Evidence map›Paper›PMID 18606736›Full record

ArticleJournal of bacteriology2008

Lawsonia intracellularis contains a gene encoding a functional rickettsia-like ATP/ADP translocase for host exploitation.

Stephan Schmitz-Esser, Ilka Haferkamp, Silvia Knab, Thomas Penz, Michelle Ast, Christian Kohl, Michael Wagner, Matthias Horn

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
5.1field-weighted citation impact, top 5% 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

17 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  5. Frontiers in veterinary science · 2018
    Review
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  16. Diatom plastids depend on nucleotide import from the cytosol.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  17. 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 2 institutions in 2 countries.

Stephan Schmitz-EsserUniversität Wien, Department für Mikrobielle Okologie, Althanstr. 14, A-1090 Vienna, Austria.
Ilka Haferkamp
Silvia Knab
Thomas Penz
Michelle Ast
Christian Kohl
Michael Wagner
Matthias Horn
University of Vienna · ATUniversity of Kaiserslautern · DE

Funding

Austrian Science Fund FWF P 19252
6 · The paper itself

Abstract

ATP/ADP translocases are a hallmark of obligate intracellular pathogens related to chlamydiae and rickettsiae. These proteins catalyze the highly specific exchange of bacterial ADP against host ATP and thus allow bacteria to exploit their hosts' energy pool, a process also referred to as energy parasitism. The genome sequence of the obligate intracellular pathogen Lawsonia intracellularis (Deltaproteobacteria), responsible for one of the most economically important diseases in the swine industry worldwide, revealed the presence of a putative ATP/ADP translocase most similar to known ATP/ADP translocases of chlamydiae and rickettsiae (around 47% amino acid sequence identity). The gene coding for the putative ATP/ADP translocase of L. intracellularis (L. intracellularis nucleotide transporter 1 [NTT1(Li)]) was cloned and expressed in the heterologous host Escherichia coli. The transport properties of NTT1(Li) were determined by measuring the uptake of radioactively labeled substrates by E. coli. NTT1(Li) transported ATP in a counterexchange mode with ADP in a highly specific manner; the substrate affinities determined were 236.3 (+/- 36.5) microM for ATP and 275.2 (+/- 28.1) microM for ADP, identifying this protein as a functional ATP/ADP translocase. NTT1(Li) is the first ATP/ADP translocase from a bacterium not related to Chlamydiae or Rickettsiales, showing that energy parasitism by ATP/ADP translocases is more widespread than previously recognized. The occurrence of an ATP/ADP translocase in L. intracellularis is explained by a relatively recent horizontal gene transfer event with rickettsiae as donors.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateBacterial ProteinsBiological TransportChromatography, Thin LayerEscherichia coliEukaryotic CellsGene Transfer, HorizontalHost-Pathogen InteractionsKineticsLawsonia BacteriaMitochondrial ADP, ATP TranslocasesMolecular Sequence DataPhylogenyPolymerase Chain ReactionRickettsiaAdenosine DiphosphateAdenosine TriphosphateBacterial ProteinsMitochondrial ADP, ATP Translocases

Identifiers

PMID18606736
PMCPMC2519521
OpenAlexW2010365159

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.