Evidence map›Paper›PMID 26551395›Full record

ArticleNature chemical biology2016

Class D β-lactamases do exist in Gram-positive bacteria.

Marta Toth, Nuno Tiago Antunes, Nichole K Stewart, Hilary Frase, Monolekha Bhattacharya, Clyde A Smith, Sergei B Vakulenko

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.1field-weighted citation impact, top 27% 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

39 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
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  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. The biogenesis of β-lactamase enzymes.Microbiology (Reading, England) · 2022
    Review
  15. Article
  16. Article
  17. Dynamic Gene Clusters Mediating Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2022
    Article
  18. Article
  19. Article
  20. Medicinal Chemistry of Inhibitors Targeting Resistant Bacteria.Current topics in medicinal chemistry · 2022
    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

7 authors at 2 institutions in 1 country.

Marta TothDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA.
Nuno Tiago AntunesDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA.
Nichole K StewartDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA.
Hilary FraseDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA.
Monolekha BhattacharyaDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA.
Clyde A SmithStanford Synchrotron Radiation Lightsource, Stanford University, Menlo Park, California, USA.
Sergei B VakulenkoDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA.
University of Notre Dame · USStanford Synchrotron Radiation Lightsource · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41GM103393
6 · The paper itself

Abstract

Production of β-lactamases of one of four molecular classes (A, B, C and D) is the major mechanism of bacterial resistance to β-lactams, the largest class of antibiotics, which have saved countless lives since their inception 70 years ago. Although several hundred efficient class D enzymes have been identified in Gram-negative pathogens over the last four decades, none have been reported in Gram-positive bacteria. Here we demonstrate that efficient class D β-lactamases capable of hydrolyzing a wide array of β-lactam substrates are widely disseminated in various species of environmental Gram-positive organisms. Class D enzymes of Gram-positive bacteria have a distinct structural architecture and employ a unique substrate-binding mode that is quite different from that of all currently known class A, C and D β-lactamases. These enzymes thus constitute a previously unknown reservoir of novel antibiotic-resistance enzymes.

Indexed as

Amino Acid SequenceArginineBacillaceaebeta-Lactamasesbeta-LactamsCrystallography, X-RayDrug Resistance, BacterialEscherichia coliGram-Positive BacteriaHydrolysisMicrobial Sensitivity TestsMolecular Sequence DataProtein ConformationSequence Homology, Amino AcidArgininebeta-Lactamasesbeta-Lactams

Identifiers

PMID26551395
PMCPMC4684797
OpenAlexW2152842167

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.