scholarly journals Molecular characterization of genes encoding plasmid- mediated-AmpC beta-lactamases in Escherichia coli isolated from urinary tract infection

2021 ◽  
Vol 39 ◽  
pp. S3
Author(s):  
Ismat Rehana ◽  
Anita Pandey ◽  
Sonali Jindal
Keyword(s):  
Escherichia Coli ◽  
Urinary Tract Infection ◽  
Urinary Tract ◽  
Tract Infection ◽  
Molecular Characterization ◽  
Beta Lactamases ◽  
Genes Encoding

scholarly journals Characterization of Escherichia coli Isolates from Hospital Inpatients or Outpatients with Urinary Tract Infection

2013 ◽  
Vol 52 (2) ◽  
pp. 407-418 ◽  
Author(s):  
F. Toval ◽  
C.-D. Kohler ◽  
U. Vogel ◽  
F. Wagenlehner ◽  
A. Mellmann ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Urinary Tract Infection ◽  
Urinary Tract ◽  
Tract Infection ◽  
Hospital Inpatients

A novel class C beta-lactamase (FOX-2) in Escherichia coli conferring resistance to cephamycins.

1997 ◽  
Vol 41 (9) ◽  
pp. 2041-2046 ◽  
Author(s):  
A Bauernfeind ◽  
S Wagner ◽  
R Jungwirth ◽  
I Schneider ◽  
D Meyer
Keyword(s):  
Escherichia Coli ◽  
Urinary Tract Infection ◽  
Urinary Tract ◽  
Amino Acid ◽  
Tract Infection ◽  
Coli Strain ◽  
Beta Lactamase ◽  
Beta Lactams ◽  
Beta Lactamases ◽  
Pcr Product

An Escherichia coli strain resistant to a broad spectrum of beta-lactams, including cephamycins, was isolated from a patient suffering from urinary tract infection. A resistance plasmid (pMVP-7) was transferred from the clinical isolate to an Escherichia coli recipient. Both strains produce a cefoxitin-hydrolyzing beta-lactamase focusing at pI 6.7. The phenotype was similar to that of a Klebsiella pneumoniae strain producing cephamycinase FOX-1, so primers were selected from the FOX-1 sequence to amplify the bla gene of the transconjugant. The PCR product obtained was sequenced. The percentage of identity of the deduced amino acid sequence with sequences of other AmpC-type beta-lactamases was 96.9% with FOX-1, 74.9% with CMY-1, and 67.7% with MOX-1. This new plasmid-mediated enzyme is most closely related to FOX-1 (11 amino acid exchanges). We therefore propose the designation FOX-2.

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