Open AccessSHV-5, a novel SHV-type beta-lactamase that hydrolyzes broad-spectrum cephalosporins and monobactams
Author(s) -
Laurent Gutmann,
B. Ferré,
F. W. Goldstein,
N. Rizk,
E. Pinto-Schuster,
Jacqu̧es Acar,
E. Collatz
Publication year - 1989
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.33.6.951
Subject(s) - sulbactam , klebsiella pneumoniae , beta lactamase inhibitors , cephalosporin , clavulanic acid , imipenem , beta lactamase , microbiology and biotechnology , tazobactam , chemistry , biology , antibiotics , biochemistry , escherichia coli , amoxicillin , antibiotic resistance , gene
SHV-5 (pI 8.2), a novel broad-spectrum beta-lactamase encoded by a ca. 150-kilobase plasmid, was found in Klebsiella pneumoniae 160. SHV-5 beta-lactamase caused decreased susceptibility to most penicillins, cephalosporins, and monobactams, except imipenem and compounds which have a C6 or C7 alpha-methoxy substituent. beta-Lactamase inhibitors (clavulanic acid, sulbactam, and tazobactam) inhibited its activity and showed a synergistic effect when associated with different hydrolyzable beta-lactam compounds. Hybridization studies suggested that this enzyme may be related to, or derived from, the SHV enzyme. Increased MICs of cephamycins and temocillin associated with a decreased synergistic effect of the inhibitors on K. pneumoniae 160 might be linked to a decrease in two outer membrane proteins.