Evidence map›Paper›PMID 10515919›Full record

ArticleJournal of bacteriology1999

In vitro characterization of peptidoglycan-associated lipoprotein (PAL)-peptidoglycan and PAL-TolB interactions.

E Bouveret, H Bénédetti, A Rigal, E Loret, C Lazdunski

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

43 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
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  4. Microbiology spectrum · 2025
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  8. Article
  9. Article
  10. Peptidoglycan-Binding Anchor Is aFrontiers in microbiology · 2021
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Outer membrane lipoprotein biogenesis: Lol is not the end.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015
    Review
  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

5 authors at 2 institutions in 1 country.

E BouveretLaboratoire d'Ingéniérie des Systèmes Macromoléculaires, Institut de Biologie Structurale et Microbiologie, Centre National de la Recherche Scientifique (CNRS), 13402 Marseille Cedex 20, France.
H Bénédetti
A Rigal
E Loret
C Lazdunski
Centre National de la Recherche Scientifique · FRInstitut de Biologie Structurale · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Tol-peptidoglycan-associated lipoprotein (PAL) system of Escherichia coli is a multiprotein complex of the envelope involved in maintaining outer membrane integrity. PAL and the periplasmic protein TolB, two components of this complex, are interacting with each other, and they have also been reported to interact with OmpA and the major lipoprotein, two proteins interacting with the peptidoglycan. All these interactions suggest a role of the Tol-PAL system in anchoring the outer membrane to the peptidoglycan. Therefore, we were interested in better understanding the interaction between PAL and the peptidoglycan. We designed an in vitro interaction assay based on the property of purified peptidoglycan to be pelleted by ultracentrifugation. Using this assay, we showed that a purified PAL protein interacted in vitro with pure peptidoglycan. A peptide competition experiment further demonstrated that the region from residues 89 to 130 of PAL was sufficient to bind the peptidoglycan. Moreover, the fact that this same region of PAL was also binding to TolB suggested that these two interactions were exclusive. Indeed, the TolB-PAL complex appeared not to be associated with the peptidoglycan. This led us to the conclusion that PAL may exist in two forms in the cell envelope, one bound to TolB and the other bound to the peptidoglycan.

Indexed as

Escherichia coli ProteinsPeriplasmic ProteinsProteoglycansAmino Acid SequenceBacterial Outer Membrane ProteinsBacterial ProteinsBinding, CompetitiveBinding SitesCell MembraneCell WallCross-Linking ReagentsEscherichia coliHaemophilus influenzaeLipoproteinsMembrane ProteinsMolecular Sequence DataBacterial Outer Membrane ProteinsBacterial ProteinsCross-Linking ReagentsEscherichia coli ProteinsExcC protein, E coliLipoproteinsMembrane ProteinsPeptide FragmentsPeptidoglycanPeriplasmic ProteinsPplA protein, Legionella pneumophilaProteoglycanstolB protein, E coli

Identifiers

PMID10515919
PMCPMC103764
OpenAlexW2151330132

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.