Evidence map›Paper›PMID 28233869›Full record

ArticleScientific reports2017

Interplay between Penicillin-binding proteins and SEDS proteins promotes bacterial cell wall synthesis.

Sophie Leclercq, Adeline Derouaux, Samir Olatunji, Claudine Fraipont, Alexander J F Egan, Waldemar Vollmer, Eefjan Breukink, Mohammed Terrak

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
14.3field-weighted citation impact, top 1% 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

64 citing papers in PubMed, 117 citations in OpenAlex.

  1. Article
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  4. Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025
    Review
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4 more citing papers are in PubMed but not listed here.

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 3 countries.

Sophie LeclercqCentre d'Ingénierie des Protéines, University of Liège, B6a, Quartier Agora, allée du six Août 11, 4000 Liège 1, Belgium.
Adeline DerouauxCentre d'Ingénierie des Protéines, University of Liège, B6a, Quartier Agora, allée du six Août 11, 4000 Liège 1, Belgium.
Samir OlatunjiCentre d'Ingénierie des Protéines, University of Liège, B6a, Quartier Agora, allée du six Août 11, 4000 Liège 1, Belgium.
Claudine FraipontCentre d'Ingénierie des Protéines, University of Liège, B6a, Quartier Agora, allée du six Août 11, 4000 Liège 1, Belgium.
Alexander J F EganInstitute for Cell and Molecular Biosciences, The Centre for Bacterial Cell Biology, Newcastle University, Richardson Road, Newcastle upon Tyne, NE2 4AX, UK.
Waldemar VollmerInstitute for Cell and Molecular Biosciences, The Centre for Bacterial Cell Biology, Newcastle University, Richardson Road, Newcastle upon Tyne, NE2 4AX, UK.
Eefjan BreukinkMembrane Biochemistry and Biophysics, Department of Chemistry, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
Mohammed TerrakCentre d'Ingénierie des Protéines, University of Liège, B6a, Quartier Agora, allée du six Août 11, 4000 Liège 1, Belgium.
University of Liège · BENewcastle University · GBUtrecht University · NL

Funding

Wellcome Trust 101824/Z/13/Z
6 · The paper itself

Abstract

Bacteria utilize specialized multi-protein machineries to synthesize the essential peptidoglycan (PG) cell wall during growth and division. The divisome controls septal PG synthesis and separation of daughter cells. In E. coli, the lipid II transporter candidate FtsW is thought to work in concert with the PG synthases penicillin-binding proteins PBP3 and PBP1b. Yet, the exact molecular mechanisms of their function in complexes are largely unknown. We show that FtsW interacts with PBP1b and lipid II and that PBP1b, FtsW and PBP3 co-purify suggesting that they form a trimeric complex. We also show that the large loop between transmembrane helices 7 and 8 of FtsW is important for the interaction with PBP3. Moreover, we found that FtsW, but not the other flippase candidate MurJ, impairs lipid II polymerization and peptide cross-linking activities of PBP1b, and that PBP3 relieves these inhibitory effects. All together the results suggest that FtsW interacts with lipid II preventing its polymerization by PBP1b unless PBP3 is also present, indicating that PBP3 facilitates lipid II release and/or its transfer to PBP1b after transport across the cytoplasmic membrane. This tight regulatory mechanism is consistent with the cell's need to ensure appropriate use of the limited pool of lipid II.

Indexed as

Bacterial ProteinsCell WallEscherichia coliEscherichia coli ProteinsMembrane ProteinsPenicillin-Binding ProteinsProtein BindingProtein MultimerizationUridine Diphosphate N-Acetylmuramic AcidBacterial ProteinsEscherichia coli ProteinsFtsW protein, BacteriaMembrane Proteinsmuramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenolPenicillin-Binding ProteinsUridine Diphosphate N-Acetylmuramic Acid

Identifiers

PMID28233869
PMCPMC5324115
OpenAlexW2590623784

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.