Human Immunodeficiency Virus Type 2 Vpx-Gag Interaction

Pancio, Heather A.; Ratner, Lee

doi:10.1128/jvi.72.6.5271-5275.1998

Cited by 24 publications

(21 citation statements)

References 25 publications

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“…One potential explanation for these results is that GFP-X89 and GFP-X101 could be less stable than GFP-Vpx or GFP-XAH. However, the truncation of HIV-2 Vpx at either residue 89 or 101 did not affect protein stability (34). The GFP-X101 fusion protein was expressed in transfected 293T cells at levels comparable to those of GFP-Vpx (Fig.…”

mentioning

confidence: 90%

“…Vpx and Vpr share considerable homology (42,44). Like Vpr, Vpx is virion associated and recruited into virions through its interaction with the p6 portion of the Gag polyprotein (1,34,47). Also similar to Vpr, one study demonstrated that Vpx, when expressed in the absence of other viral components, is a nuclear protein (5).…”

mentioning

confidence: 99%

“…Representative results are shown from three different experiments which all yielded similar results. region predicted to form an amphipathic helix, a truncation at residue 89 (X89), and a truncation at residue 101 (X101) (34). The last two mutations remove a highly conserved stretch of prolines found in C-terminal residues 102 to 112 of Vpx (11).…”

mentioning

confidence: 99%

“…The last two mutations remove a highly conserved stretch of prolines found in C-terminal residues 102 to 112 of Vpx (11). Wild-type and mutant vpx constructs described previously (34) were amplified by PCR with primers which introduced a 5Ј BspE1 site and a 3Ј XhoI site. PCR products were then cloned into the pEGFP-C1 vector (Clontech), which had been digested with BspE1-XhoI.…”

mentioning

confidence: 99%

“…Two flanking SacI sites were used for digestion and subcloning into pUC19 to generate pUC19-VpxMS. A StuI-XhoI fragment from vpx deletion mutant pTM-X101, described previously (34), was ligated into pUC19-VpxMS digested with StuI-XhoI. The entire SacI fragment was then religated back into pES.…”

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confidence: 99%

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The C-Terminal Proline-Rich Tail of Human Immunodeficiency Virus Type 2 Vpx Is Necessary for Nuclear Localization of the Viral Preintegration Complex in Nondividing Cells

Pancio

Heyden

Ratner

2000

J Virol

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Human immunodeficiency virus type 2 (HIV-2), like other lentiviruses, is capable of infecting nondividing T cells and macrophages. The present work shows that in HIV-2-infected cells, Vpx is necessary for efficient nuclear import of the preintegration complex. In agreement with this finding, the subcellular localization of a GFP-Vpx fusion protein was found to be predominantly nuclear. However, deletion of the proline-rich C-terminal 11 residues of Vpx resulted in a shift of the fusion protein to the cytoplasm. Furthermore, the same deletion in the context of the provirus resulted in a decrease in nuclear import of the preintegration complex and attenuated replication in macrophages.

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confidence: 90%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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The C-Terminal Proline-Rich Tail of Human Immunodeficiency Virus Type 2 Vpx Is Necessary for Nuclear Localization of the Viral Preintegration Complex in Nondividing Cells

Pancio

Heyden

Ratner

2000

J Virol

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Restriction of Retroviral Infection of Macrophages

Sharkey

2013

Current Topics in Microbiology and Immunology

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Primate immunodeficiency viruses are highly specialized lentiviruses that have evolved to successfully infect and persist for the lifetime of the host. Despite encountering numerous potent antiviral factors, HIVs and SIVs are successful pathogens due to the acquisition of equally potent countermeasures in the form of accessory genes. The accessory gene Vpx encoded by HIV-2 and a subset of SIVs have a profound effect on the ability of lentiviruses to infect non-dividing cells, such as macrophages. Although most virus replication occurs in activated CD4(+) T cells, myeloid lineage cells are natural targets of infection and play a central role in virus transmission, dissemination, and persistence. However, myeloid lineage cells are poorly sensitive to lentiviral infection due partly to the high-level expression of a host protein that regulates nucleic acid metabolism named SAMHD1. Degradation of SAMHD1 is induced by Vpx to eliminate this intrinsic antiviral factor. Importantly, SAMHD1 has also been implicated as a negative regulator of the innate immune response, so the interplay between SAMHD1 and Vpx is likely to have significant consequences for virus replication, persistence, and immune control.

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A Cellular Restriction Dictates the Permissivity of Nondividing Monocytes/Macrophages to Lentivirus and Gammaretrovirus Infection

Kaushik

Zhu

Stranska

et al. 2009

Cell Host & Microbe

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SUMMARY Primate lentiviruses including HIV-1 have evolved the capacity to transduce terminally differentiated, non-dividing myeloid cells and as a consequence, these viruses establish persistent infections of tissue macrophage and microglia in the host. In contrast, non-dividing myeloid cells are refractory to infection by gammaretroviruses such as MLV. Here we present evidence that a cellular restriction is the obstacle to transduction of macrophage by MLV. Neutralization of the restriction by Vpx, a primate lentiviral protein previously shown to protect primate lentiviruses from a macrophage restriction, rendered macrophage permissive to MLV infection. Packaging of Vpx within MLV virions was sufficient to confer a lentivirus phenotype for MLV. We further demonstrate that this restriction prevents transduction of quiescent monocytes by HIV-1. Monocyte- HeLa heterokaryons were resistant to HIV-1 infection while heterokaryons formed between monocytes and HeLa cells expressing Vpx were permissive to HIV-1 infection. Encapsidation of Vpx within HIV-1 virions conferred the ability to infect quiescent monocytes. Collectively our results indicate that the relative ability of lentiviruses and gammaretroviruses to transduce non-dividing, myeloid-cells is dependent upon their ability to neutralize a cellular restriction and that this restriction shapes the association of lentiviruses with myeloid cell reservoirs in the host.

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Human Immunodeficiency Virus Type 2 Vpx-Gag Interaction

Cited by 24 publications

References 25 publications

The C-Terminal Proline-Rich Tail of Human Immunodeficiency Virus Type 2 Vpx Is Necessary for Nuclear Localization of the Viral Preintegration Complex in Nondividing Cells

The C-Terminal Proline-Rich Tail of Human Immunodeficiency Virus Type 2 Vpx Is Necessary for Nuclear Localization of the Viral Preintegration Complex in Nondividing Cells

Restriction of Retroviral Infection of Macrophages

A Cellular Restriction Dictates the Permissivity of Nondividing Monocytes/Macrophages to Lentivirus and Gammaretrovirus Infection

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