Evidence map›Paper›PMID 15596813›Full record

ArticleJournal of virology2005

Cyclophilin interactions with incoming human immunodeficiency virus type 1 capsids with opposing effects on infectivity in human cells.

Theodora Hatziioannou, David Perez-Caballero, Simone Cowan, Paul D Bieniasz

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing papers in PubMed
5.1field-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

123 citing papers in PubMed, 191 citations in OpenAlex.

  1. Article
  2. Review
  3. Capsid-host interactions for HIV-1 ingress.Microbiology and molecular biology reviews : MMBR · 2023
    Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Shielding the HIV-1 capsid.Nature microbiology · 2020
    Article
  19. Article
  20. Article

63 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

4 authors at 2 institutions in 1 country.

Theodora HatziioannouAaron Diamond AIDS Research Center and Rockefeller University, New York, New York 10021, USA.
David Perez-Caballero
Simone Cowan
Paul D Bieniasz
Aaron Diamond AIDS Research Center · USRockefeller University · US

Funding

RNA Protein interactions in HIV-1 replicationR01AI050111 · NIAID · ROCKEFELLER UNIVERSITY · PI BIENIASZ, PAUL D. · 2001 to 2021
$7.9M
NIAID NIH HHS R01 AI050111NIAID NIH HHS R01AI50111
6 · The paper itself

Abstract

Cyclophilin A (CypA) is a peptidyl-prolyl isomerase that binds to the capsid protein (CA) of human immunodeficiency virus type 1 (HIV-1) and by doing so facilitates HIV-1 replication. Although CypA is incorporated into HIV-1 virions by virtue of CypA-Gag interactions that occur during virion assembly, in this study we show that the CypA-CA interaction that occurs following the entry of the viral capsid into target cells is the major determinant of CypA's effects on HIV-1 replication. Specifically, by using normal and CypA-deficient Jurkat cells, we demonstrate that the presence of CypA in the target and not the virus-producing cell enhances HIV-1 infectivity. Moreover, disruption of the CypA-CA interaction with cyclosporine A (CsA) inhibits HIV-1 infectivity only if the target cell expresses CypA. The effect of CsA on HIV-1 infection of human cells varies according to which particular cell line is used as a target, and CA mutations that confer CsA resistance and dependence exert their effects only if target cells, and not if virus-producing cells, are treated with CsA. The differential effects of CsA on HIV-1 infection in different human cells appear not to be caused by polymorphisms in the recently described retrovirus restriction factor TRIM5alpha. We speculate that CypA and/or CypA-related proteins affect the fate of incoming HIV-1 capsid either directly or by modulating interactions with unidentified host cell factors.

Indexed as

AnimalsAntiviral Restriction FactorsCapsidCapsid ProteinsCarrier ProteinsCell LineCyclophilin ACyclosporineHeLa CellsHIV-1HumansJurkat CellsMutationPeptidylprolyl IsomeraseTripartite Motif ProteinsUbiquitin-Protein LigasesAntiviral Restriction FactorsCapsid ProteinsCarrier ProteinsCyclophilin ACyclosporinePeptidylprolyl IsomeraseTRIM5 protein, humanTripartite Motif ProteinsUbiquitin-Protein Ligases

Identifiers

PMID15596813
PMCPMC538701
OpenAlexW2169732011

What OpenQuestion holds

Textmetadata
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.