ArticleJournal of virology2002
The first HxRxG motif in simian immunodeficiency virus mac239 Vpr is crucial for G(2)/M cell cycle arrest.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Vpr attenuates antiviral immune responses and is critical for full pathogenicity of SIViScience · 2023Article
- Introduction of H2C2-type zinc-binding residues into HIV-2 Vpr increases its expression level.FEBS open bio · 2018Article
- Virion-Associated Vpr Alleviates a Postintegration Block to HIV-1 Infection of Dendritic Cells.Journal of virology · 2017Article
- A comprehensive analysis of the naturally occurring polymorphisms in HIV-1 Vpr: potential impact on CTL epitopes.Virology journal · 2008Article
- SIV Vpr evolution is inversely related to disease progression in a morphine-dependent rhesus macaque model of AIDS.Virology · 2007Article
- Human immunodeficiency virus type 1 Vpr induces G2 checkpoint activation by interacting with the splicing factor SAP145.Molecular and cellular biology · 2006Article
- Activation of the ATR pathway by human immunodeficiency virus type 1 Vpr involves its direct binding to chromatin in vivo.Journal of virology · 2005Article
- Analysis of HIV-1 Vpr determinants responsible for cell growth arrest in Saccharomyces cerevisiae.Retrovirology · 2004Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The highly conserved Vpr protein mediates cell cycle arrest, transcriptional transactivation, and nuclear import of the preintegration complex in human immunodeficiency virus type 1. To identify functional domains in simian immunodeficiency virus (SIV) mac239 Vpr, we mutagenized selected motifs within an alpha-helical region and two C-terminal HxRxG motifs. All Vpr mutants located to the nucleus. Substitution of four amino acids in the alpha-helical domain did not interfere with cell cycle arrest, while a single substitution abolished cell cycle arrest function. Mutation of the first HxRxG motif to AxAxA also resulted in loss of cell cycle arrest, while mutation of the second motif had no effect. Interestingly, both Vpr mutants impaired in cell cycle arrest function also showed reduced transactivation of the SIV long terminal repeat, suggesting that arrest of cells at G(2)/M mediates or contributes to transactivation by Vpr.
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