Evidence map›Paper›PMID 35758683›Full record

ArticleMicrobiology spectrum2022

Divergent Effects of Peptidoglycan Carboxypeptidase DacA on Intrinsic β-Lactam and Vancomycin Resistance.

Si Hyoung Park, Umji Choi, Su-Hyun Ryu, Han Byeol Lee, Jin-Won Lee, Chang-Ro Lee

Open access · goldAbstract read
In one paragraph

Article in Microbiology spectrum, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 32% 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

16 citing papers in PubMed, 12 citations in OpenAlex.

  1. A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein.Proceedings of the National Academy of Sciences of the United States of America · 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

6 authors at 2 institutions in 1 country.

Si Hyoung Park *Department of Biological Sciences, Myongji University, Yongin, Gyeonggido, Republic of Korea.
Umji Choi *Department of Biological Sciences, Myongji University, Yongin, Gyeonggido, Republic of Korea.
Su-Hyun RyuDepartment of Life Science and Research Institute for Natural Sciences, Hanyang Universitygrid.49606.3d, Seoul, Republic of Korea.
Han Byeol LeeDepartment of Biological Sciences, Myongji University, Yongin, Gyeonggido, Republic of Korea.
Jin-Won LeeDepartment of Life Science and Research Institute for Natural Sciences, Hanyang Universitygrid.49606.3d, Seoul, Republic of Korea.
Chang-Ro LeeDepartment of Biological Sciences, Myongji University, Yongin, Gyeonggido, Republic of Korea.
Myongji University · KRHanyang University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vancomycin and β-lactams are clinically important antibiotics that inhibit the formation of peptidoglycan cross-links, but their binding targets are different. The binding target of vancomycin is d-alanine-d-alanine (d-Ala-d-Ala), whereas that of β-lactam is penicillin-binding proteins (PBPs). In this study, we revealed the divergent effects of peptidoglycan (PG) carboxypeptidase DacA on vancomycin and β-lactam resistance in Escherichia coli and Bacillus subtilis. The deletion of DacA induced sensitivity to most β-lactams, whereas it induced strong resistance toward vancomycin. Notably, both phenotypes did not have a strong association with ld-transpeptidases, which are necessary for the formation of PG 3-3 cross-links and covalent bonds between PG and an Lpp outer membrane (OM) lipoprotein. Vancomycin resistance was induced by an increased amount of decoy d-Ala-d-Ala residues within PG, whereas β-lactam sensitivity was associated with physical interactions between DacA and PBPs. The presence of an OM permeability barrier strongly strengthened vancomycin resistance, but it significantly weakened β-lactam sensitivity. Collectively, our results revealed two distinct functions of DacA, which involved inverse modulation of bacterial resistance to clinically important antibiotics, β-lactams and vancomycin, and presented evidence for a link between DacA and PBPs.

Indexed as

beta-LactamsPeptidoglycanAlanineAnti-Bacterial AgentsBacterial ProteinsCarboxypeptidasesEscherichia coliVancomycinVancomycin ResistanceAlanineAnti-Bacterial AgentsBacterial Proteinsbeta-LactamsCarboxypeptidasesPeptidoglycanVancomycinantibiotic resistanceDacAd-Ala-d-Aladecoyld-transpeptidasemembrane permeabilitypenicillin-binding proteinspeptidoglycan carboxypeptidasepeptidoglycan hydrolasevancomycinβ-lactam

Identifiers

PMID35758683
PMCPMC9430164
OpenAlexW4283581681

What OpenQuestion holds

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LicenceCC BY
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.