Evidence map›Paper›PMID 22022378›Full record

ArticlePloS one2011

Functional analysis of the cytoskeleton protein MreB from Chlamydophila pneumoniae.

Ahmed Gaballah, Anna Kloeckner, Christian Otten, Hans-Georg Sahl, Beate Henrichfreise

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.0field-weighted citation impact, top 7% 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

28 citing papers in PubMed, 47 citations in OpenAlex.

  1. Infection and immunity · 2026
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  2. Review
  3. Biological Regulation StudiedAccounts of chemical research · 2025
    Article
  4. Article
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  6. Solubility and Thermal Stability ofInternational journal of molecular sciences · 2022
    Article
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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

5 authors at 1 institution in 1 country.

Ahmed GaballahUniversity of Bonn, Institute for Medical Microbiology, Immunology and Parasitology, Pharmaceutical Microbiology Section, Bonn, Germany.
Anna Kloeckner
Christian Otten
Hans-Georg Sahl
Beate Henrichfreise
University of Bonn · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In rod-shaped bacteria, the bacterial actin ortholog MreB is considered to organize the incorporation of cell wall precursors into the side-wall, whereas the tubulin homologue FtsZ is known to tether incorporation of cell wall building blocks at the developing septum. For intracellular bacteria, there is no need to compensate osmotic pressure by means of a cell wall, and peptidoglycan has not been reliably detected in Chlamydiaceae. Surprisingly, a nearly complete pathway for the biosynthesis of the cell wall building block lipid II has been found in the genomes of Chlamydiaceae. In a previous study, we discussed the hypothesis that conservation of lipid II biosynthesis in cell wall-lacking bacteria may reflect the intimate molecular linkage of cell wall biosynthesis and cell division and thus an essential role of the precursor in cell division. Here, we investigate why spherical-shaped chlamydiae harbor MreB which is almost exclusively found in elongated bacteria (i.e. rods, vibrios, spirilla) whereas they lack the otherwise essential division protein FtsZ. We demonstrate that chlamydial MreB polymerizes in vitro and that polymerization is not inhibited by the blocking agent A22. As observed for MreB from Bacillus subtilis, chlamydial MreB does not require ATP for polymerization but is capable of ATP hydrolysis in phosphate release assays. Co-pelleting and bacterial two-hybrid experiments indicate that MreB from Chlamydophila (Chlamydia) pneumoniae interacts with MurF, MraY and MurG, three key components in lipid II biosynthesis. In addition, MreB polymerization is improved in the presence of MurF. Our findings suggest that MreB is involved in tethering biosynthesis of lipid II and as such may be necessary for maintaining a functional divisome machinery in Chlamydiaceae.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsChlamydophila pneumoniaeCytoskeletal ProteinsHydrolysisModels, BiologicalMutant ProteinsPolymerizationProtein BindingThioureaTwo-Hybrid System TechniquesUridine Diphosphate N-Acetylmuramic Acid2,6-dichlorobenzylthiopseudoureaAdenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsCytoskeletal Proteinsmuramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenolMutant ProteinsThioureaUridine Diphosphate N-Acetylmuramic Acid

Identifiers

PMID22022378
PMCPMC3187750
OpenAlexW1996193885

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.