Evidence map›Paper›PMID 24343649›Full record

ArticleInfection and immunity2014

BsaB, a novel adherence factor of group B Streptococcus.

Shengmei Jiang, Michael R Wessels

Open access · hybridAbstract read
In one paragraph

Article in Infection and immunity, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

26 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Review
  3. Re-framing the importance of Group BInfection and immunity · 2024
    Review
  4. Article
  5. Review
  6. Group BFrontiers in cellular and infection microbiology · 2024
    Article
  7. Infection and immunity · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Mast cell chymase decreases the severity of group B Streptococcus infections.The Journal of allergy and clinical immunology · 2018
    Article
  18. Frontiers in immunology · 2018
    Review
  19. Review
  20. Review
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

2 authors at 2 institutions in 1 country.

Shengmei JiangDivision of Infectious Diseases, Boston Children's Hospital, and Harvard Medical School, Boston, Massachusetts, USA.
Michael R Wessels
Boston Children's Hospital · USHarvard University · US

Funding

IMMUNE RESPONSE TO THE GROUP A STREPTOCOCCAL CAPSULER01AI029952 · NIAID · CHILDREN'S HOSPITAL BOSTON · PI WESSELS, MICHAEL R · 1991 to 2019
$5.6M
Virulence regulation in group B StreptococcusR01AI059502 · NIAID · CHILDREN'S HOSPITAL BOSTON · PI WESSELS, MICHAEL R · 2004 to 2008
$1.9M
NIAID NIH HHS AI29952NIAID NIH HHS AI59502NIAID NIH HHS R01 AI029952NIAID NIH HHS R01 AI059502
6 · The paper itself

Abstract

Streptococcus agalactiae (group B Streptococcus [GBS]) is a leading cause of neonatal sepsis and meningitis, peripartum infections in women, and invasive infections in chronically ill or elderly individuals. GBS can be isolated from the gastrointestinal or genital tracts of up to 30% of healthy adults, and infection is thought to arise from invasion from a colonized mucosal site. Accordingly, bacterial surface components that mediate attachment of GBS to host cells or the extracellular matrix represent key factors in the colonization and infection of the human host. We identified a conserved GBS gene of unknown function that was predicted to encode a cell wall-anchored surface protein. Deletion of the gene and a cotranscribed upstream open reading frame (ORF) in GBS strain 515 reduced bacterial adherence to VK2 vaginal epithelial cells in vitro and reduced GBS binding to fibronectin-coated microtiter wells. Expression of the gene product in Lactococcus lactis conferred the ability to adhere to VK2 cells, to fibronectin and laminin, and to fibronectin-coated ME-180 cervical epithelial cells. Expression of the recombinant protein in L. lactis also markedly increased biofilm formation. The adherence function of the protein, named bacterial surface adhesin of GBS (BsaB), depended both on a central BID1 domain found in bacterial intimin-like proteins and on the C-terminal portion of the BsaB protein. Expression of BsaB in GBS, like that of several other adhesins, was regulated by the CsrRS two-component system. We conclude that BsaB represents a newly identified adhesin that participates in GBS attachment to epithelial cells and the extracellular matrix.

Indexed as

Adhesins, BacterialBacterial ProteinsBiofilmsCell LineEpithelial CellsExtracellular MatrixFibronectinsHumansLactococcus lactisMembrane ProteinsOpen Reading FramesStreptococcus agalactiaeAdhesins, BacterialBacterial ProteinsFibronectinsMembrane Proteins

Identifiers

PMID24343649
PMCPMC3957996
OpenAlexW2053475579

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.