[Identification of a cephalosporinase susceptible to clavulanic acid in a clinical strain of Serratia fonticola].

We analyzed the beta-lactamase production of a Serratia fonticola isolated for its resistance to cefuroxime (Minimum Inhibitory Concentration > 256 mg/l) in December 1993 from a patient hospitalized in Meaux. The wild strain was resistant to amoxycillin but sensitive to augmentin, that suggested the production of a beta-lactamase susceptible to clavulanic acid. For the wild strain, beta-lactamase production was inducible and only one enzyme with an isoelectric point of 8.12 was detected. beta-lactamase production was 16 mU/mg for non-induced extracts and ranged from 100 to 230 mU/mg in the presence of inducing beta-lactams (enzyme activity was measured with penicillin G as substrate). On a Szybalski gradient a constitutive strain was obtained. Its enzyme production was 13,000 mU/mg. The kinetics and isoelectric points of the enzymes produced by the two strains were identical. This beta-lactamase hydrolyzes penicillins (amoxycillin: Vm = 60 relative to penicillin G = 100, ticarcillin: 15), first generation cephalosporins (cephalothin Vm = 930). However, this enzyme hydrolyzes efficiently oxyimino-cephalosporins: cefuroxime (Vm = 70) and cefotaxime (Vm = 120), but cephamycins are not substrates. Clavulanic acid has a very good affinity for this beta-lactamase (Ki = 0.09 microM) which is inactivated progressively (I50 = 0.045 microgram/ml). These properties shows some similarities with those of the class A beta-lactamases of P. vulgaris RO104 (pI = 8.3), P. penneri 14HBC (pI = 6.65) and the plasmid-mediated extended-spectrum MEN-1 (pI = 8.4).