Evidence map›Paper›PMID 21984942›Full record

ArticlePloS one2011

Protein glycosylation in Helicobacter pylori: beyond the flagellins?

Patrick S Hopf, Rachel S Ford, Najwa Zebian, Alexandra Merkx-Jacques, Somalinga Vijayakumar, Dinath Ratnayake, Jacqueline Hayworth, Carole Creuzenet

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
6.2field-weighted citation impact, top 4% 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

28 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. AssessingACS infectious diseases · 2026
    Article
  3. Biochemical characterization of theFrontiers in microbiology · 2025
    Article
  4. Article
  5. Differential Proteomics ofMedicina (Kaunas, Lithuania) · 2022
    Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017
    Review
  12. Protein signature characterizingInfectious agents and cancer · 2017
    Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014
    Review
  18. Review
  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 1 institution in 1 country.

Patrick S HopfInfectious Diseases Research Group, Department of Microbiology and Immunology, The University of Western Ontario, London, Ontario, Canada.
Rachel S Ford
Najwa Zebian
Alexandra Merkx-Jacques
Somalinga Vijayakumar
Dinath Ratnayake
Jacqueline Hayworth
Carole Creuzenet
Western University · CA

Funding

Canadian Institutes of Health Research MOP-62775
6 · The paper itself

Abstract

Glycosylation of flagellins by pseudaminic acid is required for virulence in Helicobacter pylori. We demonstrate that, in H. pylori, glycosylation extends to proteins other than flagellins and to sugars other than pseudaminic acid. Several candidate glycoproteins distinct from the flagellins were detected via ProQ-emerald staining and DIG- or biotin- hydrazide labeling of the soluble and outer membrane fractions of wild-type H. pylori, suggesting that protein glycosylation is not limited to the flagellins. DIG-hydrazide labeling of proteins from pseudaminic acid biosynthesis pathway mutants showed that the glycosylation of some glycoproteins is not dependent on the pseudaminic acid glycosylation pathway, indicating the existence of a novel glycosylation pathway. Fractions enriched in glycoprotein candidates by ion exchange chromatography were used to extract the sugars by acid hydrolysis. High performance anion exchange chromatography with pulsed amperometric detection revealed characteristic monosaccharide peaks in these extracts. The monosaccharides were then identified by LC-ESI-MS/MS. The spectra are consistent with sugars such as 5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-L-manno-nonulosonic acid (Pse5Ac7Ac) previously described on flagellins, 5-acetamidino-7-acetamido-3,5,7,9-tetradeoxy-L-glycero-L-manno-nonulosonic acid (Pse5Am7Ac), bacillosamine derivatives and a potential legionaminic acid derivative (Leg5AmNMe7Ac) which were not previously identified in H. pylori. These data open the way to the study of the mechanism and role of protein glycosylation on protein function and virulence in H. pylori.

Indexed as

Bacterial ProteinsChromatography, Ion ExchangeGlycosylationHelicobacter pyloriSialic AcidsSpectrometry, Mass, Electrospray IonizationVirulence5,7-diacetamido-3,5,7,9-tetradeoxynon-2-ulosonic acidBacterial ProteinsSialic Acids

Identifiers

PMID21984942
PMCPMC3184161
OpenAlexW2086225810

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.