Abstract
During evolution, pathogens have evolved strategies to counteract key cellular restriction mechanisms in order to efficiently invade target cells and fulfill essential steps of their replication cycle. Human Immunodeficiency Virus-1 and some Simian counterparts express a small multifunctional protein, Vpu, which influences viral replication. By acting as a multifunctional adapter, Vpu enhances viral particle release and infectivity. Therefore Vpu, an accessory protein, contributes to pathogenesis while avoiding superinfection. These effects rely mainly on the ability of Vpu to target the host proteins CD4 and BST-2/tetherin. Indeed, Vpu downregulates the cell surface expression of these receptors and subsequently induces their proteolysis via a mechanism involving a β -TrCP-containing E3 ubiquitin ligase complex. In this review, we will detail recent research aimed at elucidating the mechanism of Vpu-mediated CD4 and BST-2/tetherin downregulation and degradation as well as their subsequent consequences on viral pathogenesis.
Keywords: BST-2/tetherin, CD4, Human Immunodeficiency Virus-1 (HIV-1), lysosome, proteasome, SCFbTrCP E3 ubiquitin ligase, Ubiquitination, Viral Protein U (Vpu), degradation, proteolysis
Current HIV Research
Title:β -TrCP Dependency of HIV-1 Vpu-Induced Downregulation of CD4 and BST-2/Tetherin
Volume: 10 Issue: 4
Author(s): Fabien P. Blanchet, J. P. Mitchell and Vincent Piguet
Affiliation:
Keywords: BST-2/tetherin, CD4, Human Immunodeficiency Virus-1 (HIV-1), lysosome, proteasome, SCFbTrCP E3 ubiquitin ligase, Ubiquitination, Viral Protein U (Vpu), degradation, proteolysis
Abstract: During evolution, pathogens have evolved strategies to counteract key cellular restriction mechanisms in order to efficiently invade target cells and fulfill essential steps of their replication cycle. Human Immunodeficiency Virus-1 and some Simian counterparts express a small multifunctional protein, Vpu, which influences viral replication. By acting as a multifunctional adapter, Vpu enhances viral particle release and infectivity. Therefore Vpu, an accessory protein, contributes to pathogenesis while avoiding superinfection. These effects rely mainly on the ability of Vpu to target the host proteins CD4 and BST-2/tetherin. Indeed, Vpu downregulates the cell surface expression of these receptors and subsequently induces their proteolysis via a mechanism involving a β -TrCP-containing E3 ubiquitin ligase complex. In this review, we will detail recent research aimed at elucidating the mechanism of Vpu-mediated CD4 and BST-2/tetherin downregulation and degradation as well as their subsequent consequences on viral pathogenesis.
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Cite this article as:
P. Blanchet Fabien, P. Mitchell J. and Piguet Vincent, β -TrCP Dependency of HIV-1 Vpu-Induced Downregulation of CD4 and BST-2/Tetherin, Current HIV Research 2012; 10 (4) . https://dx.doi.org/10.2174/157016212800792441
DOI https://dx.doi.org/10.2174/157016212800792441 |
Print ISSN 1570-162X |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4251 |
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