Open AccessEffect of a β‐lactamase inhibitor, tazobactam, on growth and penicillin‐binding proteins of Borrelia burgdorferi
Author(s) -
Urban Carl,
Rahal James J.,
Luft Benjamin
Publication year - 1991
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1991.tb04849.x
Subject(s) - penicillin binding proteins , borrelia burgdorferi , microbiology and biotechnology , penicillin , chemistry , biochemistry , in vitro , tazobactam , antibiotics , biology , antibiotic resistance , imipenem , antibody , immunology
The effects of tazobactam, a relatively new β‐lactamase inhibitor, were investigated on growth and penicillin‐binding proteins (PBPs) of Borrellia burgdorferi . A previous communication from our group demonstrated several proteins capable of binding labelled penicillin in this organism. Of these proteins, 94‐kDa and 57‐kDa PBPs possessed the highest affinity for penicillin and were assumed to be essential proteins involved in cell‐wall synthesis. In these experiments, tazobactam was used in competition binding experiments as well as on whole spirochetes. Only the 94‐kDa and 57‐kDa PBPs were affected by increasing amounts of tazobactam during competition‐binding experiments and growth of B. burgdorferi was also inhibited. These results may explain the in vitro activity of β‐lactamase inhibitors in general and suggest a utility for these compounds when examining PBPs with hydrolysing activity and/or organisms with β‐lactamases.