Evidence map›Paper›PMID 19500353›Full record

ArticleBMC microbiology2009

The highly conserved serine threonine kinase StkP of Streptococcus pneumoniae contributes to penicillin susceptibility independently from genes encoding penicillin-binding proteins.

Ricardo Dias, David Félix, Manuela Caniça, Marie-Claude Trombe

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2009. 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
1.9field-weighted citation impact, top 15% 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, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Clinical microbiology reviews · 2025
    Review
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  7. Article
  8. Article
  9. Review
  10. Antimicrobial Resistance inMicrobiology spectrum · 2018
    Review
  11. Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Control of cell division in Streptococcus pneumoniae by the conserved Ser/Thr protein kinase StkP.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  17. Article
  18. Review
  19. Eukaryote-like serine/threonine kinases and phosphatases in bacteria.Microbiology and molecular biology reviews : MMBR · 2011
    Review
  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

4 authors at 2 institutions in 2 countries.

Ricardo DiasDepartment of Infectious Diseases, National Institute of Health Dr. Ricardo Jorge, Lisbon, Portugal. ricardo.dias@insa.min-saude.pt
David Félix
Manuela Caniça
Marie-Claude Trombe
National Institute of Health Dr. Ricardo Jorge · PTInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe serine/threonine kinase StkP of Streptococcus pneumoniae is a major virulence factor in the mouse model of infection. StkP is a modular protein with a N-terminal kinase domain a C-terminal PASTA domain carrying the signature of penicillin-binding protein (PBP) and prokaryotic serine threonine kinase. In laboratory cultures, one target of StkP is the phosphoglucosamine mutase GlmM involved in the first steps of peptidoglycan biosynthesis. In order to further elucidate the importance of StkP in S. pneumoniae, its role in resistance to beta-lactams has been assessed by mutational analysis in laboratory cultures and its genetic conservation has been investigated in isolates from infected sites (virulent), asymptomatic carriers, susceptible and non-susceptible to beta-lactams.

resultsDeletion replacement mutation in stkP conferred hypersensitivity to penicillin G and was epistatic on mutations in PBP2X, PBP2B and PBP1A from the resistant 9V clinical isolate URA1258. Genetic analysis of 55 clinical isolates identified 11 StkP alleles differing from the reference R6 allele. None relevant mutation in the kinase or the PASTA domains were found to account for susceptibility of the isolates. Rather the minimal inhibitory concentration (MIC) values of the strains appeared to be determined by their PBP alleles.

conclusionThe results of genetic dissection analysis in lab strain Cp1015 reveal that StkP is involved in the bacterial response to penicillin and is epistatic on mutations PBP 2B, 2X and 1A. However analysis of the clinical isolates did not allow us to find the StkP alleles putatively involved in determining the virulence or the resistance level of a given strain, suggesting a strong conservation of StkP in clinical isolates.

Indexed as

Bacterial ProteinsGenotypeMicrobial Sensitivity TestsModels, MolecularMutagenesisPenicillin ResistancePenicillinsPolymorphism, GeneticProtein Serine-Threonine KinasesProtein Structure, SecondarySequence DeletionStreptococcus pneumoniaeBacterial ProteinsPenicillinsProtein Serine-Threonine Kinases

Identifiers

PMID19500353
PMCPMC2700816
OpenAlexW1999441425

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Registered trials

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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.