Evidence map›Paper›PMID 20643653›Full record

ArticleThe Journal of biological chemistry2010

Streptococcus pyogenes Ser/Thr kinase-regulated cell wall hydrolase is a cell division plane-recognizing and chain-forming virulence factor.

Vijay Pancholi, Gregory Boël, Hong Jin

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.3field-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

24 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Bacterial extracellular vesicles target different bacterial species, impairing cell division and diminishing their pathogenicity.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  7. Induction ofMicrobiology (Reading, England) · 2020
    Article
  8. Article
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  12. SpyB, a Small Heme-Binding Protein, Affects the Composition of the Cell Wall inFrontiers in cellular and infection microbiology · 2016
    Article
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  15. Review
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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

3 authors at 1 institution in 1 country.

Vijay PancholiDepartment of Pathology, Ohio State University College of Medicine, Columbus, Ohio 43210-1214, USA. vijay.pancholi@osumc.edu
Gregory Boël
Hong Jin
The Ohio State University · US

Funding

Role of eukaryotic-type STK and PPPL in GAS pathogenesisR21AI064912 · NIAID · PUBLIC HEALTH RESEARCH INSTITUTE · PI PANCHOLI, VIJAY · 2005 to 2006
$421k
NIAID NIH HHS AI64912NIAID NIH HHS R21 AI064912
6 · The paper itself

Abstract

Cell division and cell wall synthesis are closely linked complex phenomena and play a crucial role in the maintenance and regulation of bacterial virulence. Eukaryotic-type Ser/Thr kinases reported in prokaryotes, including that in group A Streptococcus (GAS) (Streptococcus pyogenes Ser/Thr kinase (SP-STK)), regulate cell division, growth, and virulence. The mechanism of this regulation is, however, unknown. In this study, we demonstrated that SP-STK-controlled cell division is mediated under the positive regulation of secretory protein that possesses a cysteine and histidine-dependent aminohydrolases/peptidases (CHAP) domain with functionally active cell wall hydrolase activity (henceforth named as CdhA (CHAP-domain-containing and chain-forming cell wall hydrolase). Deletion of the CdhA-encoding gene resulted in severe cell division and growth defects in GAS mutants. The mutant expressing the truncated CdhA (devoid of the CHAP domain), although displayed no such defects, it became attenuated for virulence in mice and highly susceptible to cell wall-acting antibiotics, as observed for the mutant lacking CdhA. When CdhA was overexpressed in the wild-type GAS as well as in heterologous strains, Escherichia coli and Staphylococcus aureus, we observed a distinct increase in bacterial chain length. Our data reveal that CdhA is a multifunctional protein with a major function of the N-terminal region as a cell division plane-recognizing domain and that of the C-terminal CHAP domain as a virulence-regulating domain. CdhA is thus an important therapeutic target.

Indexed as

AnimalsBacterial ProteinsCell WallEscherichia coliGene DeletionHumansHydrolasesMiceMice, Inbred BALB CProtein Serine-Threonine KinasesStaphylococcus aureusStreptococcal InfectionsStreptococcus pyogenesVirulence FactorsBacterial ProteinsHydrolasesProtein Serine-Threonine KinasesVirulence Factors

Identifiers

PMID20643653
PMCPMC2945579
OpenAlexW2024083213

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.