Evidence map›Paper›PMID 25824223›Full record

ArticleAntimicrobial agents and chemotherapy2015

PBP1a/LpoA but not PBP1b/LpoB are involved in regulation of the major β-lactamase gene blaA in Shewanella oneidensis.

Jianhua Yin, Yiyang Sun, Yinting Mao, Miao Jin, Haichun Gao

Open access · bronzeAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.6field-weighted citation impact, top 38% 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

15 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Virulence · 2022
    Review
  7. Article
  8. Article
  9. The LpoA activator is required to stimulate the peptidoglycan polymerase activity of its cognate cell wall synthase PBP1a.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. Article
  12. Conserved mechanism of cell-wall synthase regulation revealed by the identification of a new PBP activator inProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Article
  14. Article
  15. 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

5 authors at 1 institution in 1 country.

Jianhua YinInstitute of Microbiology and College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, China Key Laboratory for Agro-Microbial Research and Utilization, Zhejiang Province, Hangzhou, Zhejiang, China.
Yiyang SunInstitute of Microbiology and College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, China Key Laboratory for Agro-Microbial Research and Utilization, Zhejiang Province, Hangzhou, Zhejiang, China.
Yinting MaoInstitute of Microbiology and College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, China Key Laboratory for Agro-Microbial Research and Utilization, Zhejiang Province, Hangzhou, Zhejiang, China.
Miao JinInstitute of Microbiology and College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, China Key Laboratory for Agro-Microbial Research and Utilization, Zhejiang Province, Hangzhou, Zhejiang, China.
Haichun GaoInstitute of Microbiology and College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, China Key Laboratory for Agro-Microbial Research and Utilization, Zhejiang Province, Hangzhou, Zhejiang, China haichung@zju.edu.cn.
Zhejiang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-Lactamase production is one of the most important strategies for Gram-negative bacteria to combat β-lactam antibiotics. Studies of the regulation of β-lactamase expression have largely been focused on the class C β-lactamase AmpC, whose induction by β-lactams requires LysR-type regulator AmpR and permease AmpG-dependent peptidoglycan recycling intermediates. In Shewanella, which is ubiquitous in aquatic environments and is a reservoir for antibiotic resistance, production of the class D β-lactamase BlaA confers bacteria with natural resistance to many β-lactams. Expression of the blaA gene in the genus representative Shewanella oneidensis is distinct from the AmpC paradigm because of the lack of an AmpR homologue and the presence of an additional AmpG-independent regulatory pathway. In this study, using transposon mutagenesis, we identify proteins that are involved in blaA regulation. Inactivation of mrcA and lpoA, which encode penicillin binding protein 1a (PBP1a) and its lipoprotein cofactor, LpoA, respectively, drastically enhances blaA expression in the absence of β-lactams. Although PBP1b and its cognate, LpoB, also exist in S. oneidensis, their roles in blaA induction are dispensable. We further show that the mrcA-mediated blaA expression is independent of AmpG.

Indexed as

Bacterial Proteinsbeta-Lactamasesbeta-LactamsGene Expression Regulation, BacterialPenicillin-Binding ProteinsShewanellaAmpC beta-lactamasesBacterial Proteinsbeta-Lactamasesbeta-LactamsPenicillin-Binding Proteins

Identifiers

PMID25824223
PMCPMC4432149
OpenAlexW2139851663

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.