Evidence map›Paper›PMID 12874317›Full record

ArticleInfection and immunity2003

Biochemical and functional analyses of the Mip protein: influence of the N-terminal half and of peptidylprolyl isomerase activity on the virulence of Legionella pneumophila.

Rolf Köhler, Jörg Fanghänel, Bettina König, Edeltraud Lüneberg, Matthias Frosch, Jens-Ulrich Rahfeld, Rolf Hilgenfeld, Gunter Fischer, Jörg Hacker, Michael Steinert

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In one paragraph

Article in Infection and immunity, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.3field-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

26 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
  2. Article
  3. Protein sociology of ProA, Mip and other secreted virulence factors at theFrontiers in cellular and infection microbiology · 2023
    Review
  4. Review
  5. Article
  6. Biochemical and functional characterization ofFrontiers in microbiology · 2022
    Article
  7. Structural characterization of PaFkbA: A periplasmic chaperone fromComputational and structural biotechnology journal · 2021
    Article
  8. Peptidyl-Prolyl-Infection and immunity · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

10 authors at 3 institutions in 2 countries.

Rolf KöhlerInstitut für Molekulare Infektionsbiologie, Universität Würzburg, D-97070 Würzburg, Germany.
Jörg Fanghänel
Bettina König
Edeltraud Lüneberg
Matthias Frosch
Jens-Ulrich Rahfeld
Rolf Hilgenfeld
Gunter Fischer
Jörg Hacker
Michael Steinert
Max Planck Research Unit for Enzymology of Protein Folding · DEInstitute of Molecular Biotechnology · ATUniversity of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The virulence factor Mip (macrophage infectivity potentiator) contributes to the intracellular survival of Legionella pneumophila, the causative agent of Legionnaires' disease. The protein consists of two domains that are connected via a very long alpha-helix (A. Riboldi-Tunnicliffe et al., Nat. Struct. Biol. 8:779-783, 2001). The fold of the C-terminal domain (residues 100 to 213) is closely related to human FK506-binding protein (FKBP12), and like FKBP12, Mip exhibits peptidylprolyl cis/trans isomerase (PPIase) activity. The alpha-helical N-terminal domain is responsible for the formation of very stable Mip homodimers. In order to determine the importance of the homodimeric state of Mip for its biochemical activities and for infectivity of Legionella, a truncated, monomeric Mip variant [Mip((77-213))] was overexpressed in Escherichia coli and characterized biochemically. In vitro isomerase activity assays revealed that the altered protein exhibits full isomerase activity towards peptide substrates. However, the deletion resulted in a dramatic loss in the efficiency of refolding of reduced and carboxy-methylated RNase T(1). By cis complementation of the Mip-negative mutant strain L. pneumophila JR32-2, we constructed the strain L. pneumophila JR32-2.4, which expresses an N-terminally truncated variant of Mip. Infection studies with these strains revealed that the N-terminal part and the dimerization of Mip but not its PPIase activity are necessary for full virulence in Acanthamoeba castellanii. Infection of guinea pigs showed that strains with dimerization-deficient Mip (JR32-2.4) or a very low PPIase activity (JR32-2.2) were significantly attenuated in the animal model. These results suggest a different role of the PPIase activity and the N-terminally mediated dimeric state of Mip in monocellular systems and during the infection of guinea pigs.

Indexed as

AcanthamoebaAnimalsBacterial ProteinsChymotrypsinDisease Models, AnimalGuinea PigsHumansImmunophilinsLegionella pneumophilaLegionnaires' DiseaseMaleMembrane ProteinsMutationPeptide FragmentsPeptidylprolyl IsomeraseRecombinant ProteinsBacterial ProteinsChymotrypsinImmunophilinsMembrane ProteinsMip protein, Legionella pneumophilaPeptide FragmentsPeptidylprolyl IsomeraseRecombinant Proteins

Identifiers

PMID12874317
PMCPMC166037
OpenAlexW2152674241

What OpenQuestion holds

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Registered trials

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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.