Evidence map›Paper›PMID 12970459›Full record

ArticleJournal of virology2003

Simian virus 40 T antigens and J domains: analysis of Hsp40 cochaperone functions in Escherichia coli.

Pierre Genevaux, Florence Lang, Françoise Schwager, Jai V Vartikar, Kathleen Rundell, James M Pipas, Costa Georgopoulos, William L Kelley

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Multi-faceted role of HSP40 in cancer.Clinical & experimental metastasis · 2009
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. 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 3 institutions in 2 countries.

Pierre GenevauxDépartement de Biochimie Médicale, Centre Médical Universitaire, Université de Genève, CH-1211 Genève 14, Switzerland.
Florence Lang
Françoise Schwager
Jai V Vartikar
Kathleen Rundell
James M Pipas
Costa Georgopoulos
William L Kelley
University of Geneva · CHUniversity of Pittsburgh · USNorthwestern University · US

Funding

SV40 T ANTIGEN--ROLE IN VIRUS GROWTH AND TRANSFORMATIONR01CA040586 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI PIPAS, JAMES M · 1985 to 2010
$2.7M
SV40 Small-t Antigen and Human Cell TransformationR01CA021327 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI RUNDELL, M KATHLEEN · 1985 to 2006
$1.8M
GENETIC ANALYSIS OF THE SV40 LARGE TUMOR ANTIGENR37CA040586 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI PIPAS, JAMES M · 1988 to 1995
–
NCI NIH HHS CA21327NCI NIH HHS CA40586NCI NIH HHS R01 CA021327NCI NIH HHS R01 CA040586
6 · The paper itself

Abstract

The N-terminal exon of DNA tumor virus T antigens represents a J domain that can direct interaction with the host-encoded Hsp70 chaperones. We have taken advantage of rapid Hsp40 cochaperone assays with Escherichia coli to assess simian virus 40 (SV40)-encoded J-domain loss of function. We found a strong correlation between loss of cochaperone function in E. coli and defective SV40 growth, suggesting that the major role of the J domain in DNA tumor viruses is to provide cochaperone function. We also report the expression of native SV40 virus T antigens in E. coli. Our results show that small t antigen, but not large T antigen (LT) or LT truncation TN125 or TN136, can functionally replace under limited growth conditions DnaJ (Hsp40) function in vivo. In addition, purified small t antigen can efficiently stimulate E. coli DnaK's (Hsp70) ATPase in vitro, thus behaving like a bona fide cochaperone. Furthermore, small t amino acids 83 to 174, which are adjacent to the viral J domain, can replace the E. coli DnaJ J-domain glycine-phenylalanine-rich domain, immediately adjacent to the J-domain sequences, even in the absence of significant amino acid similarity to their DnaJ counterpart. Taken together, our studies demonstrate that functionally related Hsp40 proteins from mammalian viral systems can be rapidly studied in bacteria and exploited to probe the universally conserved Hsp70 chaperone machine mechanism.

Indexed as

Amino Acid SequenceAntigens, Polyomavirus TransformingDNA ReplicationEscherichia coliEscherichia coli ProteinsHeat-Shock ProteinsHSP40 Heat-Shock ProteinsMolecular ChaperonesMolecular Sequence DataMutationAntigens, Polyomavirus TransformingDnaJ protein, E coliEscherichia coli ProteinsHeat-Shock ProteinsHSP40 Heat-Shock ProteinsMolecular Chaperones

Identifiers

PMID12970459
PMCPMC228479
OpenAlexW2120331515

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.