Evidence map›Paper›PMID 9596723›Full record

ArticleInfection and immunity1998

Modification of Ras in eukaryotic cells by Pseudomonas aeruginosa exoenzyme S.

E M McGuffie, D W Frank, T S Vincent, J C Olson

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

34 citing papers in PubMed, 74 citations in OpenAlex.

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  11. The role of potassium in inflammasome activation by bacteria.The Journal of biological chemistry · 2010
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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

4 authors at 2 institutions in 1 country.

E M McGuffieDepartment of Pathology and Laboratory Medicine, Medical University of South Carolina, Charleston, South Carolina 29425, USA.
D W Frank
T S Vincent
J C Olson
Medical University of South Carolina · USMedical College of Wisconsin · US

Funding

FUNCTIONAL DISSECTION OF BACTERIAL TOXINSR01AI030558 · NIAID · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI OLSON, JOAN C. · 1994 to 1996
–
NIAID NIH HHS AI30558
6 · The paper itself

Abstract

Genetic and functional data suggest that Pseudomonas aeruginosa exoenzyme S (ExoS), an ADP-ribosyltransferase, is translocated into eukaryotic cells by a bacterial type III secretory mechanism activated by contact between bacteria and host cells. Although purified ExoS is not toxic to eukaryotic cells, ExoS-producing bacteria cause reduced proliferation and viability, possibly mediated by bacterially translocated ExoS. To investigate the activity of translocated ExoS, we examined in vivo modification of Ras, a preferred in vitro substrate. The ExoS-producing strain P. aeruginosa 388 and an isogenic mutant strain, 388DeltaexoS, which fails to produce ExoS, were cocultured with HT29 colon carcinoma cells. Ras was found to be ADP-ribosylated during coculture with 388 but not with 388DeltaexoS, and Ras modification by 388 corresponded with reduction in HT29 cell DNA synthesis. Active translocation by bacteria was found to be required, since exogenous ExoS, alone or in the presence of 388DeltaexoS, was unable to modify intracellular Ras. Other ExoS-producing strains caused modification of Ras, indicating that this is not a strain-specific event. ADP-ribosylation of Rap1, an additional Ras family substrate for ExoS in vitro, was not detectable in vivo under conditions sufficient for Ras modification, suggesting possible ExoS substrate preference among Ras-related proteins. These results confirm that intracellular Ras is modified by bacterially translocated ExoS and that the inhibition of target cell proliferation correlates with the efficiency of Ras modification.

Indexed as

ADP Ribose TransferasesBacterial ToxinsAdenosine Diphosphate RiboseDNA, NeoplasmEukaryotic CellsGTP-Binding ProteinsHT29 CellsHumansPoly(ADP-ribose) PolymerasesProtein Processing, Post-TranslationalPseudomonas aeruginosarap GTP-Binding Proteinsras ProteinsSpecies SpecificitySubstrate SpecificityAdenosine Diphosphate RiboseADP Ribose TransferasesBacterial ToxinsDNA, Neoplasmexoenzyme SGTP-Binding ProteinsPoly(ADP-ribose) Polymerasesrap GTP-Binding Proteinsras Proteins

Identifiers

PMID9596723
PMCPMC108245
OpenAlexW2122965577

What OpenQuestion holds

Textmetadata
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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.