Evidence map›Paper›PMID 24391811›Full record

ArticlePloS one2013

Identification and characterization of sulfated carbohydrate-binding protein from Lactobacillus reuteri.

Keita Nishiyama, Ayaka Ochiai, Daigo Tsubokawa, Kazuhiko Ishihara, Yuji Yamamoto, Takao Mukai

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The Mucus Binding Factor Is Not Necessary forInternational journal of molecular sciences · 2022
    Article
  5. Article
  6. The probiotic and immunomodulation effects ofFrontiers in cellular and infection microbiology · 2022
    Article
  7. Adhesion and Colonization of theFrontiers in microbiology · 2022
    Article
  8. Review
  9. Potential ProbioticFrontiers in microbiology · 2021
    Article
  10. Glyceraldehyde-3-Phosphate Dehydrogenase Increases the Adhesion ofInternational journal of molecular sciences · 2020
    Article
  11. Review
  12. Article
  13. Article
  14. 3-Sulfogalactosyl-dependent adhesion ofThe Journal of biological chemistry · 2017
    Article
  15. mBio · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Keita NishiyamaDepartment of Animal Science, Kitasato University School of Veterinary Medicine, Towada, Aomori, Japan.
Ayaka OchiaiDepartment of Animal Science, Kitasato University School of Veterinary Medicine, Towada, Aomori, Japan.
Daigo TsubokawaDepartment of Parasitology, Kitasato University School of Medicine, Sagamihara, Kanagawa, Japan.
Kazuhiko IshiharaGraduate School of Medical Sciences, Kitasato University, Sagamihara, Kanagawa, Japan.
Yuji YamamotoDepartment of Animal Science, Kitasato University School of Veterinary Medicine, Towada, Aomori, Japan.
Takao MukaiDepartment of Animal Science, Kitasato University School of Veterinary Medicine, Towada, Aomori, Japan.
Kitasato University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We previously purified a putative sulfated-galactosylceramide (sulfatide)-binding protein with a molecular weight of 47 kDa from the cell surface of Lactobacillus reuteri JCM1081. The aim of this study was to identify the 47-kDa protein, examine its binding to sulfated glycolipids and mucins, and evaluate its role in bacterial adhesion to mucosal surfaces. By cloning and sequencing analysis, the 47-kDa protein was identified as elongation factor-Tu (EF-Tu). Adhesion properties were examined using 6 × Histidine-fused EF-Tu (His6-EF-Tu). Surface plasmon resonance analysis demonstrated pH-dependent binding of His6-EF-Tu to sulfated glycolipids, but not to neutral or sialylated glycolipids, suggesting that a sulfated galactose residue was responsible for EF-Tu binding. Furthermore, His6-EF-Tu was found to bind to porcine gastric mucin (PGM) by enzyme-linked immunosorbent assay. Binding was markedly reduced by sulfatase treatment of PGM and in the presence of acidic and desialylated oligosaccharide fractions containing sulfated carbohydrate residues prepared from PGM, demonstrating that sulfated carbohydrate moieties mediated binding. Histochemical staining revealed similar localization of His6-EF-Tu and high iron diamine staining in porcine mucosa. These results indicated that EF-Tu bound PGM via sulfated carbohydrate moieties. To characterize the contribution of EF-Tu to the interaction between bacterial cells and PGM, we tested whether anti-EF-Tu antibodies could inhibit the interaction. Binding of L. reuteri JCM1081 to PGM was significantly blocked in a concentration-dependent matter, demonstrating the involvement of EF-Tu in bacterial adhesion. In conclusion, the present results demonstrated, for the first time, that EF-Tu bound sulfated carbohydrate moieties of sulfated glycolipids and sulfomucin, thereby promoting adhesion of L. reuteri to mucosal surfaces.

Indexed as

AnimalsBacterial AdhesionElectrophoresis, Polyacrylamide GelEnzyme-Linked Immunosorbent AssayGastric MucosaGlycolipidsLimosilactobacillus reuteriMucinsPeptide Elongation Factor TuProtein BindingReceptors, Cell SurfaceSwineGlycolipidsMucinsPeptide Elongation Factor TuReceptors, Cell Surfacesaccharide-binding proteinssulfoglycolipidssulfomucin

Identifiers

PMID24391811
PMCPMC3877078
OpenAlexW2065798896

What OpenQuestion holds

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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.