Structural elements in the Gag polyprotein of feline immunodeficiency virus involved in Gag self-association and assembly

The Gag polyprotein of feline immunodeficiency virus (FIV) assembles at the plasma membrane of the infected cells. We aimed to identify the FIV Gag domains that interact and promote Gag multimerization. To do this we generated a series of Gag subdomains and tested their ability to associate with ful...

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Autores: Abdusetir Cerfoglio, Juan Carlos, Gonzalez, Silvia Adriana, Affranchino, Jose Luis
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2014
País:Argentina
Institución:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/35915
Acceso en línea:http://hdl.handle.net/11336/35915
Access Level:acceso abierto
Palabra clave:Lentivirus
Gag Polyprotein
Fiv Assembly
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
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spelling Structural elements in the Gag polyprotein of feline immunodeficiency virus involved in Gag self-association and assemblyAbdusetir Cerfoglio, Juan CarlosGonzalez, Silvia AdrianaAffranchino, Jose LuisLentivirusGag PolyproteinFiv Assemblyhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The Gag polyprotein of feline immunodeficiency virus (FIV) assembles at the plasma membrane of the infected cells. We aimed to identify the FIV Gag domains that interact and promote Gag multimerization. To do this we generated a series of Gag subdomains and tested their ability to associate with full-length Gag and be recruited into extracellular virus-like particles (VLPs). Removal of 37 residues from the C-terminus of FIV Gag and deletion of the N-terminal and central regions of the nucleocapsid (NC) domain attenuated but did not abrogate association with wild-type Gag, whereas a Gag mutant protein encompassing the matrix (MA) and capsid (CA) domains interacted poorly with full-length Gag. Association with wild-type Gag was abolished by deleting most of the NC together with the N-terminal 40 residues of the MA, which most likely reflects the inability of this Gag mutant to bind RNA. Notably, the CA–NC Gag subdomain both associated with wild-type Gag and was recruited into particles in a proportion close to 50 % of the total Gag-related protein mass of VLPs. Moreover, both a Gag protein lacking the C-terminal p2 peptide and a nonmyristoylated version of the polyprotein exhibited a transdominant-negative effect on the assembly of wild-type Gag. Analysis of Gag mutants carrying internal deletions within the CA revealed that the N-terminal and the C-terminal domains of the CA are necessary for Gag assembly. Our results demonstrate that the FIV CA–NC region constitutes the principal self-interaction domain of Gag and that the RNA-binding capacity of Gag is necessary for its multimerization.Fil: Abdusetir Cerfoglio, Juan Carlos. 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; ArgentinaFil: Affranchino, Jose Luis. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaSociety for General Microbiology2014-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/35915Abdusetir Cerfoglio, Juan Carlos; Gonzalez, Silvia Adriana; Affranchino, Jose Luis; Structural elements in the Gag polyprotein of feline immunodeficiency virus involved in Gag self-association and assembly; Society for General Microbiology; Journal of General Virology; 95; 9-2014; 2050-20590022-1317CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1099/vir.0.065151-0info:eu-repo/semantics/altIdentifier/url/http://jgv.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.065151-0info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2024-05-08T13:54:02Zoai:ri.conicet.gov.ar:11336/35915instacron: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:34982024-05-08 13:54:03.198CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Structural elements in the Gag polyprotein of feline immunodeficiency virus involved in Gag self-association and assembly
title Structural elements in the Gag polyprotein of feline immunodeficiency virus involved in Gag self-association and assembly
spellingShingle Structural elements in the Gag polyprotein of feline immunodeficiency virus involved in Gag self-association and assembly
Abdusetir Cerfoglio, Juan Carlos
Lentivirus
Gag Polyprotein
Fiv Assembly
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
title_short Structural elements in the Gag polyprotein of feline immunodeficiency virus involved in Gag self-association and assembly
title_full Structural elements in the Gag polyprotein of feline immunodeficiency virus involved in Gag self-association and assembly
title_fullStr Structural elements in the Gag polyprotein of feline immunodeficiency virus involved in Gag self-association and assembly
title_full_unstemmed Structural elements in the Gag polyprotein of feline immunodeficiency virus involved in Gag self-association and assembly
title_sort Structural elements in the Gag polyprotein of feline immunodeficiency virus involved in Gag self-association and assembly
dc.creator.none.fl_str_mv Abdusetir Cerfoglio, Juan Carlos
Gonzalez, Silvia Adriana
Affranchino, Jose Luis
author Abdusetir Cerfoglio, Juan Carlos
author_facet Abdusetir Cerfoglio, Juan Carlos
Gonzalez, Silvia Adriana
Affranchino, Jose Luis
author_role author
author2 Gonzalez, Silvia Adriana
Affranchino, Jose Luis
author2_role author
author
dc.subject.none.fl_str_mv Lentivirus
Gag Polyprotein
Fiv Assembly
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
topic Lentivirus
Gag Polyprotein
Fiv Assembly
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
description The Gag polyprotein of feline immunodeficiency virus (FIV) assembles at the plasma membrane of the infected cells. We aimed to identify the FIV Gag domains that interact and promote Gag multimerization. To do this we generated a series of Gag subdomains and tested their ability to associate with full-length Gag and be recruited into extracellular virus-like particles (VLPs). Removal of 37 residues from the C-terminus of FIV Gag and deletion of the N-terminal and central regions of the nucleocapsid (NC) domain attenuated but did not abrogate association with wild-type Gag, whereas a Gag mutant protein encompassing the matrix (MA) and capsid (CA) domains interacted poorly with full-length Gag. Association with wild-type Gag was abolished by deleting most of the NC together with the N-terminal 40 residues of the MA, which most likely reflects the inability of this Gag mutant to bind RNA. Notably, the CA–NC Gag subdomain both associated with wild-type Gag and was recruited into particles in a proportion close to 50 % of the total Gag-related protein mass of VLPs. Moreover, both a Gag protein lacking the C-terminal p2 peptide and a nonmyristoylated version of the polyprotein exhibited a transdominant-negative effect on the assembly of wild-type Gag. Analysis of Gag mutants carrying internal deletions within the CA revealed that the N-terminal and the C-terminal domains of the CA are necessary for Gag assembly. Our results demonstrate that the FIV CA–NC region constitutes the principal self-interaction domain of Gag and that the RNA-binding capacity of Gag is necessary for its multimerization.
publishDate 2014
dc.date.none.fl_str_mv 2014-09
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/11336/35915
Abdusetir Cerfoglio, Juan Carlos; Gonzalez, Silvia Adriana; Affranchino, Jose Luis; Structural elements in the Gag polyprotein of feline immunodeficiency virus involved in Gag self-association and assembly; Society for General Microbiology; Journal of General Virology; 95; 9-2014; 2050-2059
0022-1317
CONICET Digital
CONICET
url http://hdl.handle.net/11336/35915
identifier_str_mv Abdusetir Cerfoglio, Juan Carlos; Gonzalez, Silvia Adriana; Affranchino, Jose Luis; Structural elements in the Gag polyprotein of feline immunodeficiency virus involved in Gag self-association and assembly; Society for General Microbiology; Journal of General Virology; 95; 9-2014; 2050-2059
0022-1317
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1099/vir.0.065151-0
info:eu-repo/semantics/altIdentifier/url/http://jgv.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.065151-0
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
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Society for General Microbiology
publisher.none.fl_str_mv Society for General Microbiology
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
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_ 1799195488813056000
score 15,812429

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