Activity of avibactam against Enterobacter cloacae producing an extended-spectrum class C -lactamase enzyme
Author(s) -
Sushmita D. Lahiri,
R.A. Giacobbe,
Michele Johnstone,
Richard A. Alm
Publication year - 2014
Publication title -
journal of antimicrobial chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.124
H-Index - 194
eISSN - 1460-2091
pISSN - 0305-7453
DOI - 10.1093/jac/dku237
Subject(s) - enterobacter cloacae , avibactam , microbiology and biotechnology , enterobacter , beta lactamase inhibitors , ceftazidime/avibactam , enterobacteriaceae , enterobacteriaceae infections , chemistry , enzyme , klebsiella pneumoniae , bacterial protein , biology , escherichia coli , antibiotics , bacteria , biochemistry , genetics , gene
Extended-spectrum AmpC (ESAC) β-lactamase enzymes, which are either chromosomally encoded or plasmid encoded, have minor structural changes that broaden their substrate hydrolysis profile. The derepressed AmpC enzyme found once in Enterobacter cloacae CHE was shown to contain a six residue deletion in the H-10 helix in close proximity to the active site. Avibactam is a non-β-lactam inhibitor of Ambler class A, class C and some class D β-lactamases that is in clinical development with several β-lactam agents. It has been shown to inhibit AmpC enzymes, but its microbiological activity against isolates carrying different ESAC enzymes is less well understood.
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