Open reading frame vpr of simian immunodeficiency virus encodes a virion-associated protein

Yu, Xiaofang; Matsuda, Michiko; Essex, Max; Lee, Tun‐Hou

doi:10.1128/jvi.64.11.5688-5693.1990

Cited by 89 publications

(42 citation statements)

References 42 publications

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“…Vpr and Vpx were shown to be present in viral particles as a result of specific interactions with the Gag polypeptides (4,14,22,28,39,41,43). The presence of HIV-1 Vpr and the matrix protein in virions appears to determine nuclear transport of the preintegration complex in nondividing cells (2,11,13).…”

Section: Induction Of G 2 Arrest Is a General Function Of Vpr From DImentioning

confidence: 99%

Vpr-induced cell cycle arrest is conserved among primate lentiviruses

Planelles

Jowett

et al. 1996

J Virol

182

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We previously reported that expression of human immunodeficiency virus type 1 strain NL4-3 (HIV-1 NL4-3 ) vpr causes cells to arrest in the G 2 phase of the cell cycle. We examined the induction of cell cycle arrest by other HIV-1 isolates and by primate lentiviruses other than HIV-1. We demonstrate that the vpr genes from tissue culture-adapted or primary isolates of HIV-1 are capable of inducing G 2 arrest. In addition, we demonstrate that induction of cell cycle arrest is a conserved function of members of two other groups of primate lentiviruses, HIV-2/simian immunodeficiency virus strain sm (SIV sm )/SIV mac and SIV agm . vpr from HIV-1, HIV-2, and SIV mac induced cell cycle arrest when transfected in human (HeLa) and monkey (CV-1) cells. vpx from HIV-2 and SIV mac did not induce detectable cell cycle arrest in either cell type, and SIV agm vpx was capable of inducing arrest in CV-1 but not HeLa cells. These results indicate that induction of cell cycle perturbation is a general property of lentiviruses that infect primates. The conservation of this viral function throughout evolution suggests that it plays a key role in virus-host relationships, and elucidation of its mechanism may reveal important clues about pathology induced by primate lentiviruses.

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Section: Induction Of G 2 Arrest Is a General Function Of Vpr From DImentioning

confidence: 99%

Vpr-induced cell cycle arrest is conserved among primate lentiviruses

Planelles

Jowett

et al. 1996

J Virol

182

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“…An amphipathic helix near the N-terminus of Vpr has been implicated in the virion incorporation (Mahalingam et al, 1995a,b). Because of its virion association, it has been suggested that Vpr has an early role in HIV-1 infection, possibly in penetration or uncoating of the virus (Cohen etal., 1990a;Yuan et al, 1990;Yu et al, 1990), or in the nuclear transport of the pre-integration complex (Heinzinger et a/., 1994).…”

Section: Introductionmentioning

confidence: 99%

Extracellular addition of a domain of HIV‐1 Vpr containing the amino acid sequence motif H(S/F)RIG causes cell membrane permeabilization and death

Macreadie

Arunagiri

Hewish

et al. 1996

Molecular Microbiology

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Vpr is a virion-associated protein of human immunodeficiency virus type 1 (HIV-1) whose function in acquired immune deficiency syndrome (AIDS) has been uncertain. We previously employed yeast as a model to examine the effects of Vpr on basic cellular functions; intracellular Vpr was shown to cause cell-growth arrest and structural defects, and these effects were caused by a region of Vpr containing the sequence HFRIGCRHSRIG. Here we show that peptides containing the H(S/F)RIG amino acid sequence motif cause death when added externally to a variety of yeast including Saccharomyces cerevisiae, Kluyveromyces lactis, Candida glabrata, Candida albicans and Schizosaccharomyces pombe. Such peptides rapidly entered the cell from the time of addition, resulting in cell death. Elevated levels of ions, particularly magnesium and calcium ions, abrogated the cytotoxic effect by preventing the Vpr peptides from entering the cells. Extracellular Vpr found in the serum, or breakdown products of extracellular Vpr, may have similar effects to the Vpr peptides described here and could explain the death of uninfected bystander cells during AIDS.

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“…This 96-amino-acid protein is an important factor for the pathogenesis of HIV [1,2]. Vpr is an integral part of viral particles suggesting an important role in early stages of infection [3][4][5][6]. Vpr is involved in the transport of the preintegration complex into the host cell nucleus, which is an important feature for infection of nondividing cells [7,8].…”

mentioning

confidence: 99%

Structure of human immunodeficiency virus type 1 Vpr(34–51) peptide in micelle containing aqueous solution

Engler

Stangler

Willbold

2002

European Journal of Biochemistry

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Human immunodeficiency virus type 1 protein R (HIV-1 Vpr) promotes nuclear entry of viral nucleic acids in nondividing cells, causes G 2 cell cycle arrest and is involved in cellular differentiation and cell death. Vpr subcellular localization is as variable as its functions. It is known, that consistent with its role in nuclear transport, Vpr localizes to the nuclear envelope of human cells. Further, a reported ion channel activity of Vpr is clearly dependent on its localization in or at membranes. We focused our structural studies on the secondary structure of a peptide consisting of residues 34-51 of HIV-1 Vpr. This part of Vpr plays an important role in Vpr oligomerization, contributes to cell cycle arrest activity, and is essential for virion incorporation and binding to HHR23A, a protein involved in DNA repair. Employing NMR spectroscopy we found this part of Vpr to be almost completely a helical in the presence of micelles, as well as in trifluoroethanol containing and methanol/ chloroform solvent. Our results provide structural data suggesting residues 34-51 of Vpr to contain an amphipathic, leucine-zipper-like a helix, which serves as a basis for oligomerization of Vpr and its interactions with cellular and viral factors involved in subcellular localization and virion incorporation of Vpr.

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Open reading frame vpr of simian immunodeficiency virus encodes a virion-associated protein

Cited by 89 publications

References 42 publications

Vpr-induced cell cycle arrest is conserved among primate lentiviruses

Vpr-induced cell cycle arrest is conserved among primate lentiviruses

Extracellular addition of a domain of HIV‐1 Vpr containing the amino acid sequence motif H(S/F)RIG causes cell membrane permeabilization and death

Structure of human immunodeficiency virus type 1 Vpr(34–51) peptide in micelle containing aqueous solution

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