Evidence map›Paper›PMID 26694450›Full record

ArticleViruses2015

A Flagellar Glycan-Specific Protein Encoded by Campylobacter Phages Inhibits Host Cell Growth.

Muhammad Afzal Javed, Jessica C Sacher, Lieke B van Alphen, Robert T Patry, Christine M Szymanski

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 20% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Natural Competence and Horizontal Gene Transfer in Campylobacter.Current topics in microbiology and immunology · 2021
    Article
  8. Binding of Phage-Encoded FlaGrab to MotileFrontiers in microbiology · 2020
    Article
  9. Bacterial ABNature communications · 2019
    Article
  10. Article
  11. 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 2 countries.

Muhammad Afzal JavedAlberta Glycomics Centre and Department of Biological Sciences, CW-405 Biological Sciences Building, University of Alberta, Edmonton, AB, T6G 2E9, Canada. majavedlh@yahoo.com.
Jessica C SacherAlberta Glycomics Centre and Department of Biological Sciences, CW-405 Biological Sciences Building, University of Alberta, Edmonton, AB, T6G 2E9, Canada. sacher@ualberta.ca.
Lieke B van AlphenAlberta Glycomics Centre and Department of Biological Sciences, CW-405 Biological Sciences Building, University of Alberta, Edmonton, AB, T6G 2E9, Canada. lieke.van.alphen@mumc.nl.
Robert T PatryAlberta Glycomics Centre and Department of Biological Sciences, CW-405 Biological Sciences Building, University of Alberta, Edmonton, AB, T6G 2E9, Canada. rpatry@ualberta.ca.
Christine M SzymanskiAlberta Glycomics Centre and Department of Biological Sciences, CW-405 Biological Sciences Building, University of Alberta, Edmonton, AB, T6G 2E9, Canada. cszymans@ualberta.ca.
University of Alberta · CAAgriculture and Agri-Food Canada · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We previously characterized a carbohydrate binding protein, Gp047, derived from lytic Campylobacter phage NCTC 12673, as a promising diagnostic tool for the identification of Campylobacter jejuni and Campylobacter coli. We also demonstrated that this protein binds specifically to acetamidino-modified pseudaminic acid residues on host flagella, but the role of this protein in the phage lifecycle remains unknown. Here, we report that Gp047 is capable of inhibiting C. jejuni growth both on solid and liquid media, an activity, which we found to be bacteriostatic. The Gp047 domain responsible for bacterial growth inhibition is localized to the C-terminal quarter of the protein, and this activity is both contact- and dose-dependent. Gp047 gene homologues are present in all Campylobacter phages sequenced to date, and the resulting protein is not part of the phage particle. Therefore, these results suggest that either phages of this pathogen have evolved an effector protein capable of host-specific growth inhibition, or that Campylobacter cells have developed a mechanism of regulating their growth upon sensing an impending phage threat.

Indexed as

Anti-Bacterial AgentsCampylobacter jejuniFlagellaGrowth InhibitorsLectinsPolysaccharidesProtein BindingViral ProteinsAnti-Bacterial AgentsGrowth InhibitorsLectinsPolysaccharidesViral ProteinsbacteriophagebacteriostaticCampylobacterflagellar glycosylationglycan binding proteingrowth inhibitionreceptor binding protein

Identifiers

PMID26694450
PMCPMC4690887
OpenAlexW2212607938

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.