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. 1979 Nov;16(5):561-4.
doi: 10.1128/AAC.16.5.561.

Inactivation of beta-lactam antibiotics by Legionella pneumophila

K P Fu, H C Neu

Inactivation of beta-lactam antibiotics by Legionella pneumophila

K P Fu et al. Antimicrob Agents Chemother. 1979 Nov.

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.

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References

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