[Type TEM beta-lactamase activity in a Neisseria meningitidis strain]

We studied the beta-lactamase activity characteristics of a penicillin G resistant N. meningitidis strain (MIC = 8 micrograms/ml) isolated from a septicemic process, in an eleven month old girl, attended in the Sabadell Hospital (Barcelona). The beta-lactamase substrate profile was broad-spectrum (it hydrolyses penicillin G and cephaloridine) and the nitrocefin hydrolysis was inhibited by clavulanic acid. The analytical isoelectric focusing of the enzyme showed that the isoelectric point of the main band and, the secondary bands, were compatible with those of the type TEM-1 standard enzyme. We also obtained a positive DNA-DNA hybridization with the TEM-1 beta-lactamase (pBR322 plasmid).