Participation of PBP 3 in the acquisition of dicloxacillin resistance in Listeria monocytogenes.

GUTKIND G; OGUETA S; DE URTIAGA A; MOLLERACH M; DE TORRES RA

JOURNAL OF ANTIMICROBIAL CHEMOTHERAPY

Oxford University Press

Año: 1990 vol. 25 p. 751 - 758

0305-7453

Purified membranes of Listeria monocytogenes ATCC 15313 contain at least five penicillin-binding proteins. In two dicloxacillin resistant mutants, derived from a sensitive parent strain, a 16-fold increase in the MIC of dicloxacillin was observed. A less significant increse was detected in the MICs of other beta lactam drugs. In the mutants, PBP 3 lost its strong affinity for dicloxacillin, but remained fully susceptible to binding of 125-I-Penicillin X, as compared with the wild type strain. PBP 2 could not be detected in one of the mutants. No decrease in affinity for the radioactive tracer or dicloxacillin was detected in any other PBP of the resistant mutants.