Open AccessA plasmid‐mediated CMY‐2 β‐lactamase from an Algerian clinical isolate of Salmonella senftenberg
Author(s) -
Koeck JeanLouis,
Arlet Guillaume,
Philippon Alain,
Basmaciogullari Stéphane,
Thien Hoang Vu,
Buisson Yves,
Cavallo JeanDidier
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb10436.x
Subject(s) - cefoxitin , plasmid , microbiology and biotechnology , escherichia coli , peptide sequence , biology , beta lactamase , salmonella , enterobacteriaceae , enzyme , amino acid , gene , bacteria , biochemistry , staphylococcus aureus , genetics
Multiresistance to antibiotics including β‐lactams, e.g. cefoxitin, was transferred by conjugation to Escherichia coli strain C1a from a clinical isolate of Salmonella senftenberg recovered from stools of an Algerian child. The susceptibility pattern to β‐lactams was similar to the profile mediated by an AmpC‐type β‐lactamase. By biochemical analysis, typical AmpC‐type enzyme substrate and inhibition profiles were obtained. Finally, an amp C plasmid‐encoded β‐lactamase gene was cloned and sequenced. Its deduced amino acid sequence confirmed its identity as a class C β‐lactamase. It showed 99.5% sequence identity with the plasmid‐mediated β‐lactamase CMY‐2. The differences in the amino acid sequences of the two enzymes were located in the signal peptide.