Evidence map›Paper›PMID 30225797›Full record

ArticleNaunyn-Schmiedeberg's archives of pharmacology2019

Characterization of the glucosyltransferase activity of Legionella pneumophila effector SetA.

Nadezhda Levanova, Marcus Steinemann, Kira E Böhmer, Silvia Schneider, Yury Belyi, Andreas Schlosser, Klaus Aktories, Thomas Jank

Abstract read
PubMed Publisher
In one paragraph

Article in Naunyn-Schmiedeberg's archives of pharmacology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Structural insights into SetA-mediated Rab1 glucosylation and PI3P-guided localization during earlyProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Glycosylating Effectors ofBiomolecules · 2022
    Review
  4. Article
  5. Identification and Characterization of a NovelMolecules (Basel, Switzerland) · 2020
    Article
  6. Article
  7. Interfering with Autophagy: The Opposing Strategies Deployed byFrontiers in cellular and infection microbiology · 2020
    Review
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.

Nadezhda LevanovaInstitute for Experimental and Clinical Pharmacology and Toxicology, Faculty of Medicine, University of Freiburg, Albertstr. 25, 79104, Freiburg, Germany.
Marcus SteinemannInstitute for Experimental and Clinical Pharmacology and Toxicology, Faculty of Medicine, University of Freiburg, Albertstr. 25, 79104, Freiburg, Germany.
Kira E BöhmerInstitute for Experimental and Clinical Pharmacology and Toxicology, Faculty of Medicine, University of Freiburg, Albertstr. 25, 79104, Freiburg, Germany.
Silvia SchneiderInstitute for Experimental and Clinical Pharmacology and Toxicology, Faculty of Medicine, University of Freiburg, Albertstr. 25, 79104, Freiburg, Germany.
Yury BelyiGamaleya Research Centre for Epidemiology and Microbiology, 123098, Moscow, Russia.
Andreas SchlosserRudolf Virchow Center for Experimental Biomedicine, University of Würzburg, 97080, Würzburg, Germany.
Klaus AktoriesInstitute for Experimental and Clinical Pharmacology and Toxicology, Faculty of Medicine, University of Freiburg, Albertstr. 25, 79104, Freiburg, Germany. klaus.aktories@pharmakol.uni-freiburg.de.ORCID 0000-0002-5397-0436
Thomas JankInstitute for Experimental and Clinical Pharmacology and Toxicology, Faculty of Medicine, University of Freiburg, Albertstr. 25, 79104, Freiburg, Germany.
University of Freiburg · DEGamalei Institute of Epidemiology and Microbiology · RUUniversity of Würzburg · DE

Funding

Deutsche Forschungsgemeinschaft project AK6/24-1
6 · The paper itself

Abstract

Legionella pneumophila glucosyltransferase SetA, which is introduced into target cells by a type IV secretion system, affects the intracellular traffic of host cells. Here, we characterized the enzyme activity of the Legionella effector. We report that Asp118 and Arg121 of SetA are essential for glucohydrolase and glucotransferase activities. Exchange of Trp36 to alanine reduced the enzyme activity of SetA. All three amino acids were crucial for the cytotoxic effects of SetA in yeast. We observed that phosphatidylinositol-3-phosphate (PI3P) increased the glucosyltransferase activity of SetA severalfold, while the glucohydrolase activity was not affected. In the presence of PI3P, we observed the glucosylation of actin, vimentin and the chaperonin CCT5 in the cytosolic fraction of target cells. Studies on the functional consequences of glucosylation of skeletal muscle α-actin in vitro revealed inhibition of actin polymerization by glucosylation.

Indexed as

Amino AcidsAnimalsBacterial ProteinsCHO CellsCricetulusEscherichia coliGlucosyltransferasesHumansJurkat CellsLegionella pneumophilaMutagenesis, Site-DirectedPhosphatidylinositol PhosphatesSaccharomyces cerevisiaeAmino AcidsBacterial ProteinsGlucosyltransferasesphosphatidylinositol 3-phosphatePhosphatidylinositol PhosphatesActin polymerizationCCT5Enzyme activityGlucosylationLegionella pneumophila effector SetAVimentin

Identifiers

PMID30225797
OpenAlexW2892381555

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.