Evidence map›Paper›PMID 15155657›Full record

ArticleInfection and immunity2004

The novel fibrinogen-binding protein FbsB promotes Streptococcus agalactiae invasion into epithelial cells.

Heike Gutekunst, Bernhard J Eikmanns, Dieter J Reinscheid

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
6.0field-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

62 citing papers in PubMed, 102 citations in OpenAlex.

  1. Review
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  8. Re-framing the importance of Group BInfection and immunity · 2024
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  10. Article
  11. Frontiers in cellular and infection microbiology · 2024
    Article
  12. Article
  13. Characterization and virulence ofFrontiers in microbiology · 2023
    Article
  14. Article
  15. Review
  16. Virulence Factor Genes and Cytotoxicity ofMicrobiology spectrum · 2022
    Article
  17. Article
  18. Group B Streptococcal Neonatal Meningitis.Clinical microbiology reviews · 2022
    Review
  19. Molecular epidemiology, drug resistance, and virulence gene analysis ofFrontiers in cellular and infection microbiology · 2022
    Article
  20. Review

2 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Heike GutekunstDepartment of Microbiology and Biotechnology, University of Ulm, D-89069 Ulm, Germany.
Bernhard J Eikmanns
Dieter J Reinscheid
Universität Ulm · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Streptococcus agalactiae is a major cause of bacterial sepsis and meningitis in human newborns. The interaction of S. agalactiae with host proteins and the entry into host cells thereby represent important virulence traits of these bacteria. The present report describes the identification of the fbsB gene, encoding a novel fibrinogen-binding protein that plays a crucial role in the invasion of S. agalactiae into human cells. In Western blots and enzyme-linked immunosorbent assay (ELISA) experiments, the FbsB protein was demonstrated to interact with soluble and immobilized fibrinogen. Binding studies showed the N-terminal 388 residues of FbsB and the Aalpha-subunit of human fibrinogen to recognize each other. By reverse transcription (RT)-PCR, the fbsB gene was shown to be cotranscribed with the gbs0851 gene in S. agalactiae. Deletion of the fbsB gene in the genome of S. agalactiae did not influence the binding of the bacteria to fibrinogen, suggesting that FbsB does not participate in the attachment of S. agalactiae to fibrinogen. In tissue culture experiments, however, the fbsB deletion mutant was severely impaired in its invasion into lung epithelial cells. Bacterial invasion could be reestablished by introducing the fbsB gene on a shuttle plasmid into the fbsB deletion mutant. Furthermore, treatment of lung epithelial cells with FbsB fusion protein blocked S. agalactiae invasion of epithelial cells in a dose-dependent fashion. These results suggest an important role of the FbsB protein in the overall process of host cell entry by S. agalactiae.

Indexed as

Bacterial AdhesionBacterial ProteinsBinding SitesCarrier ProteinsCell LineEpithelial CellsFibrinogenGene DeletionHumansInfant, NewbornLungMolecular Sequence DataStreptococcus agalactiaeVirulenceBacterial ProteinsCarrier ProteinsFbsB protein, Streptococcus agalactiaeFibrinogen

Identifiers

PMID15155657
PMCPMC415667
OpenAlexW2149396146

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.