In the present case study, we attempted to observe amino acid substitutions in Gag and Env proteins and related parameters possibly associated with an increase in HIV-2 load.
In the present case study, we attempted to observe amino acid substitutions in Gag and Env proteins and related parameters possibly associated with an increase in HIV-2 load.
The V3 and V4 domains of human immunodeficiency virus type 2 (HIV-2) env genes from 14 rhesus macaques experimentally infected by HIV-2 SBL6669/H5 were sequenced.
The V3 and V4 domains of human immunodeficiency virus type 2 (HIV-2) env genes from 14 rhesus macaques experimentally infected by HIV-2 SBL6669/H5 were sequenced.
Mapping of the human immunodeficiency virus type 2envelope glycoprotein CD4 binding region and fusion domain with truncated proteins expressed by recombinant vaccinia viruses.
Mapping of the human immunodeficiency virus type 2envelope glycoprotein CD4 binding region and fusion domain with truncated proteins expressed by recombinant vaccinia viruses.
To investigate the glycoprotein determinants of viral cytopathology, we constructed chimeric env genes between a noncytopathic strain of human immunodeficiency virus type 2 (HIV-2), designated HIV-2/ST, and a highly fusogenic and cytopathic variant derived from this virus.
To investigate the glycoprotein determinants of viral cytopathology, we constructed chimeric env genes between a noncytopathic strain of human immunodeficiency virus type 2 (HIV-2), designated HIV-2/ST, and a highly fusogenic and cytopathic variant derived from this virus.
Dimerization of the envelope glycoprotein precursor and dimeric forms of the transmembrane glycoproteins were also observed in cells infected with simian immunodeficiency virus (SIV-mac), a virus closely related to HIV-2.
Dimerization of the envelope glycoprotein precursor and dimeric forms of the transmembrane glycoproteins were also observed in cells infected with simian immunodeficiency virus (SIV-mac), a virus closely related to HIV-2.
In the present case study, we attempted to observe amino acid substitutions in Gag and Env proteins and related parameters possibly associated with an increase in HIV-2 load.
The CD4-independent tropism of human immunodeficiency virus type 2 involves several regions of the envelope protein and correlates with a reduced activation threshold for envelope-mediated fusion.
The V3 and V4 domains of human immunodeficiency virus type 2 (HIV-2) env genes from 14 rhesus macaques experimentally infected by HIV-2 SBL6669/H5 were sequenced.
To investigate the glycoprotein determinants of viral cytopathology, we constructed chimeric env genes between a noncytopathic strain of human immunodeficiency virus type 2 (HIV-2), designated HIV-2/ST, and a highly fusogenic and cytopathic variant derived from this virus.
Together, these findings indicate that HIV-2 and HIV-1 support similar levels of CD4 T cell depletion <i>in vitro</i> despite HIV-2 Vpx-mediated degradation of the SAMHD1 transcription factor.
Human immunodeficiency virus type 2 (HIV-2) and simian immunodeficiency virus (SIV) encode an accessory protein called viral protein X (Vpx) that promotes proteasomal degradation of SAMHD1, leading to a rapid increase in cellular dNTP concentrations.
SAMHD1 degradation was induced by treating target macrophages with vesicular stomatitis virus glycoprotein-pseudotyped human immunodeficiency virus type 2 (HIV-2) particles containing viral protein X.
We have previously shown the existence of primary human immunodeficiency virus type 2 isolates (MIC97 and MJC97) unable to use major coreceptors to entry into peripheral blood mononuclear cells, including CCR5 and CXCR4.