Evidence map›Paper›PMID 30006399›Full record

ReviewApplied and environmental microbiology2018

Diversity and Proliferation of Metallo-β-Lactamases: a Clarion Call for Clinically Effective Metallo-β-Lactamase Inhibitors.

Anou M Somboro, John Osei Sekyere, Daniel G Amoako, Sabiha Y Essack, Linda A Bester

Open access · bronzeAbstract readReview
In one paragraph

Review in Applied and environmental microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.0field-weighted citation impact, top 4% 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

36 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Revisiting the Metallo-International journal of microbiology · 2025
    Review
  3. LysR-type transcriptional regulatorFrontiers in cellular and infection microbiology · 2025
    Article
  4. 7-Antibiotics (Basel, Switzerland) · 2024
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Synthesis and Characterization of Some New Quinoxalin-2(Molecules (Basel, Switzerland) · 2021
    Article
  18. Review
  19. Article
  20. Computationally designed peptide macrocycle inhibitors of New Delhi metallo-β-lactamase 1.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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 2 institutions in 1 country.

Anou M SomboroAntimicrobial Research Unit, School of Health Sciences, University of KwaZulu-Natal, Durban, South Africa anou.somboro@gmail.com jod14139@gmail.com.
John Osei SekyereDepartment of Medical Microbiology, Faculty of Health Sciences, University of Pretoria, Pretoria, South Africa anou.somboro@gmail.com jod14139@gmail.com.ORCID 0000-0002-9508-984X
Daniel G AmoakoAntimicrobial Research Unit, School of Health Sciences, University of KwaZulu-Natal, Durban, South Africa.
Sabiha Y EssackAntimicrobial Research Unit, School of Health Sciences, University of KwaZulu-Natal, Durban, South Africa.
Linda A BesterBiomedical Resource Unit, College of Health Sciences, University of KwaZulu-Natal, Durban, South Africa.
University of KwaZulu-Natal · ZAUniversity of Pretoria · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The worldwide proliferation of life-threatening metallo-β-lactamase (MBL)-producing Gram-negative bacteria is a serious concern to public health. MBLs are compromising the therapeutic efficacies of β-lactams, particularly carbapenems, which are last-resort antibiotics indicated for various multidrug-resistant bacterial infections. Inhibition of enzymes mediating antibiotic resistance in bacteria is one of the major promising means for overcoming bacterial resistance. Compounds having potential MBL-inhibitory activity have been reported, but none are currently under clinical trials. The need for developing safe and efficient MBL inhibitors (MBLIs) is obvious, particularly with the continuous spread of MBLs worldwide. In this review, the emergence and escalation of MBLs in Gram-negative bacteria are discussed. The relationships between different class B β-lactamases identified up to 2017 are represented by a phylogenetic tree and summarized. In addition, approved and/or clinical-phase serine β-lactamase inhibitors are recapitulated to reflect the successful advances made in developing class A β-lactamase inhibitors. Reported MBLIs, their inhibitory properties, and their purported modes of inhibition are delineated. Insights into structural variations of MBLs and the challenges involved in developing potent MBLIs are also elucidated and discussed. Currently, natural products and MBL-resistant β-lactam analogues are the most promising agents that can become clinically efficient MBLIs. A deeper comprehension of the mechanisms of action and activity spectra of the various MBLs and their inhibitors will serve as a bedrock for further investigations that can result in clinically useful MBLIs to curb this global menace.

Indexed as

AnimalsAnti-Bacterial AgentsBacterial InfectionsBacterial Proteinsbeta-Lactamase Inhibitorsbeta-LactamasesDrug Resistance, BacterialGram-Negative BacteriaHumansAnti-Bacterial AgentsBacterial Proteinsbeta-Lactamase Inhibitorsbeta-Lactamasesantibiotic resistanceGram-negative bacteriametallo-β-lactamasemetallo-β-lactamase inhibitorsβ-lactam antibioticsβ-lactamase

Identifiers

PMID30006399
PMCPMC6121990
OpenAlexW2813449674

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.