Evidence map›Paper›PMID 21901095›Full record

ArticlePLoS pathogens2011

Transportin 3 promotes a nuclear maturation step required for efficient HIV-1 integration.

Lihong Zhou, Elena Sokolskaja, Clare Jolly, William James, Sally A Cowley, Ariberto Fassati

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

99 citing papers in PubMed, 126 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The capsid revolution.Journal of molecular cell biology · 2024
    Review
  6. Review
  7. Article
  8. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
  9. Transportin-3 Facilitates Uncoating of Influenza A Virus.International journal of molecular sciences · 2022
    Article
  10. Th17 cell master transcription factor RORC2 regulates HIV-1 gene expression and viral outgrowth.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Review
  17. Review
  18. Article
  19. Review
  20. Article

39 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

6 authors at 3 institutions in 1 country.

Lihong ZhouWohl Virion Centre, Division of Infection & Immunity, University College London, London, United Kingdom.
Elena Sokolskaja
Clare Jolly
William James
Sally A Cowley
Ariberto Fassati
University College London · GBUniversity of Oxford · GBMRC Laboratory for Molecular Cell Biology · GB

Funding

Medical Research Council G0800312Medical Research Council G0900950Medical Research Council G9721629Wellcome Trust
6 · The paper itself

Abstract

The HIV/AIDS pandemic is a major global health threat and understanding the detailed molecular mechanisms of HIV replication is critical for the development of novel therapeutics. To replicate, HIV-1 must access the nucleus of infected cells and integrate into host chromosomes, however little is known about the events occurring post-nuclear entry but before integration. Here we show that the karyopherin Transportin 3 (Tnp3) promotes HIV-1 integration in different cell types. Furthermore Tnp3 binds the viral capsid proteins and tRNAs incorporated into viral particles. Interaction between Tnp3, capsid and tRNAs is stronger in the presence of RanGTP, consistent with the possibility that Tnp3 is an export factor for these substrates. In agreement with this interpretation, we found that Tnp3 exports from the nuclei viral tRNAs in a RanGTP-dependent way. Tnp3 also binds and exports from the nuclei some species of cellular tRNAs with a defective 3'CCA end. Depletion of Tnp3 results in a re-distribution of HIV-1 capsid proteins between nucleus and cytoplasm however HIV-1 bearing the N74D mutation in capsid, which is insensitive to Tnp3 depletion, does not show nucleocytoplasmic redistribution of capsid proteins. We propose that Tnp3 promotes HIV-1 infection by displacing any capsid and tRNA that remain bound to the pre-integration complex after nuclear entry to facilitate integration. The results also provide evidence for a novel tRNA nucleocytoplasmic trafficking pathway in human cells.

Indexed as

Virus IntegrationActive Transport, Cell Nucleusbeta KaryopherinsCapsid ProteinsCell LineCell NucleusCloning, MolecularDNA, ViralHIV-1HumansMutationProtein BindingRNA, Transferbeta KaryopherinsCapsid ProteinsDNA, ViralRNA, TransferTNPO3 protein, human

Identifiers

PMID21901095
PMCPMC3161976
OpenAlexW2022159627

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.