Abstract
Vpr is a lentiviral accessory protein that is expressed late during the infection cycle and is packaged in significant quantities into virus particles through a specific interaction with the P6 domain of the viral Gag precursor. Characterization of the physiologically relevant function(s) of Vpr has been hampered by the fact that in many cell lines, deletion of Vpr does not significantly affect viral fitness. However, Vpr is critical for virus replication in primary macrophages and for viral pathogenesis in vivo. It is generally accepted that Vpr does not have a specific enzymatic activity but functions as a molecular adapter to modulate viral or cellular processes for the benefit of the virus. Indeed, many Vpr interacting factors have been described by now, and the goal of this review is to summarize our current knowledge of cellular proteins targeted by Vpr.
Highlights
Primate lentiviruses are a group of retroviruses that cause slowly progressing, often incurable diseases
The Equine Infectious Anemia Virus (EIAV) S2 gene product appears to be a functional homolog of the Nef protein encoded by human and simian lentiviruses in that it has the ability to counteract the antiviral activity of the host factors SERINC3 and SERINC5 [1]
We found that wild type and Vpr-defective NL43 viruses replicated with viruses replicated very similar in all
Summary
Primate lentiviruses are a group of retroviruses that cause slowly progressing, often incurable diseases. While other HIV accessory proteins such as Vif and Nef seem to be packaged relatively nonspecifically without apparent interaction with structural viral proteins, studies on Vpr identified sequences in the P6 domain of the viral Gag precursor, as well as in Vpr, required for the specific packaging of Vpr into virions [7,8,9,10], which is facilitated by oligomerization [11,12,13]. The specific packaging of Vpr through an interaction with the viral Gag precursor suggests a function for Vpr early during virus replication. Cellular localization studies indicate that in infected cells, Vpr primarily localizes to the nucleus suggesting a role of Vpr in later stages of virus replication [22,23,24] Despite all of these insights, some of which have been reported as much as 30 years ago, the precise role of virion-associated Vpr remains unclear. Since much of the work on Vpr has been done on HIV-1 Vpr, Vpr here stands for HIV-1 Vpr unless otherwise specified
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