Open AccessInteraction of sulbactam, clavulanic acid and tazobactam with penicillin‐binding proteins of imipenem‐resistant and ‐susceptible acinetobacter baumannii
Author(s) -
Urban Carl,
Go Eddie,
Mariano Noriel,
Rahal James J.
Publication year - 1995
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.1574-6968.1995.tb07357.x
Subject(s) - imipenem , sulbactam , acinetobacter baumannii , microbiology and biotechnology , penicillin binding proteins , tazobactam , clavulanic acid , penicillin , acinetobacter , neisseriaceae , thienamycin , antibiotics , chemistry , biology , bacteria , antibiotic resistance , amoxicillin , genetics , pseudomonas aeruginosa
We have encountered clinical isolates of Acinetobacter baumannii which are resistant to all available antibiotics used in hospitals except for polymyxin B and the beta‐lactamase inhibitor, sulbactam. To investigate the mechanisms of this unique activity, affinities of sulbactam and other beta‐lactamase inhibitors for penicillin binding proteins were compared using imipenem‐resistant and imipenem‐sensitive isolates. The results of competition binding experiments indicate that all three beta‐lactamase inhibitors bound to imipenem‐susceptible Acinetobacter . Binding of sulbactam was greater than that of tazobactam and not detected with clavulanic acid to penicillin binding proteins of the imipenem‐resistant strain of Acinetobacter .