Evidence map›Paper›PMID 19961612›Full record

ArticleRetrovirology2009

Inhibition of HIV-1 integrase nuclear import and replication by a peptide bearing integrase putative nuclear localization signal.

Aviad Levin, Ayelet Armon-Omer, Joseph Rosenbluh, Naomi Melamed-Book, Adolf Graessmann, Elisabeth Waigmann, Abraham Loyter

Open access · goldAbstract read
In one paragraph

Article in Retrovirology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

22 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. The Integrase: An Overview of a Key Player Enzyme in the Antiviral Scenario.International journal of molecular sciences · 2023
    Review
  4. Article
  5. The Role of Cyclodextrins in COVID-19 Therapy-A Literature Review.International journal of molecular sciences · 2023
    Review
  6. Article
  7. Complex Relationships between HIV-1 Integrase and Its Cellular Partners.International journal of molecular sciences · 2022
    Review
  8. Contribution of yeast models to virus research.Applied microbiology and biotechnology · 2021
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
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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

7 authors at 4 institutions in 3 countries.

Aviad LevinDepartment of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem 91904, Israel. aviadl@gmail.com
Ayelet Armon-Omer
Joseph Rosenbluh
Naomi Melamed-Book
Adolf Graessmann
Elisabeth Waigmann
Abraham Loyter
Hebrew University of Jerusalem · ILFreie Universität Berlin · DERebecca Sieff Hospital · ILVienna Biocenter · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe integrase (IN) of human immunodeficiency virus type 1 (HIV-1) has been implicated in different steps during viral replication, including nuclear import of the viral pre-integration complex. The exact mechanisms underlying the nuclear import of IN and especially the question of whether it bears a functional nuclear localization signal (NLS) remain controversial.

resultsHere, we studied the nuclear import pathway of IN by using multiple in vivo and in vitro systems. Nuclear import was not observed in an importin alpha temperature-sensitive yeast mutant, indicating an importin alpha-mediated process. Direct interaction between the full-length IN and importin alpha was demonstrated in vivo using bimolecular fluorescence complementation assay (BiFC). Nuclear import studies in yeast cells, with permeabilized mammalian cells, or microinjected cultured mammalian cells strongly suggest that the IN bears a NLS domain located between residues 161 and 173. A peptide bearing this sequence -NLS-IN peptide- inhibited nuclear accumulation of IN in transfected cell-cycle arrested cells. Integration of viral cDNA as well as HIV-1 replication in viral cell-cycle arrested infected cells were blocked by the NLS-IN peptide.

conclusionOur present findings support the view that nuclear import of IN occurs via the importin alpha pathway and is promoted by a specific NLS domain. This import could be blocked by NLS-IN peptide, resulting in inhibition of viral infection, confirming the view that nuclear import of the viral pre-integration complex is mediated by viral IN.

Indexed as

Active Transport, Cell Nucleusalpha KaryopherinsAnimalsCell NucleusChlorocebus aethiopsCOS CellsHeLa CellsHIV-1HIV InfectionsHIV IntegraseHIV Integrase InhibitorsHost-Pathogen InteractionsHumansMetabolic Networks and PathwaysNuclear Localization SignalsVirus Integrationalpha KaryopherinsHIV IntegraseHIV Integrase InhibitorsNuclear Localization Signals

Identifiers

PMID19961612
PMCPMC3224947
OpenAlexW2121195814

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.