Affinities of PBPs of enterococci to cefepime and ampicillin

Abstract

The beta-lactam resistance of genus Streptococcus has been explained by the low binding affinity of penicillin-binding proteins (PBPs) to the drug. This study was carried out to resolve the mechanisms of resistance to beta-lactam antibiotics in the species of genus Enterococcus by means of binding affinities of PBPs. Streptococcus pyogenes, Enterococcus faecalis, Enterococcus faecium and Enterococcus avium were employed as assay microbes. Cefepime (CFPM) and ampicillin (ABPC) were used as representatives of cephems and penicillins, respectively. All the PBP fractions of S. pyogenes manifested high binding affinities to CFPM and ABPC, whereas PBPs 1 and 4 of E. faecalis showed high binding affinities to ABPC but not to CFPM. In E. faecium, PBPs of an exceptionally penicillin-susceptible strain manifested a high binding affinity to ABPC, but PBPs 5 and 6 showed low affinities to CFPM. beta-lactam resistant strains of E. faecium possessed PBPs 5 and 6 with low binding affinities to CFPM and ABPC. All the fractions of PBPs but PBP 1 in E. avium showed low binding affinities to CFPM. Although all the PBP fractions but PBPs 3 and 6 manifested high binding affinities to ABPC, PBPs 3 and 6 showed low binding affinities to ABPC. A strain of E. avium, which is susceptible to ABPC but moderately resistant to CFPM, lacked PBP 6. In conclusion, the resistance of E. avium to CFPM is based upon low binding affinities of the many fractions to this drug, and ABPC resistance is based upon PBPs 3 and 6 with low binding affinities to ABPC.