Lentiviral Gag assembly analyzed through the functional characterization of chimeric simian immunodeficiency viruses expressing different domains of the feline immunodeficiency virus capsid protein.

Autor: María J Esteva, José L Affranchino, Silvia A González

Publikováno v: PLoS ONE, Vol 9, Iss 12, p e114299 (2014)

To gain insight into the functional relationship between the capsid (CA) domains of the Gag polyproteins of simian and feline immunodeficiency viruses (SIV and FIV, respectively), we constructed chimeric SIVs in which the CA-coding region was partial

Externí odkaz: https://doaj.org/article/0afaca2f6f7147e08b8cdc465ae81a2e

In vitro inhibitory effect of maraviroc on the association of the simian immunodeficiency virus envelope glycoprotein with CCR5

Autor: Ignacio, Giraudy, César A, Ovejero, José L, Affranchino, Silvia A, González

Publikováno v: Virus genes. 57(1)

Asian macaques infected with simian immunodeficiency viruses (SIVs) isolated from African non-human primates develop a disease similar to human AIDS. SIV enters its target cells by binding to CD4 and a coreceptor, typically CCR5. Maraviroc is an entr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ee465c694302c2283c9fd691ea0d2ed4
https://pubmed.ncbi.nlm.nih.gov/33400102

Processing, fusogenicity, virion incorporation and CXCR4-binding activity of a feline immunodeficiency virus envelope glycoprotein lacking the two conserved N-glycosylation sites at the C-terminus of the V3 domain

Autor: Silvia A. González, José L. Affranchino

Publikováno v: Archives of Virology. 161:1761-1768

The process of feline immunodeficiency virus (FIV) entry into its target cells is initiated by the association of the surface (SU) subunit of the viral envelope glycoprotein (Env) with the cellular receptors CD134 and CXCR4. This event is followed by

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b561e9715ebeed10b1990a5b156d284c
https://doi.org/10.1007/s00705-016-2843-6

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

Autor: José L. Affranchino, Silvia A. González, César A. Ovejero

Publikováno v: CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
PLoS ONE
PLoS ONE, Vol 12, Iss 5, p e0177297 (2017)

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 t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dafefb4e45e98d18b65086319ecdf3d1
https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0177297

Palmitoylation of the feline immunodeficiency virus envelope glycoprotein and its effect on fusion activity and envelope incorporation into virions

Autor: José L. Affranchino, Mónica G. Paladino, Silvia A. González

Publikováno v: Virology

The feline immunodeficiency virus (FIV) envelope glycoprotein (Env) possesses a short cytoplasmic domain of 53 amino acids containing four highly conserved cysteines at Env positions 804, 811, 815 and 848. Since palmitoylation of transmembrane protei

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3eecec42d925cd12f26e1d9caa1723e
http://europepmc.org/articles/PMC7111954