Evidence map›Paper›PMID 32464640›Full record

ArticleThe Journal of antimicrobial chemotherapy2020

Structural and biochemical characterization of the environmental MBLs MYO-1, ECV-1 and SHD-1.

Christopher Fröhlich, Vidar Sørum, Sandra Huber, Ørjan Samuelsen, Fanny Berglund, Erik Kristiansson, Stathis D Kotsakis, Nachiket P Marathe, D G Joakim Larsson, Hanna-Kirsti S Leiros

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In one paragraph

Article in The Journal of antimicrobial chemotherapy, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 42% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

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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

10 authors at 4 institutions in 2 countries.

Christopher FröhlichThe Norwegian Structural Biology Centre (NorStruct), Department of Chemistry, UiT The Arctic University of Norway, Tromsø, Norway.
Vidar SørumDepartment of Pharmacy, UiT The Arctic University of Norway, Tromsø, Norway.
Sandra HuberDepartment of Laboratory Medicine, University Hospital of North Norway, Tromsø, Norway.
Ørjan SamuelsenDepartment of Pharmacy, UiT The Arctic University of Norway, Tromsø, Norway.
Fanny BerglundDepartment of Mathematical Sciences, Chalmers University of Technology, Gothenburg, Sweden.
Erik KristianssonDepartment of Mathematical Sciences, Chalmers University of Technology, Gothenburg, Sweden.
Stathis D KotsakisDepartment of Infectious Diseases, Institute of Biomedicine, The Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
Nachiket P MaratheDepartment of Mathematical Sciences, Chalmers University of Technology, Gothenburg, Sweden.
D G Joakim LarssonDepartment of Infectious Diseases, Institute of Biomedicine, The Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
Hanna-Kirsti S LeirosThe Norwegian Structural Biology Centre (NorStruct), Department of Chemistry, UiT The Arctic University of Norway, Tromsø, Norway.
Chalmers University of Technology · SEUiT The Arctic University of Norway · NOUniversity Hospital of North Norway · NOUniversity of Gothenburg · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMBLs form a large and heterogeneous group of bacterial enzymes conferring resistance to β-lactam antibiotics, including carbapenems. A large environmental reservoir of MBLs has been identified, which can act as a source for transfer into human pathogens. Therefore, structural investigation of environmental and clinically rare MBLs can give new insights into structure-activity relationships to explore the role of catalytic and second shell residues, which are under selective pressure.

objectivesTo investigate the structure and activity of the environmental subclass B1 MBLs MYO-1, SHD-1 and ECV-1.

methodsThe respective genes of these MBLs were cloned into vectors and expressed in Escherichia coli. Purified enzymes were characterized with respect to their catalytic efficiency (kcat/Km). The enzymatic activities and MICs were determined for a panel of different β-lactams, including penicillins, cephalosporins and carbapenems. Thermostability was measured and structures were solved using X-ray crystallography (MYO-1 and ECV-1) or generated by homology modelling (SHD-1).

resultsExpression of the environmental MBLs in E. coli resulted in the characteristic MBL profile, not affecting aztreonam susceptibility and decreasing susceptibility to carbapenems, cephalosporins and penicillins. The purified enzymes showed variable catalytic activity in the order of <5% to ∼70% compared with the clinically widespread NDM-1. The thermostability of ECV-1 and SHD-1 was up to 8°C higher than that of MYO-1 and NDM-1. Using solved structures and molecular modelling, we identified differences in their second shell composition, possibly responsible for their relatively low hydrolytic activity.

conclusionsThese results show the importance of environmental species acting as reservoirs for MBL-encoding genes.

Indexed as

beta-LactamasesEscherichia coliAnti-Bacterial AgentsCarbapenemsHumansMicrobial Sensitivity TestsAnti-Bacterial Agentsbeta-LactamasesCarbapenems

Identifiers

PMID32464640
PMCPMC7443720
OpenAlexW3030631781

What OpenQuestion holds

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LicenceCC BY
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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.