In vitro studies of plasmid-mediated penicillinase from Streptococcus faecalis suggest a staphylococcal origin.
A strain of Streptococcus faecalis with plasmid-mediated penicillinase production was studied further. Partially purified penicillinase from the S. faecalis strain hydrolyzed penicillin, ampicillin, and ureido-penicillins but not penicillinase-resistant semisynthetic penicillins, cephalosporins, or imipenem; hydrolysis was inhibited by clavulanic acid. Hydrolysis of a given antibiotic correlated with a marked increase in the minimal inhibitory concentration (MIC) of that drug when a high inoculum was used. As with most enterococci, the MICs of cephalosporins and penicillinase-resistant semisynthetic penicillins were too high for clinical usefulness, although these agents did not show an inoculum effect. Based upon hybridization under stringent conditions of plasmid DNA from the S. faecalis strain to cloned penicillinase genes from Staphylococcus aureus, it appears that these resistance determinants are highly homologous and suggests that this enzyme was introduced into streptococci from staphylococci.
Murray
B E
BE
Mederski-Samoraj
B
B
Foster
S K
SK
Brunton
J L
JL
Harford
P
P
D000900:Anti-Bacterial Agents / Q000378:metabolism; D013293:Enterococcus faecalis / Q000201:enzymology* / Q000235:genetics; D006868:Hydrolysis; D009693:Nucleic Acid Hybridization; D010405:Penicillinase / Q000235:genetics / Q000378:metabolism*; D011815:R Factors / Q000187:drug effects; D013211:Staphylococcus aureus / Q000201:enzymology* / Q000235:genetics; D013379:Substrate Specificity; D065093:beta-Lactamase Inhibitors; D047090:beta-Lactams
D000900:Anti-Bacterial Agents; D065093:beta-Lactamase Inhibitors; D047090:beta-Lactams; D010405:Penicillinase