Results 21 to 30 of about 18,811 (223)
Resilience of BST-2/Tetherin structure to single amino acid substitutions. [PDF]
PeerJ, 2019 ABSTRACTHuman Tetherin, also known as BST-2 or CD317, is a dimeric, extracellular membrane-bound protein that consists of N and C terminal membrane anchors connected by an extracellular domain. BST-2 is involved in binding enveloped viruses, such as HIV, and inhibiting viral release in addition to a role in NF-kB signaling.
Roy IR, Sutton CK, Berndsen CE.
europepmc +4 more sources
Tetherin/BST-2: Restriction Factor or Immunomodulator? [PDF]
Curr HIV Res, 2016 Cell-mediated immune (CMI) responses are critical for the control of HIV-1 infection and their importance was highlighted by the existence of viral proteins, particularly Vpu and Nef, that antagonize these responses. Pandemic HIV-1 Vpu counteracts Tetherin/BST-2, a host factor that could prevent the release of HIV-1 virions by tethering virions on the ...
Li SX, Barrett BS, Guo K, Santiago ML.
europepmc +3 more sources
Enhanced antagonism of BST-2 by a neurovirulent SIV envelope. [PDF]
J Clin Invest, 2016 Current antiretroviral therapy (ART) is not sufficient to completely suppress disease progression in the CNS, as indicated by the rising incidence of HIV-1-associated neurocognitive disorders (HAND) among infected individuals on ART. It is not clear why some HIV-1-infected patients develop HAND, despite effective repression of viral replication in the ...
Matsuda K +11 more
europepmc +4 more sources
BST-2 Diminishes HIV-1 Infectivity [PDF]
Journal of Virology, 2010 ABSTRACT Bone marrow stromal cell antigen 2 (BST-2, also known as tetherin/CD317/HM1.24) inhibits the release of human immunodeficiency virus type 1 (HIV-1) and other enveloped viruses by tethering virus particles to the cell surface. In this study, we provide evidence not only that the yield of cell-free HIV-1 particles is significantly ...
Jianyong, Zhang, Chen, Liang
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Restriction of Retroviral Replication by Tetherin/BST-2 [PDF]
Molecular Biology International, 2012 Tetherin/BST-2 is an important host restriction factor that limits the replication of HIV and other enveloped viruses. Tetherin is a type II membrane glycoprotein with a very unusual domain structure that allows it to engage budding virions and retain them on the plasma membrane of infected cells.
Hammonds, Jason +2 more
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Sensitivity to BST-2 restriction correlates with Orthobunyavirus host range. [PDF]
Virology, 2017 Orthobunyaviruses include several recently emerging viruses of significant medical and veterinary importance. There is currently very limited understanding on what determines the host species range of these pathogens. In this study we discovered that BST-2/tetherin restricts orthobunyavirus replication in a host-specific manner.
Varela M +11 more
europepmc +5 more sources
Beyond Tethering the Viral Particles: Immunomodulatory Functions of Tetherin (BST-2). [PDF]
DNA Cell Biol, 2019 Host response to viral infection is a highly regulated process involving engagement of various host factors, cytokines, chemokines, and stimulatory signals that pave the way for an antiviral immune response. The response is manifested in terms of viral sequestration, phagocytosis, and inhibition of genome replication, and, finally, if required ...
Tiwari R +3 more
europepmc +4 more sources
BST-2/Tetherin: Viral Tether, Viral Sensor or Both? [PDF]
Future Virology, 2013 In the fields of virology and innate immunity, BST-2/tetherin is well known for its ability to block the egress of enveloped viruses from infected cells. This appears to be accomplished by 'tethering' virions to the cell surface, thereby limiting virion release.
Jean K, Gustin, Janet L, Douglas
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Bending of the BST‐2 coiled‐coil during viral budding [PDF]
Proteins: Structure, Function, and Bioinformatics, 2017 Abstract BST‐2/tetherin is a human extracellular transmembrane protein that serves as a host defense factor against HIV‐1 and other viruses by inhibiting viral spreading. Structurally, BST‐2 is a homo‐dimeric coiled‐coil that is connected to the host cell membrane by N and C terminal transmembrane anchors.
Kadir A. Ozcan, Christopher E. Berndsen
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Positioning of cysteine residues within the N-terminal portion of the BST-2/tetherin ectodomain is important for functional dimerization of BST-2. [PDF]
J Biol Chem, 2015 BST-2/tetherin is a cellular host factor capable of restricting the release of a variety of enveloped viruses, including HIV-1. Structurally, BST-2 consists of an N-terminal cytoplasmic domain, a transmembrane domain, an ectodomain, and a C-terminal membrane anchor.
Welbourn S +5 more
europepmc +4 more sources