Abstract
Ten clinical isolates of Enterococcus faecalis were examined for susceptibility to the bactericidal activity of penicillin. Four of these had MBCs of penicillin equal to 2 to 4 x the MIC, and six exhibited a paradoxical response to penicillin, i.e., the bactericidal activity of the antibiotic had a concentration optimum at 2 to 4 x the MIC and decreased significantly at concentrations above this. We found that the paradoxical response to penicillin was an intrinsic and stable property of a strain, but that its phenotypic expression was not homogeneous; only a fraction of the cell population that died at low concentrations was able to survive at high penicillin concentrations. The size of this fraction increased with increasing antibiotic concentration and reached a maximum in the late-log phase of growth. All 10 strains produced a lytic enzyme that was active on Micrococcus luteus heat-killed cells, whereas only some strains lysed E. faecalis heat-killed cells. Strains producing large amounts of the latter enzyme did not show the paradoxical response to penicillin, whereas mutants of these strains that lacked this enzymatic activity paradoxically responded to the antibiotic activity. In addition, from strains that showed paradoxical response to penicillin and produced only the enzyme that was active on M. luteus, it was possible to isolate mutants that were also capable of lysing E. faecalis cells and that were killed with similar efficiency by all concentrations above the MBC. On the basis of these findings, the paradoxical response to penicillin is explained as a property of certain strains of E. faecalis; this property is genetically characterized by alterations in synthesis or activity of one autolysin but phenotypically expressed only by a few cells that are in a particular physiological condition when exposed to high concentrations of antibiotics.
MeSH Terms
Bacterial Proteins
Carrier Proteins/metabolism
Enterococcus faecalis/drug effects,genetics,metabolism
Hexosyltransferases
Micrococcus/drug effects,genetics
Muramoylpentapeptide Carboxypeptidase/metabolism
Penicillin Resistance
Penicillin-Binding Proteins
Penicillins/pharmacology
Peptidyl Transferases
Phenotype
Chemicals
Bacterial Proteins
Carrier Proteins
Penicillin-Binding Proteins
Penicillins
Peptidyl Transferases
Hexosyltransferases
Muramoylpentapeptide Carboxypeptidase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Fontana R
Institute of Microbiology, University of Verona, Italy.
Boaretti M
Grossato A
Tonin E A
Lleò M M
Satta G
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