Carbapenems are frequently used for severe hospital infections caused by K. pneumoniae, especially when isolates produce extended-spectrum β-lactamases...

introduction: pseudomonas aeruginosa is one of the leading causes of nosocomial infections, and antibiotic resistance of this pathogen is an important concern in treating such infections. the current work was conducted to investigate the prevalence of bla-imp, and bla-vim metallo-beta-lactamase (mbl) among clinical and environmental p. aeruginosa isolates obtained from icus of different hospita...

background: drug utilization evaluation (due) studies are designed to evaluate and improve the rational use of medications. dues have focused on drugs used in high risk patients such as critically ill cases in this study. carbapenems are beta-lactam type antibiotics with broad-spectrum of activity which cover gram-positive, gram-negative and anaerobic bacteria. the heavy use of carbapenems (imi...

Metallo β-lactamases is the name given to certain enzymes found in gram negative bacteria belonging to Enter-obacteriaceae which confers resistance to all β-lactam antibiotics including carbapenems except monobactams. They belong to Ambler molecular class B and Bush-Jacoby-Medeiros Group 3.1,2 Resistance to carbapenems due to production of metallo β-lactamases in Gram Negative organisms is an i...

The effect of high N-acetylcysteine (NAC) concentrations (10 and 50 mM) on antibiotic activity against 40 strains of respiratory pathogens was investigated. NAC compromised the activity of carbapenems (of mostly imipenem and, to lesser extents, meropenem and ertapenem) in a dose-dependent fashion. We demonstrated chemical instability of carbapenems in the presence of NAC. With other antibiotics...

In this review, we summarize the current "state of the art" of carbapenem antibiotics and their role in our antimicrobial armamentarium. Among the β-lactams currently available, carbapenems are unique because they are relatively resistant to hydrolysis by most β-lactamases, in some cases act as "slow substrates" or inhibitors of β-lactamases, and still target penicillin binding proteins. This "...