The Conserved Tyr176/Leu177 motif in the alpha-Helix 9 of the feline immunodeficiency virus capsid protein is critical for gag particle assembly

Autores
Ovejero, César Antonio; González, Ana Silvia; Affranchino, Jose Luis
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The capsid domain (CA) of the lentiviral Gag polyproteins has two distinct roles during virion morphogenesis. As a domain of Gag, it mediates the Gag–Gag interactions that drive immature particle assembly, whereas as a mature protein, it self-assembles into the conical core of the mature virion. Lentiviral CA proteins are composed of an N-terminal region with seven α-helices and a C-terminal domain (CA-CTD) formed by four α-helices. Structural studies performed in HIV-1 indicate that the CA-CTD helix 9 establishes homodimeric interactions that contribute to the formation of the hexameric Gag lattice in immature virions. Interestingly, the mature CA core also shows inter-hexameric associations involving helix 9 residues W184 and M185. The CA proteins of feline immunodeficiency virus (FIV) and equine infectious anemia virus (EIAV) exhibit, at equivalent positions in helix 9, the motifs Y176/L177 and L169/F170, respectively. In this paper, we investigated the relevance of the Y176/L177 motif for FIV assembly by introducing a series of amino acid substitutions into this sequence and studying their effect on in vivo and in vitro Gag assembly, CA oligomerization, mature virion production, and viral infectivity. Our results demonstrate that the Y176/L177 motif in FIV CA helix 9 is essential for Gag assembly and CA oligomerization. Notably, mutations converting the FIV CA Y176/L177 motif into the HIV-1 WM and EIAV FL sequences allow substantial particle production and viral replication in feline cells.
Fil: Ovejero, César Antonio. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: González, Ana Silvia. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Affranchino, Jose Luis. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
FELINE IMMUNODEFICIENCY VIRUS
GAG POLYPROTEIN
CAPSID PROTEIN
RETROVIRUS ASSEMBLY
RETROVIRUS INFECTIVITY
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:11336/155442
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/155442
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The Conserved Tyr176/Leu177 motif in the alpha-Helix 9 of the feline immunodeficiency virus capsid protein is critical for gag particle assemblyOvejero, César AntonioGonzález, Ana SilviaAffranchino, Jose LuisFELINE IMMUNODEFICIENCY VIRUSGAG POLYPROTEINCAPSID PROTEINRETROVIRUS ASSEMBLYRETROVIRUS INFECTIVITYhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The capsid domain (CA) of the lentiviral Gag polyproteins has two distinct roles during virion morphogenesis. As a domain of Gag, it mediates the Gag–Gag interactions that drive immature particle assembly, whereas as a mature protein, it self-assembles into the conical core of the mature virion. Lentiviral CA proteins are composed of an N-terminal region with seven α-helices and a C-terminal domain (CA-CTD) formed by four α-helices. Structural studies performed in HIV-1 indicate that the CA-CTD helix 9 establishes homodimeric interactions that contribute to the formation of the hexameric Gag lattice in immature virions. Interestingly, the mature CA core also shows inter-hexameric associations involving helix 9 residues W184 and M185. The CA proteins of feline immunodeficiency virus (FIV) and equine infectious anemia virus (EIAV) exhibit, at equivalent positions in helix 9, the motifs Y176/L177 and L169/F170, respectively. In this paper, we investigated the relevance of the Y176/L177 motif for FIV assembly by introducing a series of amino acid substitutions into this sequence and studying their effect on in vivo and in vitro Gag assembly, CA oligomerization, mature virion production, and viral infectivity. Our results demonstrate that the Y176/L177 motif in FIV CA helix 9 is essential for Gag assembly and CA oligomerization. Notably, mutations converting the FIV CA Y176/L177 motif into the HIV-1 WM and EIAV FL sequences allow substantial particle production and viral replication in feline cells.Fil: Ovejero, César Antonio. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: González, Ana Silvia. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Affranchino, Jose Luis. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaMultidisciplinary Digital Publishing Institute2019-09-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/155442Ovejero, César Antonio; González, Ana Silvia; Affranchino, Jose Luis; The Conserved Tyr176/Leu177 motif in the alpha-Helix 9 of the feline immunodeficiency virus capsid protein is critical for gag particle assembly; Multidisciplinary Digital Publishing Institute; Viruses; 11; 9; 4-9-2019; 1-141999-4915CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1999-4915/11/9/816info:eu-repo/semantics/altIdentifier/doi/10.3390/v11090816info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:44:11Zoai:ri.conicet.gov.ar:11336/155442instacron: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:34982025-09-03 09:44:12.089CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The Conserved Tyr176/Leu177 motif in the alpha-Helix 9 of the feline immunodeficiency virus capsid protein is critical for gag particle assembly
title The Conserved Tyr176/Leu177 motif in the alpha-Helix 9 of the feline immunodeficiency virus capsid protein is critical for gag particle assembly
spellingShingle The Conserved Tyr176/Leu177 motif in the alpha-Helix 9 of the feline immunodeficiency virus capsid protein is critical for gag particle assembly
Ovejero, César Antonio
FELINE IMMUNODEFICIENCY VIRUS
GAG POLYPROTEIN
CAPSID PROTEIN
RETROVIRUS ASSEMBLY
RETROVIRUS INFECTIVITY
title_short The Conserved Tyr176/Leu177 motif in the alpha-Helix 9 of the feline immunodeficiency virus capsid protein is critical for gag particle assembly
title_full The Conserved Tyr176/Leu177 motif in the alpha-Helix 9 of the feline immunodeficiency virus capsid protein is critical for gag particle assembly
title_fullStr The Conserved Tyr176/Leu177 motif in the alpha-Helix 9 of the feline immunodeficiency virus capsid protein is critical for gag particle assembly
title_full_unstemmed The Conserved Tyr176/Leu177 motif in the alpha-Helix 9 of the feline immunodeficiency virus capsid protein is critical for gag particle assembly
title_sort The Conserved Tyr176/Leu177 motif in the alpha-Helix 9 of the feline immunodeficiency virus capsid protein is critical for gag particle assembly
dc.creator.none.fl_str_mv Ovejero, César Antonio
González, Ana Silvia
Affranchino, Jose Luis
author Ovejero, César Antonio
author_facet Ovejero, César Antonio
González, Ana Silvia
Affranchino, Jose Luis
author_role author
author2 González, Ana Silvia
Affranchino, Jose Luis
author2_role author
author
dc.subject.none.fl_str_mv FELINE IMMUNODEFICIENCY VIRUS
GAG POLYPROTEIN
CAPSID PROTEIN
RETROVIRUS ASSEMBLY
RETROVIRUS INFECTIVITY
topic FELINE IMMUNODEFICIENCY VIRUS
GAG POLYPROTEIN
CAPSID PROTEIN
RETROVIRUS ASSEMBLY
RETROVIRUS INFECTIVITY
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The capsid domain (CA) of the lentiviral Gag polyproteins has two distinct roles during virion morphogenesis. As a domain of Gag, it mediates the Gag–Gag interactions that drive immature particle assembly, whereas as a mature protein, it self-assembles into the conical core of the mature virion. Lentiviral CA proteins are composed of an N-terminal region with seven α-helices and a C-terminal domain (CA-CTD) formed by four α-helices. Structural studies performed in HIV-1 indicate that the CA-CTD helix 9 establishes homodimeric interactions that contribute to the formation of the hexameric Gag lattice in immature virions. Interestingly, the mature CA core also shows inter-hexameric associations involving helix 9 residues W184 and M185. The CA proteins of feline immunodeficiency virus (FIV) and equine infectious anemia virus (EIAV) exhibit, at equivalent positions in helix 9, the motifs Y176/L177 and L169/F170, respectively. In this paper, we investigated the relevance of the Y176/L177 motif for FIV assembly by introducing a series of amino acid substitutions into this sequence and studying their effect on in vivo and in vitro Gag assembly, CA oligomerization, mature virion production, and viral infectivity. Our results demonstrate that the Y176/L177 motif in FIV CA helix 9 is essential for Gag assembly and CA oligomerization. Notably, mutations converting the FIV CA Y176/L177 motif into the HIV-1 WM and EIAV FL sequences allow substantial particle production and viral replication in feline cells.
Fil: Ovejero, César Antonio. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: González, Ana Silvia. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Affranchino, Jose Luis. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description The capsid domain (CA) of the lentiviral Gag polyproteins has two distinct roles during virion morphogenesis. As a domain of Gag, it mediates the Gag–Gag interactions that drive immature particle assembly, whereas as a mature protein, it self-assembles into the conical core of the mature virion. Lentiviral CA proteins are composed of an N-terminal region with seven α-helices and a C-terminal domain (CA-CTD) formed by four α-helices. Structural studies performed in HIV-1 indicate that the CA-CTD helix 9 establishes homodimeric interactions that contribute to the formation of the hexameric Gag lattice in immature virions. Interestingly, the mature CA core also shows inter-hexameric associations involving helix 9 residues W184 and M185. The CA proteins of feline immunodeficiency virus (FIV) and equine infectious anemia virus (EIAV) exhibit, at equivalent positions in helix 9, the motifs Y176/L177 and L169/F170, respectively. In this paper, we investigated the relevance of the Y176/L177 motif for FIV assembly by introducing a series of amino acid substitutions into this sequence and studying their effect on in vivo and in vitro Gag assembly, CA oligomerization, mature virion production, and viral infectivity. Our results demonstrate that the Y176/L177 motif in FIV CA helix 9 is essential for Gag assembly and CA oligomerization. Notably, mutations converting the FIV CA Y176/L177 motif into the HIV-1 WM and EIAV FL sequences allow substantial particle production and viral replication in feline cells.
publishDate 2019
dc.date.none.fl_str_mv 2019-09-04
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/11336/155442
Ovejero, César Antonio; González, Ana Silvia; Affranchino, Jose Luis; The Conserved Tyr176/Leu177 motif in the alpha-Helix 9 of the feline immunodeficiency virus capsid protein is critical for gag particle assembly; Multidisciplinary Digital Publishing Institute; Viruses; 11; 9; 4-9-2019; 1-14
1999-4915
CONICET Digital
CONICET
url http://hdl.handle.net/11336/155442
identifier_str_mv Ovejero, César Antonio; González, Ana Silvia; Affranchino, Jose Luis; The Conserved Tyr176/Leu177 motif in the alpha-Helix 9 of the feline immunodeficiency virus capsid protein is critical for gag particle assembly; Multidisciplinary Digital Publishing Institute; Viruses; 11; 9; 4-9-2019; 1-14
1999-4915
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.mdpi.com/1999-4915/11/9/816
info:eu-repo/semantics/altIdentifier/doi/10.3390/v11090816
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
dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
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 13.13397

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