Evidence map›Paper›PMID 11222675›Full record

ArticleJournal of virology2001

Type D retrovirus Gag polyprotein interacts with the cytosolic chaperonin TRiC.

S Hong, G Choi, S Park, A S Chung, E Hunter, S S Rhee

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

38 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
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  3. Article
  4. Review
  5. Review
  6. Article
  7. Structural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC/CCT chaperone network.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. The Mechanism and Function of Group II Chaperonins.Journal of molecular biology · 2015
    Review
  18. Article
  19. Article
  20. 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

6 authors at 4 institutions in 2 countries.

S HongLaboratory of Molecular Virology, Samsung Biomedical Research Institute, Seoul, Korea.
G Choi
S Park
A S Chung
E Hunter
S S Rhee
Samsung (South Korea) · KRBiomedical Research Institute · USKorea Advanced Institute of Science and Technology · KRUniversity of Alabama at Birmingham · US

Funding

GENETICS OF PRIMATE D TYPE RETROVIRUSESR01CA027834 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI HUNTER, ERIC · 1985 to 2011
$3.6M
GENETICS OF PRIMATE D TYPE RETROVIRUSESR37CA027834 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI HUNTER, ERIC · 1991 to 1999
–
NCI NIH HHS R01 CA027834NCI NIH HHS R37 CA027834NCI NIH HHS R39 CA27834
6 · The paper itself

Abstract

The carboxy terminus-encoding portion of the gag gene of Mason-Pfizer monkey virus (M-PMV), the prototype immunosuppressive primate type D retrovirus, encodes a 36-amino-acid, proline-rich protein domain that, in the mature virion, becomes the p4 capsid protein. The p4 domain has no known role in M-PMV replication. We found that two mutants with premature termination codons that remove half or all of the p4 domain produced lower levels of stable Gag protein and of self-assembled capsids. Interestingly, yeast two-hybrid screening revealed that p4 specifically interacted with TCP-1gamma, a subunit of the chaperonin TRiC (TCP-1 ring complex). TRiC is a cytosolic chaperonin that is known to be involved in both folding and subunit assembly of a variety of cellular proteins. TCP-1gamma also associated with high specificity with the M-PMV pp24/16-p12 domain and human immunodeficiency virus p6. Moreover, in cells, Gag polyprotein associated with the TRiC chaperonin complex and this association depended on ATP hydrolysis. In the p4 truncation mutants, the Gag-TRiC association was significantly reduced. These results strongly suggest that cytosolic chaperonin TRiC is involved in Gag folding and/or capsid assembly. We propose that TRiC associates transiently with nascent M-PMV Gag molecules to assist in their folding. Consequently, properly folded Gag molecules carry out the intermolecular interactions involved in self-assembly of the immature capsid.

Indexed as

Intracellular Signaling Peptides and ProteinsMicrotubule-Associated ProteinsCapsidChaperonin Containing TCP-1ChaperoninsCytosolGene Products, gagMason-Pfizer monkey virusNuclear ProteinsProtein Foldingt-Complex Genome RegionTwo-Hybrid System TechniquesUbiquitin-Protein LigasesVirus AssemblyChaperonin Containing TCP-1ChaperoninsGene Products, gagIntracellular Signaling Peptides and ProteinsMicrotubule-Associated ProteinsNuclear ProteinsPPP1R11 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID11222675
PMCPMC115874
OpenAlexW2008337475

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.