Evidence map›Paper›PMID 18808682›Full record

ArticleRetrovirology2008

Direct Vpr-Vpr interaction in cells monitored by two photon fluorescence correlation spectroscopy and fluorescence lifetime imaging.

Joëlle V Fritz, Pascal Didier, Jean-Pierre Clamme, Emmanuel Schaub, Delphine Muriaux, Charlotte Cabanne, Nelly Morellet, Serge Bouaziz, Jean-Luc Darlix, Yves Mély and 1 more

Abstract read
In one paragraph

Article in Retrovirology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Nano letters · 2020
    Article
  6. Article
  7. Article
  8. Article
  9. HIV-1 Vpr-a still "enigmatic multitasker".Frontiers in microbiology · 2014
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors.

Joëlle V FritzDépartement de Pharmacologie et Physico-Chimie des Interactions Cellulaires et Moléculaires, UMR 7175 CNRS, Faculté de Pharmacie, Université Louis Pasteur, Illkirch Cedex, France. joelle.fritz@pharma.u-strasbg.fr
Pascal Didier
Jean-Pierre Clamme
Emmanuel Schaub
Delphine Muriaux
Charlotte Cabanne
Nelly Morellet
Serge Bouaziz
Jean-Luc Darlix
Yves Mély
Hugues de Rocquigny

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe human immunodeficiency virus type 1 (HIV-1) encodes several regulatory proteins, notably Vpr which influences the survival of the infected cells by causing a G2/M arrest and apoptosis. Such an important role of Vpr in HIV-1 disease progression has fuelled a large number of studies, from its 3D structure to the characterization of specific cellular partners. However, no direct imaging and quantification of Vpr-Vpr interaction in living cells has yet been reported. To address this issue, eGFP- and mCherry proteins were tagged by Vpr, expressed in HeLa cells and their interaction was studied by two photon fluorescence lifetime imaging microscopy and fluorescence correlation spectroscopy.

resultsResults show that Vpr forms homo-oligomers at or close to the nuclear envelope. Moreover, Vpr dimers and trimers were found in the cytoplasm and in the nucleus. Point mutations in the three alpha helices of Vpr drastically impaired Vpr oligomerization and localization at the nuclear envelope while point mutations outside the helical regions had no effect. Theoretical structures of Vpr mutants reveal that mutations within the alpha-helices could perturb the leucine zipper like motifs. The DeltaQ44 mutation has the most drastic effect since it likely disrupts the second helix. Finally, all Vpr point mutants caused cell apoptosis suggesting that Vpr-mediated apoptosis functions independently from Vpr oligomerization.

conclusionWe report that Vpr oligomerization in HeLa cells relies on the hydrophobic core formed by the three alpha helices. This oligomerization is required for Vpr localization at the nuclear envelope but not for Vpr-mediated apoptosis.

Indexed as

Protein Interaction MappingApoptosisCell NucleusCytoplasmGenes, ReporterGreen Fluorescent ProteinsHeLa CellsHIV-1HumansImage Processing, Computer-AssistedLuminescent ProteinsModels, MolecularPoint MutationPolymersProtein BindingProtein Interaction Domains and Motifsenhanced green fluorescent proteinGreen Fluorescent ProteinsLuminescent ProteinsPolymersRecombinant Fusion ProteinsRed Fluorescent Proteinvpr Gene Products, Human Immunodeficiency Virusvpr protein, Human immunodeficiency virus 1

Identifiers

PMID18808682
PMCPMC2562391

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.