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

A. Bauernfeind | Zendy; Sylvia Wagner | Zendy; R. Jungwirth | Zendy; I Schneider | Zendy; David J. Meyer | Zendy

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

Author(s) -

A. Bauernfeind,

Sylvia Wagner,

R. Jungwirth,

I Schneider,

David J. Meyer

Publication year - 1997

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.41.9.2041

Subject(s) - cefoxitin , escherichia coli , klebsiella pneumoniae , biology , microbiology and biotechnology , plasmid , beta lactamase , enterobacteriaceae , peptide sequence , gene , bacteria , genetics , staphylococcus aureus

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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