Juan Manuel de Mendieta , Denise De Belder , Nathalie Tijet , Barbara Ghiglione , Roberto G. Melano , Melina Rapoport , Pablo Power , Adriana Di Bella , Estefanía Biondi , Fernando Pasterán , Alejandra Corso , Sonia A. Gomez
{"title":"阿根廷临床病例分离的IncN2和IncC2质粒上携带的blaoxa -48样新等位变异blaOXA-567的体内出现。","authors":"Juan Manuel de Mendieta , Denise De Belder , Nathalie Tijet , Barbara Ghiglione , Roberto G. Melano , Melina Rapoport , Pablo Power , Adriana Di Bella , Estefanía Biondi , Fernando Pasterán , Alejandra Corso , Sonia A. Gomez","doi":"10.1016/j.jgar.2024.12.008","DOIUrl":null,"url":null,"abstract":"<div><h3>Objective</h3><div>The OXA-48-like enzymes have the capacity to hydrolyse carbapenems and are members of class D β-lactamases that are primarily detected in <em>Enterobacterales</em>. The allelic variant <em>bla</em><sub>OXA-163</sub>, which has low hydrolytic activity towards carbapenems, was detected in Argentina in 2011 and has spread successfully since then, giving sporadic origin to novel local variants. The aim of this study was to analyse the phenotypic profile and dissemination strategies of two novel OXA enzymes, <em>bla</em><sub>OXA-438</sub> and <em>bla</em><sub>OXA-567</sub>, located in <em>Escherichia coli</em> M17224 and <em>Klebsiella pneumoniae</em> M21014, respectively, isolated from two paediatric patients.</div></div><div><h3>Methods</h3><div>Minimum inhibitory concentration measurements were performed to determine the phenotypic profile of the clinical isolates, transconjugants and transformant cells. Biparental conjugation, PCR, Sanger and whole-genome sequencing were performed to determine the complete genetic characteristics of the plasmids.</div></div><div><h3>Results</h3><div>Both isolates were found to be resistant to carbapenems and susceptible to ceftriaxone. <em>bla</em><sub>OXA-438</sub> was located on a 69-kb IncN<sub>2</sub> plasmid, while <em>bla</em><sub>OXA-567</sub> was found on a 175-Kb IncC<sub>2</sub> plasmid, both transferable by biparental conjugation. The close genetic environment of the <em>bla</em><sub>OXA</sub> genes suggests a common origin likely involving mobile genetic elements. Finally, the clinical case of M21014 revealed that the patient had previous infections with two genetically related <em>K. pneumoniae</em> ST6838 that carried <em>bla</em><sub>OXA-163</sub> on an IncC<sub>2</sub> plasmid with equal size and genetic hallmarks to that of M21014, providing strong evidence for the intra-patient emergence of <em>bla</em><sub>OXA-567.</sub></div></div><div><h3>Conclusions</h3><div>This research underscores the need for ongoing surveillance and integral studies to understand the emergence, biochemistry and dissemination capacity of OXA enzymes with the overarching aim to halt their spread.</div></div>","PeriodicalId":15936,"journal":{"name":"Journal of global antimicrobial resistance","volume":"41 ","pages":"Pages 88-95"},"PeriodicalIF":3.7000,"publicationDate":"2024-12-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Novel allelic variants of blaOXA-48-like carried on IncN2 and IncC2 plasmids isolated from clinical cases in Argentina: In vivo emergence of blaOXA-567\",\"authors\":\"Juan Manuel de Mendieta , Denise De Belder , Nathalie Tijet , Barbara Ghiglione , Roberto G. Melano , Melina Rapoport , Pablo Power , Adriana Di Bella , Estefanía Biondi , Fernando Pasterán , Alejandra Corso , Sonia A. Gomez\",\"doi\":\"10.1016/j.jgar.2024.12.008\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><h3>Objective</h3><div>The OXA-48-like enzymes have the capacity to hydrolyse carbapenems and are members of class D β-lactamases that are primarily detected in <em>Enterobacterales</em>. The allelic variant <em>bla</em><sub>OXA-163</sub>, which has low hydrolytic activity towards carbapenems, was detected in Argentina in 2011 and has spread successfully since then, giving sporadic origin to novel local variants. The aim of this study was to analyse the phenotypic profile and dissemination strategies of two novel OXA enzymes, <em>bla</em><sub>OXA-438</sub> and <em>bla</em><sub>OXA-567</sub>, located in <em>Escherichia coli</em> M17224 and <em>Klebsiella pneumoniae</em> M21014, respectively, isolated from two paediatric patients.</div></div><div><h3>Methods</h3><div>Minimum inhibitory concentration measurements were performed to determine the phenotypic profile of the clinical isolates, transconjugants and transformant cells. Biparental conjugation, PCR, Sanger and whole-genome sequencing were performed to determine the complete genetic characteristics of the plasmids.</div></div><div><h3>Results</h3><div>Both isolates were found to be resistant to carbapenems and susceptible to ceftriaxone. <em>bla</em><sub>OXA-438</sub> was located on a 69-kb IncN<sub>2</sub> plasmid, while <em>bla</em><sub>OXA-567</sub> was found on a 175-Kb IncC<sub>2</sub> plasmid, both transferable by biparental conjugation. The close genetic environment of the <em>bla</em><sub>OXA</sub> genes suggests a common origin likely involving mobile genetic elements. Finally, the clinical case of M21014 revealed that the patient had previous infections with two genetically related <em>K. pneumoniae</em> ST6838 that carried <em>bla</em><sub>OXA-163</sub> on an IncC<sub>2</sub> plasmid with equal size and genetic hallmarks to that of M21014, providing strong evidence for the intra-patient emergence of <em>bla</em><sub>OXA-567.</sub></div></div><div><h3>Conclusions</h3><div>This research underscores the need for ongoing surveillance and integral studies to understand the emergence, biochemistry and dissemination capacity of OXA enzymes with the overarching aim to halt their spread.</div></div>\",\"PeriodicalId\":15936,\"journal\":{\"name\":\"Journal of global antimicrobial resistance\",\"volume\":\"41 \",\"pages\":\"Pages 88-95\"},\"PeriodicalIF\":3.7000,\"publicationDate\":\"2024-12-25\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of global antimicrobial resistance\",\"FirstCategoryId\":\"3\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S2213716524004703\",\"RegionNum\":3,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"INFECTIOUS DISEASES\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of global antimicrobial resistance","FirstCategoryId":"3","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2213716524004703","RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"INFECTIOUS DISEASES","Score":null,"Total":0}
Novel allelic variants of blaOXA-48-like carried on IncN2 and IncC2 plasmids isolated from clinical cases in Argentina: In vivo emergence of blaOXA-567
Objective
The OXA-48-like enzymes have the capacity to hydrolyse carbapenems and are members of class D β-lactamases that are primarily detected in Enterobacterales. The allelic variant blaOXA-163, which has low hydrolytic activity towards carbapenems, was detected in Argentina in 2011 and has spread successfully since then, giving sporadic origin to novel local variants. The aim of this study was to analyse the phenotypic profile and dissemination strategies of two novel OXA enzymes, blaOXA-438 and blaOXA-567, located in Escherichia coli M17224 and Klebsiella pneumoniae M21014, respectively, isolated from two paediatric patients.
Methods
Minimum inhibitory concentration measurements were performed to determine the phenotypic profile of the clinical isolates, transconjugants and transformant cells. Biparental conjugation, PCR, Sanger and whole-genome sequencing were performed to determine the complete genetic characteristics of the plasmids.
Results
Both isolates were found to be resistant to carbapenems and susceptible to ceftriaxone. blaOXA-438 was located on a 69-kb IncN2 plasmid, while blaOXA-567 was found on a 175-Kb IncC2 plasmid, both transferable by biparental conjugation. The close genetic environment of the blaOXA genes suggests a common origin likely involving mobile genetic elements. Finally, the clinical case of M21014 revealed that the patient had previous infections with two genetically related K. pneumoniae ST6838 that carried blaOXA-163 on an IncC2 plasmid with equal size and genetic hallmarks to that of M21014, providing strong evidence for the intra-patient emergence of blaOXA-567.
Conclusions
This research underscores the need for ongoing surveillance and integral studies to understand the emergence, biochemistry and dissemination capacity of OXA enzymes with the overarching aim to halt their spread.
期刊介绍:
The Journal of Global Antimicrobial Resistance (JGAR) is a quarterly online journal run by an international Editorial Board that focuses on the global spread of antibiotic-resistant microbes.
JGAR is a dedicated journal for all professionals working in research, health care, the environment and animal infection control, aiming to track the resistance threat worldwide and provides a single voice devoted to antimicrobial resistance (AMR).
Featuring peer-reviewed and up to date research articles, reviews, short notes and hot topics JGAR covers the key topics related to antibacterial, antiviral, antifungal and antiparasitic resistance.