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Β-TrCP is dispensable for Vpu's ability to overcome the CD317/Tetherin-imposed restriction to HIV-1 release

The cellular transmembrane protein CD317/BST-2/HM1.24/Tetherin restricts HIV-1 infection by physically tethering mature virions to the surface of infected cells. HIV-1 counteracts this restriction by expressing the accessory protein Vpu, yet the mechanism of this antagonism is incompletely understoo...

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Bibliographic Details
Main Authors: Tervo, Hanna-Mari (Author) , Homann, Stefanie (Author) , Ambiel, Ina (Author) , Fritz, Joëlle (Author) , Fackler, Oliver Till (Author) , Keppler, Oliver Till (Author)
Format: Article (Journal)
Language:English
Published: 10 February 2011
In: Retrovirology
Year: 2011, Volume: 8, Pages: 1-15
ISSN:1742-4690
DOI:10.1186/1742-4690-8-9
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1186/1742-4690-8-9
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Author Notes:Hanna-Mari Tervo, Stefanie Homann, Ina Ambiel, Joëlle V. Fritz, Oliver T. Fackler, Oliver T. Keppler
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Summary:The cellular transmembrane protein CD317/BST-2/HM1.24/Tetherin restricts HIV-1 infection by physically tethering mature virions to the surface of infected cells. HIV-1 counteracts this restriction by expressing the accessory protein Vpu, yet the mechanism of this antagonism is incompletely understood. β-TrCP is the substrate recognition domain of an E3 ubiquitin ligase complex that interacts with the di-serine motif S52/S56 in the cytoplasmic tail of Vpu to target the CD4 receptor for proteasomal degradation. Recently, it has been suggested that β-TrCP is also critically involved in Vpu's ability to overcome the CD317-mediated virion release block.
Item Description:Gesehen am 27.10.2022
Physical Description:Online Resource
ISSN:1742-4690
DOI:10.1186/1742-4690-8-9

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