Evidence map›Paper›PMID 29020980›Full record

ArticleMicrobiome2017

Identification of 76 novel B1 metallo-β-lactamases through large-scale screening of genomic and metagenomic data.

Fanny Berglund, Nachiket P Marathe, Tobias Österlund, Johan Bengtsson-Palme, Stathis Kotsakis, Carl-Fredrik Flach, D G Joakim Larsson, Erik Kristiansson

Open access · goldAbstract read
In one paragraph

Article in Microbiome, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

49 citing papers in PubMed, 103 citations in OpenAlex.

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  10. Expanding the β-Lactamase Family in the Human Microbiome.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
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  14. Characterization of blaAnnals of clinical microbiology and antimicrobials · 2023
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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

8 authors at 2 institutions in 1 country.

Fanny BerglundDepartment of Mathematical Sciences, Chalmers University of Technology, Gothenburg, Sweden.
Nachiket P MaratheCentre for Antibiotic Resistance Research (CARe), University of Gothenburg, Gothenburg, Sweden.
Tobias ÖsterlundDepartment of Mathematical Sciences, Chalmers University of Technology, Gothenburg, Sweden.
Johan Bengtsson-PalmeCentre for Antibiotic Resistance Research (CARe), University of Gothenburg, Gothenburg, Sweden.
Stathis KotsakisCentre for Antibiotic Resistance Research (CARe), University of Gothenburg, Gothenburg, Sweden.
Carl-Fredrik FlachCentre for Antibiotic Resistance Research (CARe), University of Gothenburg, Gothenburg, Sweden.
D G Joakim LarssonCentre for Antibiotic Resistance Research (CARe), University of Gothenburg, Gothenburg, Sweden.
Erik KristianssonDepartment of Mathematical Sciences, Chalmers University of Technology, Gothenburg, Sweden. erik.kristiansson@chalmers.se.ORCID 0000-0002-8609-2414
University of Gothenburg · SEChalmers University of Technology · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMetallo-β-lactamases are bacterial enzymes that provide resistance to carbapenems, the most potent class of antibiotics. These enzymes are commonly encoded on mobile genetic elements, which, together with their broad substrate spectrum and lack of clinically useful inhibitors, make them a particularly problematic class of antibiotic resistance determinants. We hypothesized that there is a large and unexplored reservoir of unknown metallo-β-lactamases, some of which may spread to pathogens, thereby threatening public health. The aim of this study was to identify novel metallo-β-lactamases of class B1, the most clinically important subclass of these enzymes.

resultsBased on a new computational method using an optimized hidden Markov model, we analyzed over 10,000 bacterial genomes and plasmids together with more than 5 terabases of metagenomic data to identify novel metallo-β-lactamase genes. In total, 76 novel genes were predicted, forming 59 previously undescribed metallo-β-lactamase gene families. The ability to hydrolyze imipenem in an Escherichia coli host was experimentally confirmed for 18 of the 21 tested genes. Two of the novel B1 metallo-β-lactamase genes contained atypical zinc-binding motifs in their active sites, which were previously undescribed for metallo-β-lactamases. Phylogenetic analysis showed that B1 metallo-β-lactamases could be divided into five major groups based on their evolutionary origin. Our results also show that, except for one, all of the previously characterized mobile B1 β-lactamases are likely to have originated from chromosomal genes present in Shewanella spp. and other Proteobacterial species.

conclusionsThis study more than doubles the number of known B1 metallo-β-lactamases. The findings have further elucidated the diversity and evolutionary history of this important class of antibiotic resistance genes and prepare us for some of the challenges that may be faced in clinics in the future.

Indexed as

Genome, BacterialAnimalsAnti-Bacterial AgentsBacteriabeta-LactamasesEscherichia coliGenomicsHumansImipenemMarkov ChainsMetagenomicsMicrobial Sensitivity TestsPhylogenyPlasmidsAnti-Bacterial Agentsbeta-LactamasesImipenemCarbapenemasesHidden Markov modelResistomeShotgun metagenomicsβ-lactam resistance

Identifiers

PMID29020980
PMCPMC5637372
OpenAlexW2761788747

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.