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OXA-484, an OXA-48-Type Carbapenem-Hydrolyzing Class D β-Lactamase From Escherichia coli

OXA-48-like carbapenemases are among the most frequent carbapenemases in Gram-negative Enterobacterales worldwide with the highest prevalence in the Middle East, North Africa and Europe. Here, we investigated the so far uncharacterized carbapenemase OXA-484 from a clinical E. coli isolate belonging...

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Autores principales: Sommer, Julian, Gerbracht, Kristina M., Krause, Felix F., Wild, Florian, Tietgen, Manuela, Riedel-Christ, Sara, Sattler, Janko, Hamprecht, Axel, Kempf, Volkhard A. J., Göttig, Stephan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8153228/
https://www.ncbi.nlm.nih.gov/pubmed/34054758
http://dx.doi.org/10.3389/fmicb.2021.660094
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author Sommer, Julian
Gerbracht, Kristina M.
Krause, Felix F.
Wild, Florian
Tietgen, Manuela
Riedel-Christ, Sara
Sattler, Janko
Hamprecht, Axel
Kempf, Volkhard A. J.
Göttig, Stephan
author_facet Sommer, Julian
Gerbracht, Kristina M.
Krause, Felix F.
Wild, Florian
Tietgen, Manuela
Riedel-Christ, Sara
Sattler, Janko
Hamprecht, Axel
Kempf, Volkhard A. J.
Göttig, Stephan
author_sort Sommer, Julian
collection PubMed
description OXA-48-like carbapenemases are among the most frequent carbapenemases in Gram-negative Enterobacterales worldwide with the highest prevalence in the Middle East, North Africa and Europe. Here, we investigated the so far uncharacterized carbapenemase OXA-484 from a clinical E. coli isolate belonging to the high-risk clone ST410 regarding antibiotic resistance pattern, horizontal gene transfer (HGT) and genetic support. OXA-484 differs by the amino acid substitution 214G compared to the most closely related variants OXA-181 (214R) and OXA-232 (214S). The bla(OXA)(–)(484) was carried on a self-transmissible 51.5 kb IncX3 plasmid (pOXA-484) showing high sequence similarity with plasmids harboring bla(OXA)(–)(181). Intraspecies and intergenus HGT of pOXA-484 to different recipients occurred at low frequencies of 1.4 × 10(–7) to 2.1 × 10(–6). OXA-484 increased MICs of temocillin and carbapenems similar to OXA-232 and OXA-244, but lower compared with OXA-48 and OXA-181. Hence, OXA-484 combines properties of OXA-181-like plasmid support and transferability as well as β-lactamase activity of OXA-232.
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spelling pubmed-81532282021-05-27 OXA-484, an OXA-48-Type Carbapenem-Hydrolyzing Class D β-Lactamase From Escherichia coli Sommer, Julian Gerbracht, Kristina M. Krause, Felix F. Wild, Florian Tietgen, Manuela Riedel-Christ, Sara Sattler, Janko Hamprecht, Axel Kempf, Volkhard A. J. Göttig, Stephan Front Microbiol Microbiology OXA-48-like carbapenemases are among the most frequent carbapenemases in Gram-negative Enterobacterales worldwide with the highest prevalence in the Middle East, North Africa and Europe. Here, we investigated the so far uncharacterized carbapenemase OXA-484 from a clinical E. coli isolate belonging to the high-risk clone ST410 regarding antibiotic resistance pattern, horizontal gene transfer (HGT) and genetic support. OXA-484 differs by the amino acid substitution 214G compared to the most closely related variants OXA-181 (214R) and OXA-232 (214S). The bla(OXA)(–)(484) was carried on a self-transmissible 51.5 kb IncX3 plasmid (pOXA-484) showing high sequence similarity with plasmids harboring bla(OXA)(–)(181). Intraspecies and intergenus HGT of pOXA-484 to different recipients occurred at low frequencies of 1.4 × 10(–7) to 2.1 × 10(–6). OXA-484 increased MICs of temocillin and carbapenems similar to OXA-232 and OXA-244, but lower compared with OXA-48 and OXA-181. Hence, OXA-484 combines properties of OXA-181-like plasmid support and transferability as well as β-lactamase activity of OXA-232. Frontiers Media S.A. 2021-05-12 /pmc/articles/PMC8153228/ /pubmed/34054758 http://dx.doi.org/10.3389/fmicb.2021.660094 Text en Copyright © 2021 Sommer, Gerbracht, Krause, Wild, Tietgen, Riedel-Christ, Sattler, Hamprecht, Kempf and Göttig. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Sommer, Julian
Gerbracht, Kristina M.
Krause, Felix F.
Wild, Florian
Tietgen, Manuela
Riedel-Christ, Sara
Sattler, Janko
Hamprecht, Axel
Kempf, Volkhard A. J.
Göttig, Stephan
OXA-484, an OXA-48-Type Carbapenem-Hydrolyzing Class D β-Lactamase From Escherichia coli
title OXA-484, an OXA-48-Type Carbapenem-Hydrolyzing Class D β-Lactamase From Escherichia coli
title_full OXA-484, an OXA-48-Type Carbapenem-Hydrolyzing Class D β-Lactamase From Escherichia coli
title_fullStr OXA-484, an OXA-48-Type Carbapenem-Hydrolyzing Class D β-Lactamase From Escherichia coli
title_full_unstemmed OXA-484, an OXA-48-Type Carbapenem-Hydrolyzing Class D β-Lactamase From Escherichia coli
title_short OXA-484, an OXA-48-Type Carbapenem-Hydrolyzing Class D β-Lactamase From Escherichia coli
title_sort oxa-484, an oxa-48-type carbapenem-hydrolyzing class d β-lactamase from escherichia coli
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8153228/
https://www.ncbi.nlm.nih.gov/pubmed/34054758
http://dx.doi.org/10.3389/fmicb.2021.660094
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