Genetic and Phenotypic Characterization of the Novel Metallo-β-Lactamase NDM-29 From Escherichia coli
Objectives: The New Delhi metallo-β-lactamase (NDM) can hydrolyze almost all clinically available β-lactam antibiotics and has widely spread all over the world. NDM-29, a novel carbapenemase, was discovered in an Escherichia coli (19NC225) isolated from a patient with biliary tract infection in 2019...
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Frontiers Media S.A.
2021
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oai:doaj.org-article:6f122d64b2b54b748b5e178958e103332021-11-10T11:21:45ZGenetic and Phenotypic Characterization of the Novel Metallo-β-Lactamase NDM-29 From Escherichia coli1664-302X10.3389/fmicb.2021.743981https://doaj.org/article/6f122d64b2b54b748b5e178958e103332021-09-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fmicb.2021.743981/fullhttps://doaj.org/toc/1664-302XObjectives: The New Delhi metallo-β-lactamase (NDM) can hydrolyze almost all clinically available β-lactam antibiotics and has widely spread all over the world. NDM-29, a novel carbapenemase, was discovered in an Escherichia coli (19NC225) isolated from a patient with biliary tract infection in 2019 in China.Methods: Conjugation, transformation, cloning test, fitness cost, PacBio Sequel, and Illumina sequencing were performed to analyze the genetic and phenotypic characterization of blaNDM–29.Results: The susceptibility testing results showed 19NC225 was resistant to cephalosporins, carbapenems, combinations of β-lactam and β-lactamase inhibitors, and levofloxacin. Conjugation and transformation were performed to verify the transferability of NDM-29-encoding plasmid, and cloning test was conducted to prove the function of blaNDM–29 to increase carbapenem resistance. Furthermore, fitness cost test confirmed that the presence of NDM-29 exerts no survival pressure on bacteria. PacBio Sequel and Illumina sequencing were performed to analyze the genetic characterization of 19NC225, which contains two plasmids (pNC225-TEM1B and pNC225-NDM-29). pNC225-NDM-29, exhibiting 99.96% identity and 100% coverage with pNDM-BTR (an IncN1 plasmid from an E. coli in urine specimen from Beijing in 2013), showed responsibility for the multidrug-resistant (MDR) phenotype. Compared with blaNDM–1, blaNDM–29, located on pNC225-NDM-29, carries a G388A (D130N) mutation. The region harboring blaNDM–29 is located in an ISKpn19-based transposon, and two Tn6292 remnants are symmetrically located upstream and downstream of the transposon. The sequence results also indicated several important virulence genes.Conclusion: The findings of the novel carbapenemase NDM-29 could pose a threat to the control of antimicrobial resistance and arouse attention about the mutation of bacteria.Ying ZhuYing ZhuXinmiao JiaXinmiao JiaPeiyao JiaPeiyao JiaXue LiXue LiQiwen YangFrontiers Media S.A.articlecarbapenemaseNDMEscherichia coliwhole-genome sequenceantimicrobial resistanceMicrobiologyQR1-502ENFrontiers in Microbiology, Vol 12 (2021) |
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carbapenemase NDM Escherichia coli whole-genome sequence antimicrobial resistance Microbiology QR1-502 |
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carbapenemase NDM Escherichia coli whole-genome sequence antimicrobial resistance Microbiology QR1-502 Ying Zhu Ying Zhu Xinmiao Jia Xinmiao Jia Peiyao Jia Peiyao Jia Xue Li Xue Li Qiwen Yang Genetic and Phenotypic Characterization of the Novel Metallo-β-Lactamase NDM-29 From Escherichia coli |
| description |
Objectives: The New Delhi metallo-β-lactamase (NDM) can hydrolyze almost all clinically available β-lactam antibiotics and has widely spread all over the world. NDM-29, a novel carbapenemase, was discovered in an Escherichia coli (19NC225) isolated from a patient with biliary tract infection in 2019 in China.Methods: Conjugation, transformation, cloning test, fitness cost, PacBio Sequel, and Illumina sequencing were performed to analyze the genetic and phenotypic characterization of blaNDM–29.Results: The susceptibility testing results showed 19NC225 was resistant to cephalosporins, carbapenems, combinations of β-lactam and β-lactamase inhibitors, and levofloxacin. Conjugation and transformation were performed to verify the transferability of NDM-29-encoding plasmid, and cloning test was conducted to prove the function of blaNDM–29 to increase carbapenem resistance. Furthermore, fitness cost test confirmed that the presence of NDM-29 exerts no survival pressure on bacteria. PacBio Sequel and Illumina sequencing were performed to analyze the genetic characterization of 19NC225, which contains two plasmids (pNC225-TEM1B and pNC225-NDM-29). pNC225-NDM-29, exhibiting 99.96% identity and 100% coverage with pNDM-BTR (an IncN1 plasmid from an E. coli in urine specimen from Beijing in 2013), showed responsibility for the multidrug-resistant (MDR) phenotype. Compared with blaNDM–1, blaNDM–29, located on pNC225-NDM-29, carries a G388A (D130N) mutation. The region harboring blaNDM–29 is located in an ISKpn19-based transposon, and two Tn6292 remnants are symmetrically located upstream and downstream of the transposon. The sequence results also indicated several important virulence genes.Conclusion: The findings of the novel carbapenemase NDM-29 could pose a threat to the control of antimicrobial resistance and arouse attention about the mutation of bacteria. |
| format |
article |
| author |
Ying Zhu Ying Zhu Xinmiao Jia Xinmiao Jia Peiyao Jia Peiyao Jia Xue Li Xue Li Qiwen Yang |
| author_facet |
Ying Zhu Ying Zhu Xinmiao Jia Xinmiao Jia Peiyao Jia Peiyao Jia Xue Li Xue Li Qiwen Yang |
| author_sort |
Ying Zhu |
| title |
Genetic and Phenotypic Characterization of the Novel Metallo-β-Lactamase NDM-29 From Escherichia coli |
| title_short |
Genetic and Phenotypic Characterization of the Novel Metallo-β-Lactamase NDM-29 From Escherichia coli |
| title_full |
Genetic and Phenotypic Characterization of the Novel Metallo-β-Lactamase NDM-29 From Escherichia coli |
| title_fullStr |
Genetic and Phenotypic Characterization of the Novel Metallo-β-Lactamase NDM-29 From Escherichia coli |
| title_full_unstemmed |
Genetic and Phenotypic Characterization of the Novel Metallo-β-Lactamase NDM-29 From Escherichia coli |
| title_sort |
genetic and phenotypic characterization of the novel metallo-β-lactamase ndm-29 from escherichia coli |
| publisher |
Frontiers Media S.A. |
| publishDate |
2021 |
| url |
https://doaj.org/article/6f122d64b2b54b748b5e178958e10333 |
| work_keys_str_mv |
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