Inactivation of beta-lactam antibiotics by Legionella pneumophila.
Antimicrob Agents Chemother, 1979/11;16(5):561-4.
PMID: 316686
Impact factor: 5.938
Abstract
Beta-lactam-inactivating activity has been found in all sero-groups of Legionella pneumophila. The beta-lactamase activity could be detected in intact cells and released by ethylenediaminetetraacetic acid treatment, indicating that it is located in the periplasmic space. The enzyme acted primarily as a cephalosporinase hydrolyzing cefamandole, cephalothin, cephaloridine, and also penicillin G and ampicillin. Cefoxitin and cefuroxime were not hydrolyzed. Clavulanic acid and CP-45,899, beta-lactamase inhibitors, prevented the hydrolysis of cephalosporins and penicillins. The beta-lactamase activity appears to be different from that found in Enterobacteriaceae and Pseudomonas.
MeSH terms
Anti-Bacterial Agents; Drug Resistance, Microbial; Legionnaires' Disease; Microbial Sensitivity Tests; Substrate Specificity; Time Factors; beta-Lactamases; beta-Lactams
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