title: Penicillin-binding proteins in Listeria monocytogenes.
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.
authors.affiliation: Department of Microbiology and Immunology, Faculty of Pharmacy and Biochemistry, University of Buenos Aires, Argentina.
authors.forename: G O
authors.initials: GO
authors.lastname: Gutkind
authors.forename: M E
authors.initials: ME
authors.lastname: Mollerach
authors.forename: R A
authors.initials: RA
authors.lastname: De Torres
mesh_terms: D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000032:analysis*; D004009:Dicloxacillin / Q000494:pharmacology; D006602:Hexosyltransferases; D008089:Listeria monocytogenes / Q000032:analysis* / Q000187:drug effects; D008826:Microbial Sensitivity Tests; D002267:Muramoylpentapeptide Carboxypeptidase / Q000032:analysis*; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D004009:Dicloxacillin; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase