Inactivation of beta-lactam antibiotics by Legionella pneumophila.
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.
D000900:Anti-Bacterial Agents / Q000378:metabolism*; D004352:Drug Resistance, Microbial; D007877:Legionnaires' Disease / Q000382:microbiology*; D008826:Microbial Sensitivity Tests; D013379:Substrate Specificity; D013997:Time Factors; D001618:beta-Lactamases / Q000378:metabolism; D047090:beta-Lactams / Q000378:metabolism
D000900:Anti-Bacterial Agents; D047090:beta-Lactams; D001618:beta-Lactamases