Evidence map›Paper›PMID 32292164›Full record

ArticleeLife2020

Antagonism of PP2A is an independent and conserved function of HIV-1 Vif and causes cell cycle arrest.

Sara Marelli, James C Williamson, Anna V Protasio, Adi Naamati, Edward Jd Greenwood, Janet E Deane, Paul J Lehner, Nicholas J Matheson

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

28 citing papers in PubMed, 28 citations in OpenAlex.

  1. Manipulation of the cell cycle by HIV-1.Biochemical Society transactions · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. 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
  7. Fitness Landscapes of APOBEC3G Antagonism by HIV-1 Vif proteins.bioRxiv : the preprint server for biology · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Structural insights into PPP2R5A degradation by HIV-1 Vif.Nature structural & molecular biology · 2024
    Article
  12. Article
  13. Review
  14. Review
  15. HIV-1 Vif protein sequence variations in South African people living with HIV and their influence on Vif-APOBEC3G interaction.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2024
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
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

8 authors at 1 institution in 1 country.

Sara MarelliDepartment of Medicine, University of Cambridge, Cambridge, United Kingdom.
James C WilliamsonDepartment of Medicine, University of Cambridge, Cambridge, United Kingdom.
Anna V ProtasioDepartment of Medicine, University of Cambridge, Cambridge, United Kingdom.
Adi NaamatiDepartment of Medicine, University of Cambridge, Cambridge, United Kingdom.
Edward Jd GreenwoodDepartment of Medicine, University of Cambridge, Cambridge, United Kingdom.ORCID 0000-0002-5224-0263
Janet E DeaneDepartment of Clinical Neuroscience, University of Cambridge, Cambridge, United Kingdom.ORCID 0000-0002-4863-0330
Paul J LehnerDepartment of Medicine, University of Cambridge, Cambridge, United Kingdom.ORCID 0000-0001-9383-1054
Nicholas J MathesonDepartment of Medicine, University of Cambridge, Cambridge, United Kingdom.ORCID 0000-0002-3318-1851
University of Cambridge · GB

Funding

Medical Research Council MR/P008801/1Wellcome Trust
6 · The paper itself

Abstract

The seminal description of the cellular restriction factor APOBEC3G and its antagonism by HIV-1 Vif has underpinned two decades of research on the host-virus interaction. We recently reported that HIV-1 Vif is also able to degrade the PPP2R5 family of regulatory subunits of key cellular phosphatase PP2A (PPP2R5A-E; Greenwood et al., 2016; Naamati et al., 2019). We now identify amino acid polymorphisms at positions 31 and 128 of HIV-1 Vif which selectively regulate the degradation of PPP2R5 family proteins. These residues covary across HIV-1 viruses in vivo, favouring depletion of PPP2R5A-E. Through analysis of point mutants and naturally occurring Vif variants, we further show that degradation of PPP2R5 family subunits is both necessary and sufficient for Vif-dependent G2/M cell cycle arrest. Antagonism of PP2A by HIV-1 Vif is therefore independent of APOBEC3 family proteins, and regulates cell cycle progression in HIV-infected cells.

Indexed as

Cell Cycle CheckpointsAPOBEC DeaminasesFlow CytometryHIV-1Host Microbial InteractionsHumansPoint MutationProtein Phosphatase 2vif Gene Products, Human Immunodeficiency VirusAPOBEC3 proteins, humanAPOBEC DeaminasesPPP2R5A protein, humanProtein Phosphatase 2vif Gene Products, Human Immunodeficiency Virusvif protein, Human immunodeficiency virus 1cell cycleHIVinfectious diseasemicrobiologyPP2AVifvirus

Identifiers

PMID32292164
PMCPMC7920553
OpenAlexW3016035954

What Socratic 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 Socratic graph.