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dc.contributor.author
Abdusetir Cerfoglio, Juan Carlos  
dc.contributor.author
Gonzalez, Silvia Adriana  
dc.contributor.author
Affranchino, Jose Luis  
dc.date.available
2018-02-06T21:36:59Z  
dc.date.issued
2014-09  
dc.identifier.citation
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  
dc.identifier.issn
0022-1317  
dc.identifier.uri
http://hdl.handle.net/11336/35915  
dc.description.abstract
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.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Society for General Microbiology  
dc.rights
info:eu-repo/semantics/restrictedAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
Lentivirus  
dc.subject
Gag Polyprotein  
dc.subject
Fiv Assembly  
dc.subject.classification
Otras Ciencias Biológicas  
dc.subject.classification
Ciencias Biológicas  
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS  
dc.title
Structural elements in the Gag polyprotein of feline immunodeficiency virus involved in Gag self-association and assembly  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2018-02-06T20:07:23Z  
dc.journal.volume
95  
dc.journal.pagination
2050-2059  
dc.journal.pais
Reino Unido  
dc.description.fil
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; Argentina  
dc.description.fil
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  
dc.description.fil
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  
dc.journal.title
Journal of General Virology  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1099/vir.0.065151-0  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://jgv.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.065151-0