Evidence map›Paper›PMID 23714361›Full record

ArticleMolecular oral microbiology2013

Gingipain-dependent degradation of mammalian target of rapamycin pathway proteins by the periodontal pathogen Porphyromonas gingivalis during invasion.

P Stafford, J Higham, A Pinnock, C Murdoch, C W I Douglas, G P Stafford, D W Lambert

Abstract read
In one paragraph

Article in Molecular oral microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

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  10. Microbiome-mediated incapacitation of interferon lambda production in the oral mucosa.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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

7 authors at 1 institution in 1 country.

P StaffordIntegrated Bioscience, School of Clinical Dentistry, University of Sheffield, Sheffield, UK.
J Higham
A Pinnock
C Murdoch
C W I Douglas
G P Stafford
D W Lambert
University of Sheffield · GB

Funding

The Dunhill Medical Trust R141/1109
6 · The paper itself

Abstract

Porphyromonas gingivalis and Tannerella forsythia are gram-negative pathogens strongly associated with periodontitis. Their abilities to interact, invade and persist within host cells are considered crucial to their pathogenicity, but the mechanisms by which they subvert host defences are not well understood. In this study, we set out to investigate whether P. gingivalis and T. forsythia directly target key signalling molecules that may modulate the host cell phenotype to favour invasion and persistence. Our data identify, for the first time, that P. gingivalis, but not T. forsythia, reduces levels of intracellular mammalian target of rapamycin (mTOR) in oral epithelial cells following invasion over a 4-h time course, via the action of gingipains. The ability of cytochalasin D to abrogate P. gingivalis-mediated mTOR degradation suggests that this effect is dependent upon cellular invasion. We also show that levels of several other proteins in the mTOR signalling pathway are modulated by gingipains, either directly or as a consequence of mTOR degradation including p-4E-BP1. Taken together, our data suggest that P. gingivalis manipulates the mTOR pathway, providing evidence for a potentially novel mechanism by which P. gingivalis mediates its effects on host cell responses to infection.

Indexed as

Adaptor Proteins, Signal TransducingAdhesins, BacterialBacteroidaceae InfectionsBacteroidesBacteroides InfectionsCarrier ProteinsCell LineCell Line, TumorCysteine EndopeptidasesCytochalasin DEpithelial CellsGingipain Cysteine EndopeptidasesHumansKeratinocytesMechanistic Target of Rapamycin Complex 1Mechanistic Target of Rapamycin Complex 2Adaptor Proteins, Signal TransducingAdhesins, BacterialCarrier ProteinsCysteine EndopeptidasesCytochalasin DGingipain Cysteine EndopeptidasesMechanistic Target of Rapamycin Complex 1Mechanistic Target of Rapamycin Complex 2Multiprotein ComplexesNucleic Acid Synthesis InhibitorsOncogene Protein v-aktRapamycin-Insensitive Companion of mTOR ProteinRegulatory-Associated Protein of mTORRICTOR protein, humanRPTOR protein, humanTOR Serine-Threonine Kinasesdegradationgingipainsmammalian target of rapamycinperiodontitisPorphyromonas gingivalis

Identifiers

PMID23714361
PMCPMC4993231
OpenAlexW2133645349

What OpenQuestion holds

Textmetadata
LicenceTDM
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.