Evidence map›Paper›PMID 21804002›Full record

ArticleJournal of bacteriology2011

O-linked glycosylation of the PilA pilin protein of Francisella tularensis: identification of the endogenous protein-targeting oligosaccharyltransferase and characterization of the native oligosaccharide.

Wolfgang Egge-Jacobsen, Emelie Näslund Salomonsson, Finn Erik Aas, Anna-Lena Forslund, Hanne C Winther-Larsen, Josef Maier, Anna Macellaro, Kerstin Kuoppa, Petra C F Oyston, Richard W Titball and 4 more

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Review
  3. Sweet complexity:Frontiers in cellular and infection microbiology · 2024
    Review
  4. CRISPRi-Mediated Silencing ofJournal of proteome research · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. A General ProteinFrontiers in microbiology · 2018
    Article
  11. Role of Glycosylation/Deglycolysation Processes inFrontiers in cellular and infection microbiology · 2017
    Review
  12. Glycosylation of a Capsule-Like Complex (CLC) byFrontiers in microbiology · 2017
    Article
  13. Article
  14. From the Outside-In: The Francisella tularensis Envelope and Virulence.Frontiers in cellular and infection microbiology · 2015
    Review
  15. Article
  16. The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014
    Review
  17. Uncovering the components of the Francisella tularensis virulence stealth strategy.Frontiers in cellular and infection microbiology · 2014
    Review
  18. Article
  19. Review
  20. Type IV pilin proteins: versatile molecular modules.Microbiology and molecular biology reviews : MMBR · 2012
    Review
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

14 authors at 5 institutions in 3 countries.

Wolfgang Egge-JacobsenDepartment of Molecular Biosciences, University of Oslo, 0316 Oslo, Norway. w.m.egge-jacobsen@imbv.uio.no
Emelie Näslund Salomonsson
Finn Erik Aas
Anna-Lena Forslund
Hanne C Winther-Larsen
Josef Maier
Anna Macellaro
Kerstin Kuoppa
Petra C F Oyston
Richard W Titball
Rebecca M Thomas
Åke Forsberg
Joann L Prior
Michael Koomey
Swedish Defence Research Agency · SEUniversity of Oslo · NODefence Science and Technology Laboratory · GBUmeå University · SEUniversity of Exeter · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Findings from a number of studies suggest that the PilA pilin proteins may play an important role in the pathogenesis of disease caused by species within the genus Francisella. As such, a thorough understanding of PilA structure and chemistry is warranted. Here, we definitively identified the PglA protein-targeting oligosaccharyltransferase by virtue of its necessity for PilA glycosylation in Francisella tularensis and its sufficiency for PilA glycosylation in Escherichia coli. In addition, we used mass spectrometry to examine PilA affinity purified from Francisella tularensis subsp. tularensis and F. tularensis subsp. holarctica and demonstrated that the protein undergoes multisite, O-linked glycosylation with a pentasaccharide of the structure HexNac-Hex-Hex-HexNac-HexNac. Further analyses revealed microheterogeneity related to forms of the pentasaccharide carrying unusual moieties linked to the distal sugar via a phosphate bridge. Type A and type B strains of Francisella subspecies thus express an O-linked protein glycosylation system utilizing core biosynthetic and assembly pathways conserved in other members of the proteobacteria. As PglA appears to be highly conserved in Francisella species, O-linked protein glycosylation may be a feature common to members of this genus.

Indexed as

Bacterial ProteinsFimbriae ProteinsFrancisella tularensisGlycopeptidesGlycosylationHexosyltransferasesImmunoblottingMass SpectrometryMembrane ProteinsOligosaccharidesPolysaccharidesBacterial Proteinsdolichyl-diphosphooligosaccharide - protein glycotransferaseFimbriae ProteinsGlycopeptidesHexosyltransferasesMembrane ProteinsOligosaccharidesPolysaccharides

Identifiers

PMID21804002
PMCPMC3187425
OpenAlexW2160208907

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.