The Conserved Tyr176/Leu177 Motif in the α-Helix 9 of the Feline Immunodeficiency Virus Capsid Protein Is Critical for Gag Particle Assembly

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

Publikováno v: Viruses, Vol 11, Iss 9, p 816 (2019)

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-assem

Externí odkaz: https://doaj.org/article/0735903bb7b342f08d6b625704df8a04

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

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

Publikováno v: Virus Genes. 57:106-110

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=doi_________::24cfdfed4ac830a878506626fc80a979
https://doi.org/10.1007/s11262-020-01816-7

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