Results 191 to 200 of about 18,811 (223)
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Intracellular Logistics of BST-2/Tetherin
Current HIV Research, 2012Bone marrow stromal antigen 2 (BST-2) is a type II membrane protein with two targeting signals, one of which is located in the cytoplasmic domain and contains a non-canonical dual tyrosine-based motif responsible for its endocytosis from the plasma membrane, and the other is a C-terminal glycosylphosphatidylinositol anchor that facilitates its ...
Hideaki, Fujita +3 more
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Eukaryotic expression of Porcine BST-2 gene and identification of biological activity of BST-2
2011 International Conference on Remote Sensing, Environment and Transportation Engineering, 2011BST-2 is a new kind of antivirus protein that is induced by IFN α/β. The BST-2 gene fragment was amplified by RT-PCR from pig kidney cells (PK-15) and subcloned into the pLenti7.3/V5-TOPO vector and the positive clone was filtrated. The positive plasmids were transfected into the HEK293T cells. The expressed protein was analyzed by SDS-PAGE.
null Tinghong Zhang +3 more
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An unconventional BST-2 function: Down-regulation of transient protein expression
Biochemical and Biophysical Research Communications, 2014While viral inhibition by tethering of budding virions to host cell membranes has been focused upon as one of the main functions of BST-2/tetherin, BST-2 is thought to possess other functions as well. Overexpression of BST-2 was found here to down-regulate transient protein expression.
Jaraspim, Narkpuk +5 more
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Cancerous Phenotypes Exhibited by NIH/3T3 Fibroblasts Overexpressing BST‐2
The FASEB Journal, 2020Oncogenesis is a multistep process initiated by the accumulation of genetic and/or epigenetic changes that culminate in the transformation of normal cells into cancer cells. The genetic and/or epigenetic changes result in dysregulated gene expression signature that may involve key cancer driving genes such as ...
Folnetti Alvarez, Chioma Okeoma
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Ubiquitination of BST-2 Protein by HIV-1 Vpu Protein Does Not Require Lysine, Serine, or Threonine Residues within the BST-2 Cytoplasmic Domain [PDF]
Journal of Biological Chemistry, 2012 The cellular protein BST-2/CD317/Tetherin has been shown to inhibit the release of HIV-1 and other enveloped viruses from infected cells. The HIV-1 accessory protein Vpu binds to both BST-2 and βTrCP, a substrate-recognition subunit for the SCF (Skip1-Cullin1-F-box protein) E3 ubiquitin ligase complex.
Jean K, Gustin +3 more
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Enhanced production of enveloped viruses in BST‐2‐deficient cell lines
Biotechnology and Bioengineering, 2017ABSTRACTDespite all the advantages that cell‐cultured influenza vaccines have over egg‐based influenza vaccines, the inferior productivity of cell‐culture systems is a major drawback that must be addressed. BST‐2 (tetherin) is a host restriction factor which inhibits budding‐out of various enveloped viruses from infected host cells.
Eunbi Yi +4 more
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[Inhibition of HBV Release by BST-2].
Bing du xue bao = Chinese journal of virology, 2016Bone marrow stromal antigen 2 (BST-2) is a kind of host restriction factor. Since it was discovered to be responsible for the defect in virion release of HIV-1 mutants lacking the accessory gene vpu in 2008, it was thought to mainly restrict the viruses by directly tethering viral particles at the plasma membrane. Recent reports suggest that BST-2 also
Zhu, Han, Xiaofang, Yu, Wenyan, Zhang
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BST-2: at the Crossroads of Viral Pathogenesis and Oncogenesis
Future Virology, 2016BST-2 is a moonlight protein with several protective and deleterious functions. Regulation of virus restriction and tumor aggressiveness are the most studied aspects of BST-2 function and thus, the main focus of this perspective. Virus inhibition roles of BST-2 have therapeutic potential that, if properly harnessed, could result in near broad spectrum ...
Wadie D Mahauad-Fernandez +1 more
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The Disulfide Bonds within BST-2 Enhance Tensile Strength during Viral Tethering
Biochemistry, 2016Human BST-2/tetherin is a host factor that inhibits the release of enveloped viruses, including HIV-1, HIV-2, and SIV, from the cell surface by tethering viruses to the host cell membrane. BST-2 has an α-helical ectodomain that forms disulfide-linked dimers between two monomers forming a coiled coil. The ectodomain contains three cysteine residues that
Kelly E, Du Pont +4 more
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A novel peptide to disrupt the interaction of BST‐2 and Vpu
Peptide Science, 2014ABSTRACTBone marrow stromal cell antigen 2 (BST‐2) inhibits the release of HIV‐1 and other enveloped viruses from the cell surface. HIV‐1 Vpu binds to BST‐2 through an interaction between transmembrane domains (TMD) of the two proteins and induces the downregulation of cell surface BST‐2, thereby counteracting its antiviral activity.
Zeyun, Mi +7 more
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