Article (Scientific journals)
Genetic and biochemical characterisation of CTX-M-37 extended-spectrum β-lactamase from an Enterobacter cloacae clinical isolate from Mongolia
Lee, K.; Yong, D.; Jeong, S. H. et al.
2017In Journal of Global Antimicrobial Resistance, 10, p. 3-7
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Keywords :
CTX-M-37; Enterobacter cloacae; Extended-spectrum β-lactamase; Genetic environment; Kinetic parameters; Article; Escherichia coli; Kluyvera cryocrescens; Mongolia; DNA sequence; Kluyvera; Anti-Bacterial Agents; Bacterial Proteins; Cefotaxime; Genes, Bacterial; Humans; Kinetics; Microbial Sensitivity Tests; Sequence Analysis, DNA
Abstract :
[en] Objectives The aims of this study were to determine the resistance level of a bla CTX-M-37 -carrying Enterobacter cloacae isolate from Mongolia, to analyse kinetic parameters of the purified enzyme and to compare the genetic environment of the gene. Methods Minimum inhibitory concentrations (MICs) were determined using the Clinical and Laboratory Standards Institute (CLSI) agar dilution method. Purified CTX-M-37 enzyme was used to determined kinetic parameters. The genetic environment of the blaCTX-M-37 gene in E. cloacae was compared with a Kluyvera cryocrescens isolate. Results The E. cloacae isolate showed relatively low-level resistance to cefotaxime (MIC = 16 mg/L) compared with a CTX-M-3-producing strain (MIC = 256 mg/L), and CTX-M-37 had a lower k cat /K m value for cefotaxime (2.0 μM −1  s −1 ) compared with CTX-M-3 (3.5 μM −1  s −1 ), possibly due to Asn114Asp substitution. The bla CTX-M-37 gene in the E. cloacae isolate was carried on a conjugative plasmid and was associated with an ISEcp1 element containing the −35 and −10 putative promoter sequences TTGAAA and TACAAT, respectively, unlike in the K. cryocrescens isolate. Conclusions The CTX-M-37-producing E. cloacae isolate showed relatively low-level resistance to cefotaxime and the purified enzyme had lower kinetic parameters as the result of Asn114Asp substitution. Presence of an ISEcp1 element and putative promoters upstream of the bla CTX-M-37 gene in E. cloacae, but not in the K. cryocrescens isolate, indicated their roles in mobilisation and expression of the gene. © 2017 International Society for Chemotherapy of Infection and Cancer
Disciplines :
Biochemistry, biophysics & molecular biology
Microbiology
Author, co-author :
Lee, K.;  Department of Laboratory Medicine and Research Institute of Bacterial Resistance, Yonsei University College of Medicine, 50-1 Yonsei-ro, Seodaemun-gu, Seoul, 03722, South Korea
Yong, D.;  Department of Laboratory Medicine and Research Institute of Bacterial Resistance, Yonsei University College of Medicine, 50-1 Yonsei-ro, Seodaemun-gu, Seoul, 03722, South Korea
Jeong, S. H.;  Department of Laboratory Medicine and Research Institute of Bacterial Resistance, Yonsei University College of Medicine, 50-1 Yonsei-ro, Seodaemun-gu, Seoul, 03722, South Korea
Tulgaa, K.;  Department of Molecular Biology and Genetics, Research Center of Antimicrobial Resistance, Health Sciences University of Mongolia, Zorig Str. 4, Ulaanbaatar, Mongolia
Docquier, Jean-Denis ;  Université de Liège - ULiège > Département des sciences de la vie > Centre d'ingénierie des protéines
Rossolini, G. M.;  Department of Medical Biotechnologies, University of Siena, Viale Bracci 1, Siena, I-53100, Italy
Chong, Y.;  Department of Laboratory Medicine and Research Institute of Bacterial Resistance, Yonsei University College of Medicine, 50-1 Yonsei-ro, Seodaemun-gu, Seoul, 03722, South Korea
Language :
English
Title :
Genetic and biochemical characterisation of CTX-M-37 extended-spectrum β-lactamase from an Enterobacter cloacae clinical isolate from Mongolia
Publication date :
2017
Journal title :
Journal of Global Antimicrobial Resistance
ISSN :
2213-7165
eISSN :
2213-7173
Publisher :
Elsevier Ltd
Volume :
10
Pages :
3-7
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 19 November 2020

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