Evidence map›Paper›PMID 25136029›Full record

ArticleAntimicrobial agents and chemotherapy2014

Distinct roles of major peptidoglycan recycling enzymes in β-Lactamase production in Shewanella oneidensis.

Jianhua Yin, Yinting Mao, Lili Ju, Miao Jin, Yiyang Sun, Shouguang Jin, Haichun Gao

Open access · greenAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.5field-weighted citation impact, top 45% 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

12 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. NagX, a periplasmic β-Antimicrobial agents and chemotherapy · 2026
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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

7 authors at 2 institutions in 2 countries.

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.
Yinting MaoInstitute of Microbiology and College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, China.
Lili JuInstitute of Microbiology and College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, China.
Miao JinInstitute of Microbiology and College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, China.
Yiyang SunInstitute of Microbiology and College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, China.
Shouguang JinDepartment of Molecular Genetics and Microbiology, University of Florida, Gainesville, Florida, USA.
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 · CNUniversity of Florida · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-Lactam antibiotics were the earliest discovered and are the most widely used group of antibiotics that work by inactivating penicillin-binding proteins to inhibit peptidoglycan biosynthesis. As one of the most efficient defense strategies, many bacteria produce β-lactam-degrading enzymes, β-lactamases, whose biochemical functions and regulation have been extensively studied. A signal transduction pathway for β-lactamase induction by β-lactam antibiotics, consisting of the major peptidoglycan recycling enzymes and the LysR-type transcriptional regulator, AmpR, has been recently unveiled in some bacteria. Because inactivation of some of these proteins, especially the permease AmpG and the β-hexosaminidase NagZ, results in substantially elevated susceptibility to the antibiotics, these have been recognized as potential therapeutic targets. Here, we show a contrasting scenario in Shewanella oneidensis, in which the homologue of AmpR is absent. Loss of AmpG or NagZ enhances β-lactam resistance drastically, whereas other identified major peptidoglycan recycling enzymes are dispensable. Moreover, our data indicate that there exists a parallel signal transduction pathway for β-lactamase induction, which is independent of either AmpG or NagZ.

Indexed as

Bacterial Proteinsbeta-Lactamasesbeta-Lactam Resistancebeta-Lactamsbeta-N-AcetylhexosaminidasesDNA-Binding ProteinsDrug Resistance, Multiple, BacterialEscherichia coliGene Knockout TechniquesGram-Negative Bacterial InfectionsMembrane Transport ProteinsMicrobial Sensitivity TestsPenicillin-Binding ProteinsPeptidoglycanPromoter Regions, GeneticPseudomonas aeruginosaAmpG protein, BacteriaAmpR protein, BacteriaBacterial Proteinsbeta-Lactamasesbeta-Lactamsbeta-N-AcetylhexosaminidasesBlaA protein, BacteriaDNA-Binding ProteinsMembrane Transport ProteinsPenicillin-Binding ProteinsPeptidoglycan

Identifiers

PMID25136029
PMCPMC4249409
OpenAlexW1967312581

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.