Abstract
The penicillin-binding proteins (PBPs) in two strains of Bacteroides uniformiswere visualized and identified by gel electrophoresis and subsequent fluorography. One of the strains ( B. uniformisB 371) was highly β-lactam resistant and β-lactamase producing, and the other was a reference ATCC type strain (ATCC 8492). Clavulanic acid was used in the assay to block the β-lactamase activity. Five major PBPs could be demonstrated, ranging in molecular weights from 66–92 kD. The PBP patterns of the two strains were similar except for PBP 4, which had a slightly higher molecular weight in the resistant strain B. uniformisB 371. A competition assay with ampicillin, piperacillin, cephalothin and cephaloridine showed differences in binding to the PBPs of the two strains. The binding of piperacillin to PBP 1 was more than ten-fold lower in the B 371 strain compared with the ATCC 8492 strain. The IC 50s of piperacillin, cephalothin and cephaloridine for PBP 4 were between seven and 300-fold higher in the B 371 strain than in the ATCC strain.
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