Evidence map›Paper›PMID 24816601›Full record

ArticleJournal of bacteriology2014

Identification and characterization of glycoproteins on the spore surface of Clostridium difficile.

Philippa C R Strong, Kelly M Fulton, Annie Aubry, Simon Foote, Susan M Twine, Susan M Logan

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

  1. Genomic and phenotypic insight intoEmerging microbes & infections · 2026
    Article
  2. Phylogenomic analysis of the collagen-like BclA proteins inApplied and environmental microbiology · 2026
    Article
  3. Preparation of Spores with the 70:30 Method.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  4. Immunization Strategies Against Clostridioides difficile.Advances in experimental medicine and biology · 2024
    Review
  5. Article
  6. Article
  7. Vaccines · 2020
    Article
  8. Vegetative Cell and Spore Proteomes ofJournal of proteome research · 2019
    Article
  9. Review
  10. New class of precision antimicrobials redefines role ofScience translational medicine · 2017
    Article
  11. Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017
    Review
  12. Review
  13. Article
  14. Article
  15. Effect ofmSphere
    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 1 institution in 1 country.

Philippa C R StrongVaccine Program, Human Health Therapeutics Portfolio, National Research Council of Canada, Ottawa, Ontario, Canada.
Kelly M FultonVaccine Program, Human Health Therapeutics Portfolio, National Research Council of Canada, Ottawa, Ontario, Canada.
Annie AubryVaccine Program, Human Health Therapeutics Portfolio, National Research Council of Canada, Ottawa, Ontario, Canada.
Simon FooteVaccine Program, Human Health Therapeutics Portfolio, National Research Council of Canada, Ottawa, Ontario, Canada.
Susan M TwineVaccine Program, Human Health Therapeutics Portfolio, National Research Council of Canada, Ottawa, Ontario, Canada.
Susan M LoganVaccine Program, Human Health Therapeutics Portfolio, National Research Council of Canada, Ottawa, Ontario, Canada susan.logan@nrc-cnrc.gc.ca.
National Research Council Canada · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this study, we identify a major spore surface protein, BclA, and provide evidence that this protein is glycosylated. Following extraction of the spore surface, solubilized proteins were separated by one-dimensional PAGE and stained with glycostain to reveal a reactive high-molecular-mass region of approximately 600 kDa. Tandem mass spectrometry analysis of in-gel digests showed this band to contain peptides corresponding to a putative exosporangial glycoprotein (BclA3) and identified a number of glycopeptides modified with multiple N-acetyl hexosamine moieties and, in some cases, capped with novel glycans. In addition, we demonstrate that the glycosyltransferase gene sgtA (gene CD3350 in strain 630 and CDR3194 in strain R20291), which is located immediately upstream of the bclA3 homolog, is involved in the glycosylation of the spore surface, and is cotranscribed with bclA3. The presence of anti-β-O-GlcNAc-reactive material was demonstrated on the surface of spores by immunofluorescence and in surface extracts by Western blotting, although each strain produced a distinct pattern of reactivity. Reactivity of the spore surface with the anti-β-O-GlcNAc antibody was abolished in the 630 and R20291 glycosyltransferase mutant strains, while complementation with a wild-type copy of the gene restored the β-O-GlcNAc reactivity. Phenotypic testing of R20291 glycosyltransferase mutant spores revealed no significant change in sensitivity to ethanol or lysozyme. However, a change in the resistance to heat of R20291 glycosyltransferase mutant spores compared to R20291 spores was observed, as was the ability to adhere to and be internalized by macrophages.

Indexed as

Amino Acid SequenceAnimalsBacterial AdhesionClostridioides difficileComputational BiologyGene Expression Regulation, BacterialMacrophagesMembrane GlycoproteinsMiceMolecular Sequence DataSpores, BacterialMembrane Glycoproteins

Identifiers

PMID24816601
PMCPMC4097583
OpenAlexW2133859175

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.