Penicillin‐binding proteins in Listeria monocytogenes
- 1 July 1989
- Vol. 97 (7-12) , 1013-1017
- https://doi.org/10.1111/j.1699-0463.1989.tb00511.x
Abstract
The Penicillin-Binding Proteins (PBP) of Listeria monocytogenes 29-CCM-A: 454 (ATCC 15313) are described by the use of 125I-Penicillin X as radiotracer. The membranes of this tolerant bacilli contained at least five proteins with different affinities for the radiotracer or Dicloxacillin. The molecular weights of these proteins were estimated as 76, 74, 67, 66 and 47 KDa. Dicloxacillin induced the formation of straight filaments when present at sub-inhibitory concentrations, while Penicillin G did not induce any visible alteration in the morphology of this microorganism.Keywords
This publication has 11 references indexed in Scilit:
- Lounging in a lysosome: the intracellular lifestyle of Coxiella burnetiiCellular Microbiology, 2007
- Antimicrobial susceptibilities of Listeria monocytogenes strains isolated from 1958 to 1982 in SwedenAntimicrobial Agents and Chemotherapy, 1985
- PENICILLIN-BINDING PROTEINS AND THE MECHANISM OF ACTION OF BETA-LACTAM ANTIBIOTICSAnnual Review of Biochemistry, 1983
- Synthesis of a 125I-radiolabeled penicillin for penicillin-binding proteins studiesAnalytical Biochemistry, 1983
- The Mechanism of the Irreversible Antimicrobial Effects of Penicillins: How the Beta-Lactam Antibiotics Kill and Lyse BacteriaAnnual Review of Microbiology, 1979
- Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.Proceedings of the National Academy of Sciences, 1975
- Penicillin-binding proteins and cell shape in E. coliNature, 1975
- Five Penicillin-binding Components Occur in Bacillus subtilis MembranesJournal of Biological Chemistry, 1972
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Listeria monocytogenes and listeric infectionsMicrobiology and Molecular Biology Reviews, 1966