Evidence map›Paper›PMID 19395494›Full record

ArticleJournal of bacteriology2009

Molecular dissection of the secA2 locus of group B Streptococcus reveals that glycosylation of the Srr1 LPXTG protein is required for full virulence.

Michel-Yves Mistou, Shaynoor Dramsi, Sara Brega, Claire Poyart, Patrick Trieu-Cuot

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
9.8field-weighted citation impact, top 2% 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

63 citing papers in PubMed, 94 citations in OpenAlex.

  1. Review
  2. A CRISPRi library screen in group BInfection and immunity · 2025
    Article
  3. A CRISPRi Library Screen in Group BbioRxiv : the preprint server for biology · 2024
    Article
  4. Fraxetin Targeting to Sortase A Decreases the Pathogenicity ofAnimals : an open access journal from MDPI · 2024
    Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Tandem sialoglycan-binding modules in aThe Journal of biological chemistry · 2020
    Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Streptococcus oralis subsp.Infection and immunity · 2019
    Article
  20. Review

3 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

5 authors at 3 institutions in 2 countries.

Michel-Yves MistouInstitut Pasteur, Unité de Biologie des Bactéries Pathogènes à Gram-Positif, URA CNRS 2172, Paris Cedex 15, France. mistou@pasteur.fr
Shaynoor Dramsi
Sara Brega
Claire Poyart
Patrick Trieu-Cuot
Centre National de la Recherche Scientifique · FRInstitut Pasteur · FRDélégation Paris 5 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In streptococci, the secA2 locus includes genes encoding the following: (i) the accessory Sec components (SecA2, SecY2, and at least three accessory secretion proteins), (ii) two essential glycosyltranferases (GTs) (GtfA and GtfB), (iii) a variable number of dispensable additional GTs, and (iv) a secreted serine-rich LPXTG protein which is glycosylated in the cytoplasm and transported to the cell surface by this accessory Sec system. The secA2 locus of Streptococcus agalactiae strain NEM316 is structurally related to those found in other streptococci and encodes the serine-rich surface protein Srr1. We demonstrated that expression of Srr1 but not that of the SecA2 components and the associated GTs is regulated by the standalone transcriptional regulator Rga. Srr1 is synthesized as a glycosylated precursor, secreted by the SecA2 system, and anchored to the cell wall by the housekeeping sortase A. Srr1 was localized preferentially at the old poles. GtfA and/or GtfB, but not the six additional GTs, is essential for the production of Srr1. These GTs are involved in the attachment of GlcNac and sialic acid to Srr1. Full glycosylation of Srr1 is associated with the cell surface display of a protein that is more resistant to proteolytic attack. Srr1 contributes to bacterial adherence to human epithelial cell lines and virulence in a neonatal rat model. The extent of Srr1 glycosylation by GtfC to -H modulates bacterial adherence and virulence.

Indexed as

AminoacyltransferasesAnimalsAnimals, NewbornBacterial AdhesionBacterial ProteinsCell WallCysteine EndopeptidasesGlycosylationPolymerase Chain ReactionRatsRats, Sprague-DawleyStreptococcal InfectionsStreptococcus agalactiaeTranscription, GeneticTrypsinVirulenceAminoacyltransferasesBacterial ProteinsCysteine Endopeptidasessortase ATrypsin

Identifiers

PMID19395494
PMCPMC2698466
OpenAlexW2040651284

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.