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Volume 131, Issue 8

One or Two Low Affinity Penicillin-binding Proteins May Be Responsible for the Range of Susceptibility of Enterococcus faecium to Benzylpenicillin Free

Abstract

Summary: Three benzylpenicillin-resistant, clinical isolates of (MIC values 16-64 μ;g ml) contained six penicillin-binding proteins (PBPs), of which PBP5 was the most abundant and had the lowest affinity for the antibiotic. Four benzylpenicillin-susceptible strains (MIC values 0·031-0·5 μ;g ml) were obtained as spontaneous derivatives from these above organisms. There were significant decreases in the amounts of PBP5 in each of the derivatives, with the concomitant appearance of a new, higher affinity PBP (5) in three strains. Increased amounts of PBP5, with no changes in PBP5, were found in several mutants with intermediate-level benzylpenicillin-resistance (MIC values 1-8 μ;g ml) selected from two of the susceptible strains. Examination of 18 other clinical isolates, with a wide range of susceptibilities to benzylpenicillin (MIC values 0·062-128 μ;g ml), showed that PBP5 was present in 13 strains, and PBP5 in all of them, but in differing amounts. The results concerning the relative amounts and relative affinities of PBPs 5 and 5 allowed the categorization of the various strains into six groups, within which organisms had somewhat similar susceptibilities to benzylpenicillin.

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© Society for General Microbiology 1985
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1985-08-01
2024-04-26
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One or Two Low Affinity Penicillin-binding Proteins May Be Responsible for the Range of Susceptibility of Enterococcus faecium to Benzylpenicillin
Microbiology 131, 1933 (1985); https://doi.org/10.1099/00221287-131-8-1933
/content/journal/micro/10.1099/00221287-131-8-1933
/content/journal/micro/10.1099/00221287-131-8-1933
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