Results 11 to 20 of about 8,539 (222)
The HIV-1 Vpu viroporin inhibitor BIT225 does not affect Vpu-mediated tetherin antagonism.
Among its many roles, the HIV-1 accessory protein Vpu performs a viroporin function and also antagonizes the host cell restriction factor tetherin through its transmembrane domain.
Björn D Kuhl +6 more
doaj +4 more sources
Vpu and BST2: still not there yet? [PDF]
Extensive investigations have identified two cellular proteins in humans that potently inhibit HIV-1 replication and are widely accepted as ‘restriction factors’.
Peter Gee +5 more
core +5 more sources
Association of Vpu-Binding Protein with Microtubules and Vpu-Dependent Redistribution of HIV-1 Gag Protein [PDF]
The efficient exit of HIV-1 particles from cells requires the action of the viral encoded protein Vpu. Vpu-binding protein (Ubp) is a cellular protein that interacts with both Vpu and the major structural component of the viral capsid (Gag) and appears ...
Dall, Aaron +3 more
core +3 more sources
The transmembrane domain of HIV-1 Vpu is sufficient to confer anti-tetherin activity to SIVcpz and SIVgor Vpu proteins : cytoplasmic determinants of Vpu function [PDF]
Background: The acquisition of effective Vpu-mediated anti-tetherin activity to promote virion release following transmission of SIVcpzPtt from central chimpanzees (Pan troglodytes troglodytes) to humans distinguishes pandemic HIV-1 group M strains from ...
Kirchhoff, F. +15 more
core +5 more sources
During human immunodeficiency virus-1 (HIV-1) assembly, the host proteins CD4 (the HIV-1 receptor) and tetherin (an interferon stimulated anti-viral protein) both reduce viral fitness.
Tiffany M Lucas +3 more
doaj +2 more sources
Vpu-APEX2 fusion protein design and activity.
(A) A schematic representation of C-terminally tagged Vpu constructs; Vpu-FLAG and Vpu-FLAG-APEX2. A GGGS linker lies between the FLAG epitope and APEX2. (B) HeLa P4.R5 cells were transfected with Vpu constructs bearing C-terminal FLAG or FLAG and APEX2.
Sumit K. Chanda (11768006) +11 more
core +1 more source
Successful viruses must overcome the body's immune defenses. In this issue of Cell Host & Microbe, Goffinet et al. (2009) provide evidence that the host protein CD317, the target of the HIV Vpu protein, is part of an ancient innate immune response directed against budding viruses.
openaire +2 more sources
The RING-CH ligase K5 antagonizes restriction of KSHV and HIV-1 particle release by mediating ubiquitin-dependent endosomal degradation of tetherin [PDF]
Tetherin (CD317/BST2) is an interferon-induced membrane protein that inhibits the release of diverse enveloped viral particles. Several mammalian viruses have evolved countermeasures that inactivate tetherin, with the prototype being the HIV-1 Vpu ...
Wilson, Sam J. +48 more
core +1 more source

