Evidence map›Paper›PMID 16177372›Full record

ArticleInfection and immunity2005

Role of HtrA in surface protein expression and biofilm formation by Streptococcus mutans.

Saswati Biswas, Indranil Biswas

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

50 citing papers in PubMed, 98 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Investigating the role of aFrontiers in oral health · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Extracellular Pneumococcal Serine Proteases Affect Nasopharyngeal Colonization.Frontiers in cellular and infection microbiology · 2020
    Article
  17. Review
  18. Frontiers in cellular and infection microbiology · 2020
    Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Saswati BiswasDivision of Basic Biomedical Sciences, University of South Dakota School of Medicine, Vermillion, 57069-2390, USA. ibiswas@usd.edu
Indranil Biswas
University of South Dakota · US

Funding

WESTCORE DNA SEQUENCING AND GENOTYPING CORE FACILITYP20RR016479 · NCRR · UNIVERSITY OF SOUTH DAKOTA · PI EICHLER, BARRETT · 2001 to 2011
$32.2M
NCRR NIH HHS 2 P20 RR016479NCRR NIH HHS P20 RR016479
6 · The paper itself

Abstract

The HtrA surface protease in gram-positive bacteria is involved in the processing and maturation of extracellular proteins and degradation of abnormal or misfolded proteins. Inactivation of htrA has been shown to affect the tolerance to thermal and environmental stress and to reduce virulence. We found that inactivation of Streptococcus mutans htrA by gene-replacement also resulted in a reduced ability to withstand exposure to low and high temperatures, low pH, and oxidative and DNA damaging agents. The htrA mutation affected surface expression of several extracellular proteins including glucan-binding protein B (GbpB), glucosyltransferases, and fructosyltransferase. In addition, htrA mutation also altered the surface expression of enolase and glyceraldehyde-3-phosphate dehydrogenease, two glycolytic enzymes that are known to be present on the streptococcal cell surface. As expected, microscopic analysis of in vitro grown biofilm structure revealed that the htrA deficient biofilms adopted a much more granular patchy appearance, rather than the relatively smooth confluent layer normally seen in the wild type. These results suggest that HtrA plays an important role in the biogenesis of extracellular proteins including surface associated glycolytic enzymes and in biofilm formation of S. mutans.

Indexed as

BiofilmsDNA DamageHeat-Shock ProteinsHydrogen-Ion ConcentrationMembrane ProteinsMutationPeriplasmic ProteinsSerine EndopeptidasesStreptococcus mutansTemperatureDegP proteaseHeat-Shock ProteinsMembrane ProteinsPeriplasmic ProteinsSerine Endopeptidases

Identifiers

PMID16177372
PMCPMC1230926
OpenAlexW2165161053

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.