Evidence map›Paper›PMID 23049930›Full record

ArticlePloS one2012

Human nucleoporins promote HIV-1 docking at the nuclear pore, nuclear import and integration.

Francesca Di Nunzio, Anne Danckaert, Thomas Fricke, Patricio Perez, Juliette Fernandez, Emmanuelle Perret, Pascal Roux, Spencer Shorte, Pierre Charneau, Felipe Diaz-Griffero and 1 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 131 papers.

0numbers the graph read from it
0cells of the map it votes in
131citing papers in PubMed
5.4field-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

131 citing papers in PubMed, 187 citations in OpenAlex.

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  13. Lenacapavir disrupts HIV-1 core integrity while stabilizing the capsid lattice.Proceedings of the National Academy of Sciences of the United States of America · 2025
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71 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

11 authors at 3 institutions in 2 countries.

Francesca Di NunzioMolecular Virology and Vaccinology Unit, CNRS URA 3015, Department of Virology, Institut Pasteur, Paris, France.
Anne Danckaert
Thomas Fricke
Patricio Perez
Juliette Fernandez
Emmanuelle Perret
Pascal Roux
Spencer Shorte
Pierre Charneau
Felipe Diaz-Griffero
Nathalie J Arhel
Institut Pasteur · FRAlbert Einstein College of Medicine · USDepartment of Virology · FR

Funding

Role of Cellular Factors in Retroviral Uncoating and Synthesis of Viral DNAR01AI087390 · NIAID · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI DIAZ-GRIFFERO, FELIPE · 2010 to 2024
$6.8M
Role of the B-box-v-1 Restriction by TRIM5alpha proteinsR00MH086162 · NIMH · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI DIAZ-GRIFFERO, FELIPE · 2010 to 2011
$496k
NIAID NIH HHS R01 AI087390NIMH NIH HHS 4R00MH086162-02NIMH NIH HHS R00 MH086162
6 · The paper itself

Abstract

The nuclear pore complex (NPC) mediates nucleo-cytoplasmic transport of macromolecules and is an obligatory point of passage and functional bottleneck in the replication of some viruses. The Human Immunodeficiency Virus (HIV) has evolved the required mechanisms for active nuclear import of its genome through the NPC. However the mechanisms by which the NPC allows or even assists HIV translocation are still unknown. We investigated the involvement of four key nucleoporins in HIV-1 docking, translocation, and integration: Nup358/RanBP2, Nup214/CAN, Nup98 and Nup153. Although all induce defects in infectivity when depleted, only Nup153 actually showed any evidence of participating in HIV-1 translocation through the nuclear pore. We show that Nup358/RanBP2 mediates docking of HIV-1 cores on NPC cytoplasmic filaments by interacting with the cores and that the C-terminus of Nup358/RanBP2 comprising a cyclophilin-homology domain contributes to binding. We also show that Nup214/CAN and Nup98 play no role in HIV-1 nuclear import per se: Nup214/CAN plays an indirect role in infectivity read-outs through its effect on mRNA export, while the reduction of expression of Nup98 shows a slight reduction in proviral integration. Our work shows the involvement of nucleoporins in diverse and functionally separable steps of HIV infection and nuclear import.

Indexed as

Active Transport, Cell NucleusHeLa CellsHIV-1HIV InfectionsHumansMolecular ChaperonesNuclear PoreNuclear Pore Complex ProteinsProtein BindingMolecular ChaperonesNuclear Pore Complex Proteinsran-binding protein 2

Identifiers

PMID23049930
PMCPMC3457934
OpenAlexW2038356077

What OpenQuestion holds

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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.