Evidence map›Paper›PMID 24753244›Full record

ArticleThe Journal of biological chemistry2014

Functional identification of conserved residues involved in Lactobacillus rhamnosus strain GG sortase specificity and pilus biogenesis.

François P Douillard, Pia Rasinkangas, Ingemar von Ossowski, Justus Reunanen, Airi Palva, Willem M de Vos

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Characterization of Highly Mucus-Adherent Non-GMO Derivatives ofFrontiers in bioengineering and biotechnology · 2020
    Article
  9. Novel Molecular Insights about Lactobacillar Sortase-Dependent Piliation.International journal of molecular sciences · 2017
    Review
  10. Structure and specificity of a new class of CaThe Journal of biological chemistry · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

6 authors at 2 institutions in 2 countries.

François P DouillardFrom the Department of Veterinary Biosciences, University of Helsinki, Helsinki 00790, Finland and francois.douillard@helsinki.fi.
Pia RasinkangasFrom the Department of Veterinary Biosciences, University of Helsinki, Helsinki 00790, Finland and.
Ingemar von OssowskiFrom the Department of Veterinary Biosciences, University of Helsinki, Helsinki 00790, Finland and.
Justus ReunanenFrom the Department of Veterinary Biosciences, University of Helsinki, Helsinki 00790, Finland and.
Airi PalvaFrom the Department of Veterinary Biosciences, University of Helsinki, Helsinki 00790, Finland and.
Willem M de VosFrom the Department of Veterinary Biosciences, University of Helsinki, Helsinki 00790, Finland and the Laboratory of Microbiology, Wageningen University, 6708 PB Wageningen, The Netherlands.
University of Helsinki · FIWageningen University & Research · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In Gram-positive bacteria, sortase-dependent pili mediate the adhesion of bacteria to host epithelial cells and play a pivotal role in colonization, host signaling, and biofilm formation. Lactobacillus rhamnosus strain GG, a well known probiotic bacterium, also displays on its cell surface mucus-binding pilus structures, along with other LPXTG surface proteins, which are processed by sortases upon specific recognition of a highly conserved LPXTG motif. Bioinformatic analysis of all predicted LPXTG proteins encoded by the L. rhamnosus GG genome revealed a remarkable conservation of glycine residues juxtaposed to the canonical LPXTG motif. Here, we investigated and defined the role of this so-called triple glycine (TG) motif in determining sortase specificity during the pilus assembly and anchoring. Mutagenesis of the TG motif resulted in a lack or an alteration of the L. rhamnosus GG pilus structures, indicating that the TG motif is critical in pilus assembly and that they govern the pilin-specific and housekeeping sortase specificity. This allowed us to propose a regulatory model of the L. rhamnosus GG pilus biogenesis. Remarkably, the TG motif was identified in multiple pilus gene clusters of other Gram-positive bacteria, suggesting that similar signaling mechanisms occur in other, mainly pathogenic, species.

Indexed as

AminoacyltransferasesBacterial AdhesionBacterial ProteinsCysteine EndopeptidasesEnzyme ActivationFimbriae, BacterialFimbriae ProteinsGlycineLacticaseibacillus rhamnosusMicroscopy, Electron, TransmissionMutagenesis, Site-DirectedProbioticsSignal TransductionSubstrate SpecificityAminoacyltransferasesBacterial ProteinsCysteine EndopeptidasesFimbriae ProteinsGlycinesortase ABacterial AdhesionElectron Microscopy (EM)Protein MotifSignalingSite-directed Mutagenesis

Identifiers

PMID24753244
PMCPMC4140931
OpenAlexW2010599934

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.