Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor

Autores
Ovejero, César Antonio; Affranchino, Jose Luis; Gonzalez, Silvia Adriana
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The formation of immature lentiviral particles is dependent on the multimerization of the Gag polyprotein at the plasma membrane of the infected cells. One key player in the virus assembly process is the capsid (CA) domain of Gag, which establishes the protein-protein interactions that give rise to the hexagonal lattice of Gag molecules in the immature virion. To gain a better understanding of the functional equivalence between the CA proteins of simian and feline immunodeficiency viruses (SIV and FIV, respectively), we generated a series of chimeric FIV Gag proteins in which the CA-coding region was partially or totally replaced by its SIV counterpart. All the FIV Gag chimeras were found to be assembly-defective; however, all of them are able to interact with wild-type SIV Gag and be recruited into extracellular virus-like particles, regardless of the SIV CA sequences present in the chimeric FIV Gag. The results presented here markedly contrast with our previous findings showing that chimeric SIVs carrying FIV CA-derived sequences are assembly-competent. Overall, our data support the notion that although the SIV and FIV CA proteins share 51% amino acid sequence similarity and exhibit a similar organization, i.e., an N-terminal domain joined by a flexible linker to a C-terminal domain, their functional exchange between these different lentiviruses is strictly dependent on the context of the recipient Gag precursor.
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: Affranchino, Jose Luis. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Gonzalez, Silvia Adriana. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
SIV
FIV
GAG POLYPROTEIN
VIRAL ASSEMBLY
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:11336/72614
Acceder
id CONICETDig_b922952b7e3241665d029ffca026fcbe
oai_identifier_str oai:ri.conicet.gov.ar:11336/72614
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursorOvejero, César AntonioAffranchino, Jose LuisGonzalez, Silvia AdrianaSIVFIVGAG POLYPROTEINVIRAL ASSEMBLYhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The formation of immature lentiviral particles is dependent on the multimerization of the Gag polyprotein at the plasma membrane of the infected cells. One key player in the virus assembly process is the capsid (CA) domain of Gag, which establishes the protein-protein interactions that give rise to the hexagonal lattice of Gag molecules in the immature virion. To gain a better understanding of the functional equivalence between the CA proteins of simian and feline immunodeficiency viruses (SIV and FIV, respectively), we generated a series of chimeric FIV Gag proteins in which the CA-coding region was partially or totally replaced by its SIV counterpart. All the FIV Gag chimeras were found to be assembly-defective; however, all of them are able to interact with wild-type SIV Gag and be recruited into extracellular virus-like particles, regardless of the SIV CA sequences present in the chimeric FIV Gag. The results presented here markedly contrast with our previous findings showing that chimeric SIVs carrying FIV CA-derived sequences are assembly-competent. Overall, our data support the notion that although the SIV and FIV CA proteins share 51% amino acid sequence similarity and exhibit a similar organization, i.e., an N-terminal domain joined by a flexible linker to a C-terminal domain, their functional exchange between these different lentiviruses is strictly dependent on the context of the recipient Gag precursor.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: Affranchino, Jose Luis. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Gonzalez, Silvia Adriana. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaPublic Library of Science2017-05info: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/11336/72614Ovejero, César Antonio; Affranchino, Jose Luis; Gonzalez, Silvia Adriana; Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor; Public Library of Science; Plos One; 12; 5; 5-2017; 1-19; e01772971932-6203CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0177297info:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0177297info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:31:27Zoai:ri.conicet.gov.ar:11336/72614instacron: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 10:31:27.482CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor
title Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor
spellingShingle Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor
Ovejero, César Antonio
SIV
FIV
GAG POLYPROTEIN
VIRAL ASSEMBLY
title_short Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor
title_full Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor
title_fullStr Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor
title_full_unstemmed Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor
title_sort Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor
dc.creator.none.fl_str_mv Ovejero, César Antonio
Affranchino, Jose Luis
Gonzalez, Silvia Adriana
author Ovejero, César Antonio
author_facet Ovejero, César Antonio
Affranchino, Jose Luis
Gonzalez, Silvia Adriana
author_role author
author2 Affranchino, Jose Luis
Gonzalez, Silvia Adriana
author2_role author
author
dc.subject.none.fl_str_mv SIV
FIV
GAG POLYPROTEIN
VIRAL ASSEMBLY
topic SIV
FIV
GAG POLYPROTEIN
VIRAL ASSEMBLY
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The formation of immature lentiviral particles is dependent on the multimerization of the Gag polyprotein at the plasma membrane of the infected cells. One key player in the virus assembly process is the capsid (CA) domain of Gag, which establishes the protein-protein interactions that give rise to the hexagonal lattice of Gag molecules in the immature virion. To gain a better understanding of the functional equivalence between the CA proteins of simian and feline immunodeficiency viruses (SIV and FIV, respectively), we generated a series of chimeric FIV Gag proteins in which the CA-coding region was partially or totally replaced by its SIV counterpart. All the FIV Gag chimeras were found to be assembly-defective; however, all of them are able to interact with wild-type SIV Gag and be recruited into extracellular virus-like particles, regardless of the SIV CA sequences present in the chimeric FIV Gag. The results presented here markedly contrast with our previous findings showing that chimeric SIVs carrying FIV CA-derived sequences are assembly-competent. Overall, our data support the notion that although the SIV and FIV CA proteins share 51% amino acid sequence similarity and exhibit a similar organization, i.e., an N-terminal domain joined by a flexible linker to a C-terminal domain, their functional exchange between these different lentiviruses is strictly dependent on the context of the recipient Gag precursor.
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: Affranchino, Jose Luis. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Gonzalez, Silvia Adriana. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description The formation of immature lentiviral particles is dependent on the multimerization of the Gag polyprotein at the plasma membrane of the infected cells. One key player in the virus assembly process is the capsid (CA) domain of Gag, which establishes the protein-protein interactions that give rise to the hexagonal lattice of Gag molecules in the immature virion. To gain a better understanding of the functional equivalence between the CA proteins of simian and feline immunodeficiency viruses (SIV and FIV, respectively), we generated a series of chimeric FIV Gag proteins in which the CA-coding region was partially or totally replaced by its SIV counterpart. All the FIV Gag chimeras were found to be assembly-defective; however, all of them are able to interact with wild-type SIV Gag and be recruited into extracellular virus-like particles, regardless of the SIV CA sequences present in the chimeric FIV Gag. The results presented here markedly contrast with our previous findings showing that chimeric SIVs carrying FIV CA-derived sequences are assembly-competent. Overall, our data support the notion that although the SIV and FIV CA proteins share 51% amino acid sequence similarity and exhibit a similar organization, i.e., an N-terminal domain joined by a flexible linker to a C-terminal domain, their functional exchange between these different lentiviruses is strictly dependent on the context of the recipient Gag precursor.
publishDate 2017
dc.date.none.fl_str_mv 2017-05
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/11336/72614
Ovejero, César Antonio; Affranchino, Jose Luis; Gonzalez, Silvia Adriana; Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor; Public Library of Science; Plos One; 12; 5; 5-2017; 1-19; e0177297
1932-6203
CONICET Digital
CONICET
url http://hdl.handle.net/11336/72614
identifier_str_mv Ovejero, César Antonio; Affranchino, Jose Luis; Gonzalez, Silvia Adriana; Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor; Public Library of Science; Plos One; 12; 5; 5-2017; 1-19; e0177297
1932-6203
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0177297
info:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0177297
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
application/pdf
dc.publisher.none.fl_str_mv Public Library of Science
publisher.none.fl_str_mv Public Library of Science
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_ 1844614325053947904
score 13.070432

Publicaciones similares