Penicillin-binding proteins (PBPs) of NCTC 775, NCTC 7171 and an isolate of (strain 37) highly resistant to β-lactam antibiotics were visualised by autoradiography. Five PBPs were detected in NCTC 775 and six in NCTC 7171. Additional PBPs could not be found in the resistant isolate of

The PBP affinities of β lactams were compared with MIC values. The affinities of PBPs 3 and 4 of NCTC 775 for penicillin G, ampicillin, cefathiamidine, cephaloridine and cephazolin were related to the sensitivity of the strain to these antibiotics as were the affinities of PBPs 4 and 5 in each strain for the β lactams. It is postulated that PBPs 3 and 4 of NCTC 775 and PBPs 4 and 5 of are the relevant target enzymes of the test antibiotics. PBPs 4 and 5 of the highly β-lactam-resistant strain 37 showed proportionally low affinities for the five β lactams compared to that of the less resistant strain NCTC 7171. Decreased affinities of PBPs 4 and 5 may account for the resistance in strain 37 to β lactams. The affinities for PBP 1, 2 and 5 in NCTC 775 and PBPs 1, 2, 3 and 6 in were not related to the antibiotic sensitivities.


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