SHV-5, a novel SHV-type beta-lactamase that hydrolyzes broad-spectrum cephalosporins and monobactams.
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.
Gutmann
L
L
Laboratoire de Microbiologie Médicale, Hospital Broussais, Paris, France.
Ferré
B
B
Goldstein
F W
FW
Rizk
N
N
Pinto-Schuster
E
E
Acar
J F
JF
Collatz
E
E
D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D002511:Cephalosporins / Q000378:metabolism*; D004269:DNA, Bacterial / Q000096:biosynthesis; D007711:Klebsiella pneumoniae / Q000201:enzymology*; D008826:Microbial Sensitivity Tests; D008997:Monobactams / Q000378:metabolism*; D009693:Nucleic Acid Hybridization; D010957:Plasmids; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases / Q000096:biosynthesis / Q000378:metabolism*
D000900:Anti-Bacterial Agents; D001425:Bacterial Outer Membrane Proteins; D002511:Cephalosporins; D004269:DNA, Bacterial; D008997:Monobactams; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases