Evidence map›Paper›PMID 16940531›Full record

ArticleJournal of virology2006

Novel function of prothymosin alpha as a potent inhibitor of human immunodeficiency virus type 1 gene expression in primary macrophages.

Arevik Mosoian, Avelino Teixeira, Anthony A High, Robert E Christian, Donald F Hunt, Jeffrey Shabanowitz, Xinyan Liu, Mary Klotman

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
0.8field-weighted citation impact, top 35% 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

25 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The CD8Microbiology and molecular biology reviews : MMBR · 2021
    Review
  6. Identification of Diagnostic Markers Correlated With HIVFrontiers in molecular biosciences · 2021
    Article
  7. Article
  8. Canonical Wnts Mediate CD8Journal of immunology (Baltimore, Md. : 1950) · 2020
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Soluble factors from T cells inhibiting X4 strains of HIV are a mixture of β chemokines and RNases.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  18. Article
  19. Article
  20. Molecular Understanding of HIV-1 Latency.Advances in virology · 2012
    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 2 institutions in 1 country.

Arevik MosoianDepartment of Medicine, Division of Infectious Diseases, Mount Sinai School of Medicine, Box 1090, New York, NY 10029, USA.
Avelino Teixeira
Anthony A High
Robert E Christian
Donald F Hunt
Jeffrey Shabanowitz
Xinyan Liu
Mary Klotman
Icahn School of Medicine at Mount Sinai · USUniversity of Virginia · US

Funding

PROTEIN SEQUENCING BY TANDEM MASS SPECTROMETRYR01GM037537 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HUNT, DONALD F · 1987 to 2023
$17.8M
HIV1 INHIBITORY PROTEINS FROM TRANSFORMED CD8+ CELLSR01AI043698 · NIAID · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI KLOTMAN, MARY E. · 1998 to 2002
$831k
NIAID NIH HHS AI 043698-02NIGMS NIH HHS R01 GM037537
6 · The paper itself

Abstract

CD8(+) T lymphocytes control human immunodeficiency virus type 1 (HIV-1) infection by a cytotoxic major histocompatibility complex-restricted pathway as well as by secretion of noncytotoxic soluble inhibitory factors. Several components of CD8(+) cell supernatants have been identified that contribute to the latter activity. In this study we report that prothymosin alpha (ProTalpha), a protein found in the cell culture medium of the herpesvirus saimiri-transformed CD8(+) T-cell line, K#1 50K, has potent HIV-1-inhibitory activity. Depletion of native ProTalpha from an HIV-1-inhibitory fraction of CD8(+) cell supernatants removes the inhibitory activity, supporting its role in inhibition via soluble mediators. ProTalpha is an abundant, acidic peptide that has been reported to be localized in the nucleus and associated with cell proliferation and activation of transcription. In this report we demonstrate that ProTalpha suppresses HIV-1 replication, its activity is target cell specific, and inhibition occurs following viral integration. Native and recombinant ProTalpha protein potently inhibit HIV-1 long terminal repeat (LTR)-driven gene expression in macrophages. Furthermore studies using different promoters in lentiviral vectors (cytomegalovirus and phosphoglycerate kinase) revealed that suppression of viral replication by ProTalpha is not HIV LTR specific.

Indexed as

Gene Expression Regulation, ViralHIV Long Terminal RepeatAnti-HIV AgentsCD8-Positive T-LymphocytesHeLa CellsHIV-1HumansLentivirusMacrophagesPromoter Regions, GeneticProtein PrecursorsThymosinVirus ReplicationAnti-HIV AgentsProtein Precursorsprothymosin alphaThymosin

Identifiers

PMID16940531
PMCPMC1563913
OpenAlexW2005667005

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.