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

    Abdusetir Cerfoglio, Juan C.; González, Silvia A.; Affranchino, José L. (2014)
    The Gag polyprotein of feline immunodeficiency virus (FIV) assembles at the plasma membrane of the infected cells. Since the FIV Gag domains whose interaction promotes Gag multimerization have not been identified, we ...
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    In vitro binding of simian immunodeficiency virus matrix protein to the cytoplasmic domain of the envelope glycoprotein 

    Manrique, Julieta M.; Affranchino, José L.; González, Silvia A. (2008)
    Incorporation of the envelope (Env) glycoprotein into budding virions is a key step in the replication cycle of lentiviruses. Previously, we provided genetic and biochemical evidence indicating that Env packaging into ...
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    Mapping of the Self-Interaction Domains in the Simian Immunodeficiency Virus Gag Polyprotein 

    Rauddi, María L.; Mac Donald, Cecilia L.; Affranchino, José L.; González, Silvia A. (2011)
    To gain a better understanding of the assembly process in simian immunodeficiency virus (SIV), we first established the conditions under which recombinant SIV Gag lacking the C-terminal p6 domain (SIV GagΔp6) assembled in ...
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    In vitro assembly of the feline immunodeficiency virus Gag polyprotein 

    Affranchino, José L.; González, Silvia A. (2010)
    The retroviral Gag protein is the only viral product that is necessary for the assembly of virions in mammalian cells. We have established an in vitro assembly system to study the assembly properties of purified feline ...
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    Mutations at the C-terminus of the simian immunodeficiency virus envelope glycoprotein affect gp120-gp41 stability on virions 

    González, Silvia; Affranchino, José L. (2005)
    The transmembrane (TM) subunit of the envelope (Env) glycoprotein of the simian immunodeficiency virus (SIV) contains an unusually long cytoplasmic domain of 164 amino acids. Previously, we identified domains in the SIV ...
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    Understanding the Process ofEnvelope Glycoprotein Incorporation into Virions in Simian and Feline Immunodeficiency Viruses 

    Affranchino, José L.; González, Silvia A. (2014)
    The lentiviral envelope glycoproteins (Env) mediate virus entry by interacting with specific receptors present at the cell surface, thereby determining viral tropism and pathogenesis. Therefore, Env incorporation into ...
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    El virus de la gripe porcina y la amenaza de una pandemia 

    Affranchino, José L. (2009)
    Se sabe desde hace décadas que existen virus de origen porcino causantes de influenza o gripe en humanos. Desde 1958 se registraron, por lo menos, unos trescientos casos de esas gripes, incluidas varias muertes. En marzo ...
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    Palmitoylation of the feline immunodeficiency virus envelope glycoprotein and its effect on fusion activity and envelope incorporation into virions 

    González, Silvia A.; Paladino, Mónica G.; Affranchino, José L. (2012)
    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 ...
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    Importance of the short cytoplasmic domain of the feline immunodeficiency virus transmembrane glycoprotein for fusion activity and envelope glycoprotein incorporation into virions 

    Celma, Cristina; Paladino, Mónica G.; González, Silvia A.; Affranchino, José L. (2007)
    The mature form of the envelope (Env) glycoprotein of lentiviruses is a heterodimer composed of the surface (SU) and transmembrane (TM) subunits. Feline immunodeficiency virus (FIV) possesses a TM glycoprotein with a ...
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    Replacement of the V3 Domain in the Surface Subunit of the Feline Immunodeficiency Virus Envelope Glycoprotein with the Equivalent Region of a T Cell-Tropic Human Immunodeficiency Virus Type 1 Results in a Chimeric Surface Protein That Efficiently Binds to CXCR4 

    González, Silvia A.; Falcón, Juan I.; Affranchino, José L. (2014)
    Feline immunodeficiency virus (FIV) and the T cell-tropic strains of human immunodeficiency virus type 1 (HIV-1) share the use of the chemokine receptor CXCR4 for cell entry. To study this process further we developed a ...

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    Affranchino, José L. (10)
    González, Silvia A. (8)Paladino, Mónica G. (2)Abdusetir Cerfoglio, Juan C. (1)Celma, Cristina (1)Falcón, Juan I. (1)González, Silvia (1)Mac Donald, Cecilia L. (1)Manrique, Julieta M. (1)Rauddi, María L. (1)SubjectFeline immunodeficiency virus (5)Envelope glycoprotein (4)Gag polyprotein (3)Glicoproteína de la envoltura (3)poliproteína Gag (3)Simian immunodeficiency virus (3)Virus de la inmunodeficiencia del simio (3)Virus de la inmunodeficiencia felina (3)virus de la inmunodeficiencia felina (3)Actividad fusogénica (2)... View MoreDate Issued2014 (3)2012 (1)2011 (1)2010 (1)2009 (1)2008 (1)2007 (1)2005 (1)

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