Open AccessDissemination of the novel plasmid-mediated beta-lactamase CTX-1, which confers resistance to broad-spectrum cephalosporins, and its inhibition by beta-lactamase inhibitors
Author(s) -
M Kitzis,
D Billot-Klein,
F. W. Goldstein,
R. Williamson,
Guy Tran Van Nhieu,
Jean Carlet,
J. F. Acar,
Ludwig Gutmann
Publication year - 1988
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.32.1.9
Subject(s) - aztreonam , cefotaxime , ceftazidime , sulbactam , cephalosporin , beta lactamase , microbiology and biotechnology , piperacillin , clavulanic acid , imipenem , biology , beta lactamase inhibitors , plasmid , cefoperazone , cefoxitin , moxalactam , antibiotics , antibiotic resistance , bacteria , amoxicillin , biochemistry , gene , escherichia coli , genetics , pseudomonas aeruginosa , staphylococcus aureus
The novel beta-lactamase CTX-1 (pI 6.3) encoded on a transferable 84-kilobase plasmid was found in six different bacterial species. It was responsible for a significant decrease in susceptibility towards most penicillins and cephalosporins, except imipenem, temocillin, and cephalosporins which have a 7-alpha-methoxy substituent. Synergy between either ampicillin, piperacillin, cefotaxime, ceftazidime, or aztreonam and three beta-lactamase inhibitors (clavulanic acid, sulbactam, and YTR 830) was generally found for different strains harboring CTX-1. This enzyme may be related to or derived from the TEM enzyme, since an intragenic probe of the TEM-1 gene hybridized with a fragment of the plasmid carrying CTX-1.
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