Open AccessBinding of beta-lactam antibiotics to penicillin-binding proteins of Staphylococcus aureus and Streptococcus faecalis: relation to antibacterial activity
Author(s) -
Nafsika H. Georgopapadakou,
F Y Liu
Publication year - 1980
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.18.5.834
Subject(s) - penicillin binding proteins , staphylococcus aureus , penicillin , microbiology and biotechnology , antibiotics , context (archaeology) , enterococcus faecalis , streptococcus , chemistry , bacteria , biology , biochemistry , genetics , paleontology
The binding of 14 structurally diverse beta-lactam antibiotics to penicillin-binding proteins of Staphylococcus aureus and Streptococcus faecalis was studied, and the results were examined in the context of the antibacterial activity of the compounds. Penicillin-binding proteins 1 (molecular weight, 87,000) and 3 (molecular weight, 75,000) of S. aureus and penicillin-binding proteins 1 (molecular weight, 105,000) and 3 (molecular weight, 79,000) of S. faecalis bound beta-lactam antibiotics at concentrations comparable to minimum inhibitory concentrations and might therefore be essential. The low affinity of S. faecalis penicillin-binding proteins, relative to that of S. aureus penicillin-binding proteins, toward most beta-lactam antibiotics is probably responsible for the resistance of the former organism to most of these compounds.