Evidence map›Paper›PMID 23292771›Full record

ArticleJournal of bacteriology2013

Novel twin streptolysin S-like peptides encoded in the sag operon homologue of beta-hemolytic Streptococcus anginosus.

Atsushi Tabata, Kota Nakano, Kazuto Ohkura, Toshifumi Tomoyasu, Ken Kikuchi, Robert A Whiley, Hideaki Nagamune

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.9field-weighted citation impact, top 7% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Streptococcus anginosus: the potential role in the progression of gastric cancer.Journal of cancer research and clinical oncology · 2025
    Review
  5. Article
  6. Article
  7. Streptococcal peptides and their roles in host-microbe interactions.Frontiers in cellular and infection microbiology · 2023
    Review
  8. Virulence factors ofFrontiers in microbiology · 2022
    Review
  9. Review
  10. β-HemolyticJournal of oral microbiology · 2019
    Article
  11. The Pathogenesis OfInfection and drug resistance · 2019
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

7 authors at 4 institutions in 2 countries.

Atsushi TabataDepartment of Biological Science and Technology, Life System, Institute of Technology and Science, The University of Tokushima Graduate School, Minamijosanjima-cho, Tokushima, Japan.
Kota Nakano
Kazuto Ohkura
Toshifumi Tomoyasu
Ken Kikuchi
Robert A Whiley
Hideaki Nagamune
Tokushima University · JPJuntendo University · JPQueen Mary University of London · GBSuzuka University of Medical Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Streptococcus anginosus is a member of the anginosus group streptococci, which form part of the normal human oral flora. In contrast to the pyogenic group streptococci, our knowledge of the virulence factors of the anginosus group streptococci, including S. anginosus, is not sufficient to allow a clear understanding of the basis of their pathogenicity. Generally, hemolysins are thought to be important virulence factors in streptococcal infections. In the present study, a sag operon homologue was shown to be responsible for beta-hemolysis in S. anginosus strains by random gene knockout. Interestingly, contrary to pyogenic group streptococci, beta-hemolytic S. anginosus was shown to have two tandem sagA homologues, encoding streptolysin S (SLS)-like peptides, in the sag operon homologue. Gene deletion and complementation experiments revealed that both genes were functional, and these SLS-like peptides were essential for beta-hemolysis in beta-hemolytic S. anginosus. Furthermore, the amino acid sequence of these SLS-like peptides differed from that of the typical SLS of S. pyogenes, especially in their propeptide domain, and an amino acid residue indicated to be important for the cytolytic activity of SLS in S. pyogenes was deleted in both S. anginosus homologues. These data suggest that SLS-like peptides encoded by two sagA homologues in beta-hemolytic S. anginosus may be potential virulence factors with a different structure essential for hemolytic activity and/or the maturation process compared to the typical SLS present in pyogenic group streptococci.

Indexed as

OperonAmino Acid SequenceBacterial ProteinsGene Knockout TechniquesHemolysin ProteinsMolecular Sequence DataPromoter Regions, GeneticSequence DeletionStreptococcus anginosusStreptococcus pyogenesStreptolysinsTranscription, GeneticBacterial ProteinsHemolysin Proteinsstreptolysin SStreptolysins

Identifiers

PMID23292771
PMCPMC3571330
OpenAlexW2135239833

What OpenQuestion holds

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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.