Evidence map›Paper›PMID 23241367›Full record

ArticleMolecular oral microbiology2013

Phenotypic characterization of the foldase homologue PrsA in Streptococcus mutans.

L Guo, T Wu, W Hu, X He, S Sharma, P Webster, J K Gimzewski, X Zhou, R Lux, W Shi

Abstract read
In one paragraph

Article in Molecular oral microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.6field-weighted citation impact, top 12% 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

20 citing papers in PubMed, 32 citations in OpenAlex.

  1. The roles of theJournal of bacteriology · 2026
    Article
  2. Membrane Vesicles ofMicroorganisms · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. GFP fusions of Sec-routed extracellular proteins inMicrobial cell (Graz, Austria) · 2023
    Article
  9. Virulence · 2022
    Article
  10. Cnm ofFrontiers in cellular and infection microbiology · 2022
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Dimeric Structure of the Bacterial Extracellular Foldase PrsA.The Journal of biological chemistry · 2015
    Article
  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

10 authors at 4 institutions in 2 countries.

L GuoSchool of Dentistry, University of California, Los Angeles, CA, USA.
T Wu
W Hu
X He
S Sharma
P Webster
J K Gimzewski
X Zhou
R Lux
W Shi
University of California, Los Angeles · USSichuan University · CNCalifornia NanoSystems Institute · USHouse Clinic · US

Funding

Making a quantum leap in plaque research with modern sciencesR01DE020102 · NIDCR · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HE, XUESONG, MCLEAN, JEFFREY SCOTT · 2010 to 2020
$3.7M
NIDCR NIH HHS 1-R01-DE020102NIDCR NIH HHS R01 DE020102
6 · The paper itself

Abstract

Streptococcus mutans is generally considered to be the principal etiological agent for dental caries. Many of the proteins necessary for its colonization of the oral cavity and pathogenesis are exported to the cell surface or the extracellular matrix, a process that requires the assistance of the export machineries. Bioinformatic analysis revealed that the S. mutans genome contains a prsA gene, whose counterparts in other gram-positive bacteria, including Bacillus and Lactococcus, encode functions involved in protein post-export. In this study, we constructed a PrsA-deficient derivative of S. mutans and demonstrated that the prsA mutant displayed an altered cell wall/membrane protein profile as well as cell-surface-related phenotypes, including auto-aggregation, increased surface hydrophobicity and abnormal biofilm formation. Further analysis revealed that the disruption of the prsA gene resulted in reduced insoluble glucan production by cell surface localized glucosyltransferases, and mutacin as well as cell surface-display of a heterologous expressed GFP fusion to the cell surface protein SpaP. Our study suggested that PrsA in S. mutans encodes functions similar to those identified in Bacillus, and so is likely to be involved in protein post-export.

Indexed as

Bacterial AdhesionBacterial ProteinsBacteriocinsBiofilmsCell MembraneCell WallEscherichia coliGene DeletionGlucansGlucosyltransferasesHumansHydrophobic and Hydrophilic InteractionsLipoproteinsMembrane ProteinsMicrobial ViabilityMutationBacterial ProteinsBacteriocinsGlucansGlucosyltransferasesLipoproteinsMembrane Proteinsmutacin IVPolysaccharides, BacterialprsA protein, bacteria

Identifiers

PMID23241367
PMCPMC3819222
OpenAlexW2040671472

What OpenQuestion holds

Textmetadata
LicenceTDM
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.