Evidence map›Paper›PMID 30397053›Full record

ArticleAntimicrobial agents and chemotherapy2019

Characterization of the First OXA-10 Natural Variant with Increased Carbapenemase Activity.

Stathis D Kotsakis, Carl-Fredrik Flach, Mohammad Razavi, D G Joakim Larsson

Open access · bronzeAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.0field-weighted citation impact, top 29% 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

29 citing papers in PubMed, 33 citations in OpenAlex.

  1. Lanthipeptides fromMicrobiology spectrum · 2026
    Article
  2. Carbapenem resistance mediated byMicrobiology spectrum · 2026
    Article
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  9. Traditional marketed meats as a reservoir of multidrug-resistant Escherichia coli.International microbiology : the official journal of the Spanish Society for Microbiology · 2025
    Article
  10. Article
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  13. Article
  14. Identification of IncA Plasmid, HarboringAntibiotics (Basel, Switzerland) · 2023
    Article
  15. Article
  16. Review
  17. Insight into the Mechanisms of Carbapenem Resistance inAntibiotics (Basel, Switzerland) · 2023
    Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Stathis D KotsakisDepartment of Infectious Diseases, Institute of Biomedicine, The Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
Carl-Fredrik FlachDepartment of Infectious Diseases, Institute of Biomedicine, The Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
Mohammad RazaviDepartment of Infectious Diseases, Institute of Biomedicine, The Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
D G Joakim LarssonDepartment of Infectious Diseases, Institute of Biomedicine, The Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden joakim.larsson@fysiologi.gu.se.
University of Gothenburg · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

While carbapenem resistance in Gram-negative bacteria is mainly due to the production of efficient carbapenemases, β-lactamases with a narrower spectrum may also contribute to resistance when combined with additional mechanisms. OXA-10-type class D β-lactamases, previously shown to be weak carbapenemases, could represent such a case. In this study, two novel OXA-10 variants were identified as the sole carbapenem-hydrolyzing enzymes in meropenem-resistant enterobacteria isolated from hospital wastewater and found by next-generation sequencing to express additional β-lactam resistance mechanisms. The new variants, OXA-655 and OXA-656, were carried by two related IncQ1 broad-host-range plasmids. Compared to the sequence of OXA-10, they both harbored a Thr26Met substitution, with OXA-655 also bearing a leucine instead of a valine in position 117 of the SAV catalytic motif. Susceptibility profiling of laboratory strains replicating the natural

Indexed as

Amino Acid SubstitutionAnti-Bacterial AgentsBase Sequencebeta-Lactamasesbeta-Lactam ResistanceCatalytic DomainCefoxitinCloning, MolecularEnterobacteriaceaeGene ExpressionHospitalsHumansHydrolysisIsoenzymesKineticsMeropenemAnti-Bacterial Agentsbeta-lactamase OXA-10beta-LactamasesCefoxitinIsoenzymesMeropenemOxacillinPenicillinsRecombinant ProteinstemocillinWastewatercarbapenemasesCHDLIncQOXA-10β-lactamases

Identifiers

PMID30397053
PMCPMC6325193
OpenAlexW2898798406

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.