Evidence map›Paper›PMID 27690223›Full record

ArticleeLife2016

Temporal proteomic analysis of HIV infection reveals remodelling of the host phosphoproteome by lentiviral Vif variants.

Edward Jd Greenwood, Nicholas J Matheson, Kim Wals, Dick Jh van den Boomen, Robin Antrobus, James C Williamson, Paul J Lehner

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
5.8field-weighted citation impact, top 4% of its field
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

70 citing papers in PubMed, 96 citations in OpenAlex.

  1. Manipulation of the cell cycle by HIV-1.Biochemical Society transactions · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. HIV-1 Vif and Vpr cooperatively modulate the cell cycle to maximize per-cell virion production.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Fitness Landscapes of APOBEC3G Antagonism by HIV-1 Vif proteins.bioRxiv : the preprint server for biology · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Structural insights into PPP2R5A degradation by HIV-1 Vif.Nature structural & molecular biology · 2024
    Article
  13. Altered memory CCR6EBioMedicine · 2024
    Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

10 more citing papers are in PubMed but not listed here.

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

7 authors at 1 institution in 1 country.

Edward Jd GreenwoodCambridge Institute for Medical Research, Department of Medicine, University of Cambridge, Cambridge, United Kingdom.
Nicholas J MathesonCambridge Institute for Medical Research, Department of Medicine, University of Cambridge, Cambridge, United Kingdom.ORCID 0000-0002-3318-1851
Kim WalsCambridge Institute for Medical Research, Department of Medicine, University of Cambridge, Cambridge, United Kingdom.
Dick Jh van den BoomenCambridge Institute for Medical Research, Department of Medicine, University of Cambridge, Cambridge, United Kingdom.
Robin AntrobusCambridge Institute for Medical Research, Department of Medicine, University of Cambridge, Cambridge, United Kingdom.
James C WilliamsonCambridge Institute for Medical Research, Department of Medicine, University of Cambridge, Cambridge, United Kingdom.
Paul J LehnerCambridge Institute for Medical Research, Department of Medicine, University of Cambridge, Cambridge, United Kingdom.ORCID 0000-0001-9383-1054
University of Cambridge · GB

Funding

Wellcome TrustWellcome Trust 093964/Z/10/ZWellcome Trust 101835/Z/13/Z
6 · The paper itself

Abstract

Viruses manipulate host factors to enhance their replication and evade cellular restriction. We used multiplex tandem mass tag (TMT)-based whole cell proteomics to perform a comprehensive time course analysis of >6500 viral and cellular proteins during HIV infection. To enable specific functional predictions, we categorized cellular proteins regulated by HIV according to their patterns of temporal expression. We focussed on proteins depleted with similar kinetics to APOBEC3C, and found the viral accessory protein Vif to be necessary and sufficient for CUL5-dependent proteasomal degradation of all members of the B56 family of regulatory subunits of the key cellular phosphatase PP2A (PPP2R5A-E). Quantitative phosphoproteomic analysis of HIV-infected cells confirmed Vif-dependent hyperphosphorylation of >200 cellular proteins, particularly substrates of the aurora kinases. The ability of Vif to target PPP2R5 subunits is found in primate and non-primate lentiviral lineages, and remodeling of the cellular phosphoproteome is therefore a second ancient and conserved Vif function.

Indexed as

Host-Pathogen InteractionsCells, CulturedHIVHIV InfectionsHumansPhosphoproteinsProteomeProteomicsTime Factorsvif Gene Products, Human Immunodeficiency VirusPhosphoproteinsProteomevif Gene Products, Human Immunodeficiency Virusvif protein, Human immunodeficiency virus 1HIVhumaninfectious diseaselentivirusmicrobiologyphosphorylationPP2AproteomicsVif

Identifiers

PMID27690223
PMCPMC5085607
OpenAlexW2527165350

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.