Evidence map›Paper›PMID 17951390›Full record

ArticleJournal of bacteriology2007

O-linked glycosylation ensures the normal conformation of the autotransporter adhesin involved in diffuse adherence.

Marie-Eve Charbonneau, Victoria Girard, Anastasia Nikolakakis, Manuel Campos, Frédéric Berthiaume, France Dumas, François Lépine, Michael Mourez

Abstract read
In one paragraph

Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.5field-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

32 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Biofilm Formation byMicroorganisms · 2023
    Article
  5. Review
  6. Review
  7. Review
  8. Adhesive Functions or Pseudogenization of Type Va Autotransporters inFrontiers in cellular and infection microbiology · 2021
    Article
  9. Review
  10. Article
  11. Quantitative Proteomic Profiling of Marine DiatomFrontiers in microbiology · 2020
    Article
  12. Protein post-translational modifications in bacteria.Nature reviews. Microbiology · 2019
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014
    Review
  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

8 authors at 3 institutions in 1 country.

Marie-Eve CharbonneauUniversité de Montréal, Faculté de Médecine Vétérinaire, 3200 Sicotte, St.-Hyacinthe, Québec J2S 7C6, Canada.
Victoria Girard
Anastasia Nikolakakis
Manuel Campos
Frédéric Berthiaume
France Dumas
François Lépine
Michael Mourez
Université de Montréal · CAInstitut National de la Recherche Scientifique · CABiotechnology Research Institute · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Escherichia coli adhesin involved in diffuse adherence (AIDA-I) is one of the few glycosylated proteins found in Escherichia coli. Glycosylation is mediated by a specific heptosyltransferase encoded by the aah gene, but little is known about the role of this modification and the mechanism involved. In this study, we identified several peptides of AIDA-I modified by the addition of heptoses by use of mass spectrometry and N-terminal sequencing of proteolytic fragments of AIDA-I. One threonine and 15 serine residues were identified as bearing heptoses, thus demonstrating for the first time that AIDA-I is O-glycosylated. We observed that unglycosylated AIDA-I is expressed in smaller amounts than its glycosylated counterpart and shows extensive signs of degradation upon heat extraction. We also observed that unglycosylated AIDA-I is more sensitive to proteases and induces important extracytoplasmic stress. Lastly, as was previously shown, we noted that glycosylation is required for AIDA-I to mediate adhesion to cultured epithelial cells, but purified mature AIDA-I fused to GST was found to bind in vitro to cells whether or not it was glycosylated. Taken together, our results suggest that glycosylation is required to ensure a normal conformation of AIDA-I and may be only indirectly necessary for its cell-binding function.

Indexed as

Protein ConformationProtein Processing, Post-TranslationalAdhesins, Escherichia coliBacterial AdhesionCell LineEpithelial CellsEscherichia coliGlycosylationHeptosesHumansMass SpectrometryPeptide HydrolasesPeptidesSequence Analysis, ProteinSerineThreonineAdhesins, Escherichia coliAIDA-I protein, E coliHeptosesPeptide HydrolasesPeptidesSerineThreonine

Identifiers

PMID17951390
PMCPMC2168594
OpenAlexW2054512592

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.