Evidence map›Paper›PMID 12117979›Full record

ArticleInfection and immunity2002

Mobilization of protein kinase C in macrophages induced by Listeria monocytogenes affects its internalization and escape from the phagosome.

Sandra J Wadsworth, Howard Goldfine

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2002. 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
5.8field-weighted citation impact, top 4% 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, 88 citations in OpenAlex.

  1. Article
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  4. Life without air.The Journal of biological chemistry · 2020
    Article
  5. Article
  6. Microbiology spectrum · 2018
    Review
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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

2 authors at 1 institution in 1 country.

Sandra J WadsworthDepartment of Microbiology, University of Pennsylvania School of Medicine, Philadelphia 19104-6076, USA.
Howard Goldfine
University of Pennsylvania · US

Funding

PHOSPHOLIPASES AND THE PATHOGENESIS OF LISTERIA MONOCYTOR01AI045153 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI GOLDFINE, HOWARD · 2000 to 2004
$1.4M
PHOSPHOLIPASES AND THE PATHOGENESIS OF LISTERIAR01GM052797 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GOLDFINE, HOWARD · 1995 to 1998
–
NIAID NIH HHS AI 45153NIAID NIH HHS R01 AI045153NIGMS NIH HHS GM 52797
6 · The paper itself

Abstract

Listeriolysin O (LLO) and a phosphatidylinositol-specific phospholipase C (PI-PLC) are known virulence factors of Listeria monocytogenes in both tissue cultures and the murine model of infection. LLO is a member of a family of pore-forming cholesterol-dependent cytotoxins and is known to play an essential role in escape from the primary phagocytic vacuole of macrophages. PI-PLC plays an accessory role, in that PI-PLC mutants are partially defective in escape. We have shown that both of these molecules are essential for initiating rapid increases in the calcium level in the J774 murine macrophage cell line (S. J. Wadsworth and H. Goldfine, Infect. Immun. 67:1770-1778, 1999). Here we show that both LLO and PI-PLC are required for translocation of protein kinase C delta (PKC delta) to the periphery of J774 cells and for translocation of PKC beta II to early endosomes beginning within the first minute after addition of bacteria to the culture medium. Treatment with the calcium channel blocker SK&F 96365 inhibited translocation of PKC beta II but not PKC delta. Our findings lead us to propose a host signaling pathway requiring LLO and the formation of diacylglycerol by PI-PLC in which calcium-independent PKC delta is responsible for the initial calcium signal and the subsequent PKC beta II translocation. LLO-dependent translocation of PKC beta I to early endosomes also occurs between 1 and 4 min after infection, but this occurs in the absence of PI-PLC. All of these signals were observed in cells that had not internalized bacteria. Blocking PKC beta translocation with hispidin resulted in more rapid uptake of wild-type bacteria and greatly reduced escape from the primary phagocytic vacuoles of J774 cells.

Indexed as

Bacterial ToxinsAcetophenonesAnimalsBacterial ProteinsBenzopyransBiological TransportCalcium Channel BlockersCell LineEndosomesEnzyme InhibitorsHeat-Shock ProteinsHemolysin ProteinsImidazolesIsoenzymesListeria monocytogenesMacrophages1-(2-(3-(4-methoxyphenyl)propoxy)-4-methoxyphenylethyl)-1H-imidazoleAcetophenonesBacterial ProteinsBacterial ToxinsBenzopyransCalcium Channel BlockersEnzyme InhibitorsHeat-Shock ProteinsHemolysin ProteinshispidinhlyA protein, Listeria monocytogenesImidazolesIsoenzymesPhosphatidylinositol Diacylglycerol-LyasePhosphoinositide Phospholipase CPrkcd protein, mouseProtein Kinase CProtein Kinase C betaProtein Kinase C-deltaPyronesrottlerinType C Phospholipases

Identifiers

PMID12117979
PMCPMC128209
OpenAlexW2129520858

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.