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.
Instituto de Estudios Inmunológicos y Fisiopatológicos
Materia
Biología
HIV
Gag
RPL7
Interaction
Chaperone activity
Nucleocapsid
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/97566

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network_name_str SEDICI (UNLP)
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, HuguesBiologíaHIVGagRPL7InteractionChaperone activityNucleocapsidBackground: 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.Instituto de Estudios Inmunológicos y Fisiopatológicos2016-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf1-14http://sedici.unlp.edu.ar/handle/10915/97566enginfo:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/57847info: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/issn/1742-4690info:eu-repo/semantics/altIdentifier/doi/10.1186/s12977-016-0287-4info:eu-repo/semantics/altIdentifier/hdl/11336/57847info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:20:15Zoai:sedici.unlp.edu.ar:10915/97566Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:20:16.042SEDICI (UNLP) - Universidad Nacional de La Platafalse
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
Biología
HIV
Gag
RPL7
Interaction
Chaperone activity
Nucleocapsid
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 Biología
HIV
Gag
RPL7
Interaction
Chaperone activity
Nucleocapsid
topic Biología
HIV
Gag
RPL7
Interaction
Chaperone activity
Nucleocapsid
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.
Instituto de Estudios Inmunológicos y Fisiopatológicos
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
Articulo
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://sedici.unlp.edu.ar/handle/10915/97566
url http://sedici.unlp.edu.ar/handle/10915/97566
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/57847
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/issn/1742-4690
info:eu-repo/semantics/altIdentifier/doi/10.1186/s12977-016-0287-4
info:eu-repo/semantics/altIdentifier/hdl/11336/57847
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
1-14
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
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reponame_str SEDICI (UNLP)
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instacron_str UNLP
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repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
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