent DNA/RNA chaperone activity higher than that of Gag. In addition, Gag and RPL7 can function in concert to drive rapid nucleic acid hybridization. Conclusions: Our results show that GagNC interacts with the ribosomal protein RPL7 endowed with nucleic acid chaperone activity, favoring the notion that RPL7 could be a Gag helper chaperoning factor possibly contributing to the start of Gag assembly.Fil: El Mekdad, Hala. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; FranciaFil: Boutant, Emmanuel. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; FranciaFil: Karnib, Hassan. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; FranciaFil: Biedma, Marina Elizabeth. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Estudios Inmunológicos y Fisiopatológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Estudios Inmunológicos y Fisiopatológicos; Argentina. Université de Strasbourg; Francia. Inserm; FranciaFil: Sharma, Kamal Kant. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; FranciaFil: Malytska, Iuliia. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; FranciaFil: Laumond, Géraldine. Université de Strasbourg; Francia. Inserm; FranciaFil: Roy, Marion. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; FranciaFil: Réal, Eléonore. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; FranciaFil: Paillart, Jean Christophe. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; FranciaFil: Moog, Christiane. Université de Strasbourg; Francia. Inserm; FranciaFil: Darlix, Jean Luc. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; FranciaFil: Mély, Yves. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; FranciaFil: de Rocquigny, Hugues. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; FranciaBioMed Central2016-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/57847El Mekdad, Hala; Boutant, Emmanuel; Karnib, Hassan; Biedma, Marina Elizabeth; Sharma, Kamal Kant; et al.; Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling; BioMed Central; Retrovirology; 13; 1; 7-2016; 1-141742-4690CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4982112/info:eu-repo/semantics/altIdentifier/url/https://retrovirology.biomedcentral.com/articles/10.1186/s12977-016-0287-4info:eu-repo/semantics/altIdentifier/doi/10.1186/s12977-016-0287-4info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:09:45Zoai:ri.conicet.gov.ar:11336/57847instacron: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 10:09:46.16CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling
title Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling
spellingShingle Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling
El Mekdad, Hala
CHAPERONE ACTIVITY
GAG
HIV
INTERACTION
NUCLEOCAPSID
RPL7
title_short Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling
title_full Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling
title_fullStr Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling
title_full_unstemmed Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling
title_sort Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling
dc.creator.none.fl_str_mv El Mekdad, Hala
Boutant, Emmanuel
Karnib, Hassan
Biedma, Marina Elizabeth
Sharma, Kamal Kant
Malytska, Iuliia
Laumond, Géraldine
Roy, Marion
Réal, Eléonore
Paillart, Jean Christophe
Moog, Christiane
Darlix, Jean Luc
Mély, Yves
de Rocquigny, Hugues
author El Mekdad, Hala
author_facet El Mekdad, Hala
Boutant, Emmanuel
Karnib, Hassan
Biedma, Marina Elizabeth
Sharma, Kamal Kant
Malytska, Iuliia
Laumond, Géraldine
Roy, Marion
Réal, Eléonore
Paillart, Jean Christophe
Moog, Christiane
Darlix, Jean Luc
Mély, Yves
de Rocquigny, Hugues
author_role author
author2 Boutant, Emmanuel
Karnib, Hassan
Biedma, Marina Elizabeth
Sharma, Kamal Kant
Malytska, Iuliia
Laumond, Géraldine
Roy, Marion
Réal, Eléonore
Paillart, Jean Christophe
Moog, Christiane
Darlix, Jean Luc
Mély, Yves
de Rocquigny, Hugues
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv CHAPERONE ACTIVITY
GAG
HIV
INTERACTION
NUCLEOCAPSID
RPL7
topic CHAPERONE ACTIVITY
GAG
HIV
INTERACTION
NUCLEOCAPSID
RPL7
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Background: In HIV-1 infected cells, the integrated viral DNA is transcribed by the host cell machinery to generate the full length HIV-1 RNA (FL RNA) that serves as mRNA encoding for the Gag and GagPol precursors. Virion formation is orchestrated by Gag, and the current view is that a specific interaction between newly made Gag molecules and FL RNA initiates the process. This in turn would cause FL RNA dimerization by the NC domain of Gag (GagNC). However the RNA chaperoning activity of unprocessed Gag is low as compared to the mature NC protein. This prompted us to search for GagNC co-factors. Results: Here we report that RPL7, a major ribosomal protein involved in translation regulation, is a partner of Gag via its interaction with the NC domain. This interaction is mediated by the NC zinc fingers and the N- and C-termini of RPL7, respectively, but seems independent of RNA binding, Gag oligomerization and its interaction with the plasma membrane. Interestingly, RPL7 is shown for the first time to exhibit a potent DNA/RNA chaperone activity higher than that of Gag. In addition, Gag and RPL7 can function in concert to drive rapid nucleic acid hybridization. Conclusions: Our results show that GagNC interacts with the ribosomal protein RPL7 endowed with nucleic acid chaperone activity, favoring the notion that RPL7 could be a Gag helper chaperoning factor possibly contributing to the start of Gag assembly.
Fil: El Mekdad, Hala. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; Francia
Fil: Boutant, Emmanuel. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; Francia
Fil: Karnib, Hassan. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Biedma, Marina Elizabeth. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Estudios Inmunológicos y Fisiopatológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Estudios Inmunológicos y Fisiopatológicos; Argentina. Université de Strasbourg; Francia. Inserm; Francia
Fil: Sharma, Kamal Kant. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; Francia
Fil: Malytska, Iuliia. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Laumond, Géraldine. Université de Strasbourg; Francia. Inserm; Francia
Fil: Roy, Marion. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Réal, Eléonore. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; Francia
Fil: Paillart, Jean Christophe. Centre National de la Recherche Scientifique; Francia. Université de Strasbourg; Francia
Fil: Moog, Christiane. Université de Strasbourg; Francia. Inserm; Francia
Fil: Darlix, Jean Luc. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Mély, Yves. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia
Fil: de Rocquigny, Hugues. Université de Strasbourg; Francia. Centre National de la Recherche Scientifique; Francia
description Background: In HIV-1 infected cells, the integrated viral DNA is transcribed by the host cell machinery to generate the full length HIV-1 RNA (FL RNA) that serves as mRNA encoding for the Gag and GagPol precursors. Virion formation is orchestrated by Gag, and the current view is that a specific interaction between newly made Gag molecules and FL RNA initiates the process. This in turn would cause FL RNA dimerization by the NC domain of Gag (GagNC). However the RNA chaperoning activity of unprocessed Gag is low as compared to the mature NC protein. This prompted us to search for GagNC co-factors. Results: Here we report that RPL7, a major ribosomal protein involved in translation regulation, is a partner of Gag via its interaction with the NC domain. This interaction is mediated by the NC zinc fingers and the N- and C-termini of RPL7, respectively, but seems independent of RNA binding, Gag oligomerization and its interaction with the plasma membrane. Interestingly, RPL7 is shown for the first time to exhibit a potent DNA/RNA chaperone activity higher than that of Gag. In addition, Gag and RPL7 can function in concert to drive rapid nucleic acid hybridization. Conclusions: Our results show that GagNC interacts with the ribosomal protein RPL7 endowed with nucleic acid chaperone activity, favoring the notion that RPL7 could be a Gag helper chaperoning factor possibly contributing to the start of Gag assembly.
publishDate 2016
dc.date.none.fl_str_mv 2016-07
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/11336/57847
El Mekdad, Hala; Boutant, Emmanuel; Karnib, Hassan; Biedma, Marina Elizabeth; Sharma, Kamal Kant; et al.; Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling; BioMed Central; Retrovirology; 13; 1; 7-2016; 1-14
1742-4690
CONICET Digital
CONICET
url http://hdl.handle.net/11336/57847
identifier_str_mv El Mekdad, Hala; Boutant, Emmanuel; Karnib, Hassan; Biedma, Marina Elizabeth; Sharma, Kamal Kant; et al.; Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling; BioMed Central; Retrovirology; 13; 1; 7-2016; 1-14
1742-4690
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4982112/
info:eu-repo/semantics/altIdentifier/url/https://retrovirology.biomedcentral.com/articles/10.1186/s12977-016-0287-4
info:eu-repo/semantics/altIdentifier/doi/10.1186/s12977-016-0287-4
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv BioMed Central
publisher.none.fl_str_mv BioMed Central
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
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score 13.070432

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