Results 81 to 90 of about 4,158 (155)

Tetherin can restrict cell-free and cell-cell transmission of HIV from primary macrophages to T cells.

PLoS Pathogens, 2014
Bst-2/Tetherin inhibits the release of HIV by tethering newly formed virus particles to the plasma membrane of infected cells. Although the mechanisms of Tetherin-mediated restriction are increasingly well understood, the biological relevance of this ...
Sebastian Giese, Mark Marsh
doaj   +1 more source

The depletion of tetherin by Vpu correlates with its ability to block tetherin antiviral activity.

, 2013
(A) The depletion of tetherin by Vpu correlates in a dose-dependent manner with its ability to block tetherin antiviral activity. 293T cells were transfected with an HIV-1 provirus deleted for Vpu, together with a fixed dose of human HA-tagged tetherin ...
Madeleine Zufferey (359889), Bastien Mangeat (25357), Jeremy Luban (126908), Martin Lehmann (45732), Gustavo Gers-Huber (158677), Vincent Piguet (192012)   +5 more
core   +1 more source

Retroviral Retention Activates a Syk-Dependent HemITAM in Human Tetherin [PDF]

, 2014
SummaryTetherin (BST2/CD317) restricts the release of enveloped viral particles from infected cells. Coupled to this virion retention, hominid tetherins induce proinflammatory gene expression via activating NF-κB.
Pickering, Suzanne, Neil, Stuart J.D., Curnock, Rachel, Neil, Stuart J D, Galão, Rui Pedro; id_orcid, Galão, Rui Pedro   +5 more
core   +1 more source

Molecular evolution of the primate antiviral restriction factor tetherin.

PLoS ONE, 2010
BackgroundTetherin is a recently identified antiviral restriction factor that restricts HIV-1 particle release in the absence of the HIV-1 viral protein U (Vpu). It is reminiscent of APOBEC3G and TRIM5a that also antagonize HIV.
Jun Liu, Keping Chen, Jian-Hua Wang, Chiyu Zhang   +3 more
doaj   +1 more source

Polarity changes in the transmembrane domain core of HIV-1 Vpu inhibits its anti-tetherin activity.

PLoS ONE, 2011
Tetherin (BST-2/CD317) is an interferon-inducible antiviral protein that restricts the release of enveloped viruses from infected cells. The HIV-1 accessory protein Vpu can efficiently antagonize this restriction.
Mingyu Lv, Jiawen Wang, Xiaodan Wang, Tao Zuo, Yingzi Zhu, Wei Kong, Xianghui Yu   +6 more
doaj   +1 more source

Vpu protects HIV-infected cells from antibody-dependent cellular phagocytosis by counteracting tetherin

Cell Reports
Summary: Tetherin is an interferon-inducible transmembrane protein that inhibits the detachment of enveloped viruses from infected cells. HIV-1 Vpu counteracts this restriction by removing tetherin from sites of virus release.
Brian J. Snow, Nida K. Keles, Ahmed Ali, Ryan T. Behrens, Sanath Kumar Janaka, David T. Evans   +5 more
doaj   +1 more source

BCA2/Rabring7 promotes tetherin-dependent HIV-1 restriction.

PLoS Pathogens, 2009
Host cell factors can either positively or negatively regulate the assembly and egress of HIV-1 particles from infected cells. Recent reports have identified a previously uncharacterized transmembrane protein, tetherin/CD317/BST-2, as a crucial host ...
Kei Miyakawa, Akihide Ryo, Tsutomu Murakami, Kenji Ohba, Shoji Yamaoka, Mitsunori Fukuda, John Guatelli, Naoki Yamamoto   +7 more
doaj   +1 more source

Localization of Lck-Vpu-Tetherin-HA fusion proteins.

, 2013
(A–E) Single cell clones of 293T cells stably expressing the indicated proteins namely: Lck-Tetherin (A), Lck-CTD2/6-Tetherin (B), Lck-H1-Tetherin (C), Lck-H2-Tetherin (D) or WT Tetherin (E) were fixed, permeabilized and stained using α-HA antibodies ...
Trinity Zang (215703), Paul D. Bieniasz (215716), Matthew W. McNatt (220810)   +2 more
core   +1 more source

Distribution of Nef and tetherin in SIV-infected cells.

, 2013
293T cells expressing HA-tagged rhesus tetherin were infected with VSV-G pseudotyped SIVmac239 Δenv and stained for tetherin (green), Nef (red) and the cell nucleus (blue).
Lawrence J. Stern (49046), Ruth Serra-Moreno (66346), Kerstin Zimmermann (432785), David T. Evans (140189)   +3 more
core   +1 more source

Serine Phosphorylation of HIV-1 Vpu and Its Binding to Tetherin Regulates Interaction with Clathrin Adaptors.

PLoS Pathogens, 2015
HIV-1 Vpu prevents incorporation of tetherin (BST2/ CD317) into budding virions and targets it for ESCRT-dependent endosomal degradation via a clathrin-dependent process. This requires a variant acidic dileucine-sorting motif (ExxxLV) in Vpu.
Tonya Kueck, Toshana L Foster, Julia Weinelt, Jonathan C Sumner, Suzanne Pickering, Stuart J D Neil   +5 more
doaj   +1 more source