Evidence map›Paper›PMID 18678668›Full record

ArticleInfection and immunity2008

Binding of the Streptococcus gordonii DL1 surface protein Hsa to the host cell membrane glycoproteins CD11b, CD43, and CD50.

Yumiko Urano-Tashiro, Ayako Yajima, Eizo Takashima, Yukihiro Takahashi, Kiyoshi Konishi

Abstract read
In one paragraph

Article in Infection and immunity, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

17 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Frontiers in cellular and infection microbiology · 2022
    Article
  3. Article
  4. Article
  5. Microorganisms · 2020
    Review
  6. Article
  7. Serine-Rich Repeat Adhesins Contribute toFrontiers in microbiology · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Shear-enhanced oral microbial adhesion.Applied and environmental microbiology · 2010
    Article
  17. Crystal structure of the variable domain of the Streptococcus gordonii surface protein SspB.Protein science : a publication of the Protein Society · 2009
    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 1 institution in 1 country.

Yumiko Urano-TashiroDepartment of Microbiology, School of Life Dentistry at Tokyo, Nippon Dental University, Tokyo, Japan. yumiurano@tky.ndu.ac.jp
Ayako Yajima
Eizo Takashima
Yukihiro Takahashi
Kiyoshi Konishi
Nippon Dental University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Infective endocarditis is frequently attributed to oral streptococci. The mechanisms of pathogenesis, however, are not well understood, although interaction between streptococci and phagocytes are thought to be very important. A highly expressed surface component of Streptococcus gordonii, Hsa, which has sialic acid-binding activity, contributes to infective endocarditis in vivo. In the present study, we found that S. gordonii DL1 binds to HL-60 cells differentiated into monocytes, granulocytes, and macrophages. Using a glutathione S-transferase (GST) fusion to the NR2 domain, which is the sialic acid-binding region of Hsa, we confirmed that the Hsa NR2 domain also binds to differentiated HL-60 cells. To identify which sialoglycoproteins on the surface of differentiated HL-60 cells are receptors for Hsa, intrinsic membrane proteins were assessed by bacterial overlay and far-Western blotting. S. gordonii DL1 adhered to 100- to 150-kDa proteins, a reaction that was abolished by neuraminidase treatment. These sialoglycoproteins were identified as CD11b, CD43, and CD50 by GST pull-down assay and immunoprecipitation with each specific monoclonal antibody. These data suggest that S. gordonii DL1 Hsa specifically binds to three glycoproteins as receptors and that this interaction may be the initial bacterial binding step in infective endocarditis by oral streptococci.

Indexed as

Adhesins, BacterialAntigens, CDBlotting, Far-WesternCarrier ProteinsCD11b AntigenCell Adhesion MoleculesCell Line, TumorHemagglutinins, ViralHumansImmunoprecipitationLeukosialinMembrane ProteinsNeuraminidaseProtein BindingSialoglycoproteinsStreptococcus gordoniiAdhesins, BacterialAntigens, CDCarrier ProteinsCD11b AntigenCell Adhesion MoleculesHemagglutinins, Viralhsa protein, Streptococcus gordoniiICAM3 protein, humanITGAM protein, humanLeukosialinMembrane ProteinsNeuraminidaseSialoglycoproteinsSPN protein, human

Identifiers

PMID18678668
PMCPMC2546842
OpenAlexW2152603321

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.