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Structural elements in the Gag polyprotein of feline immunodeficiency virus involved in Gag self-association and assembly
(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 ...
Mapping of the Self-Interaction Domains in the Simian Immunodeficiency Virus Gag Polyprotein
(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 ...
In vitro assembly of the feline immunodeficiency virus Gag polyprotein
(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 ...
Understanding the Process ofEnvelope Glycoprotein Incorporation into Virions in Simian and Feline Immunodeficiency Viruses
(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 ...
Palmitoylation of the feline immunodeficiency virus envelope glycoprotein and its effect on fusion activity and envelope incorporation into virions
(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 ...
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
(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 ...