Bactericidal effect of sulbactam against Acinetobacter baumannii ATCC 19606 studied by 2D-DIGE and mass spectrometry.

Abstract

Acinetobacter baumannii has been associated with several severe hospital-acquired infections such as ventilator-associated pneumonia and meningitis. Sulbactam, a β-lactamase inhibitor, is usually combined with β-lactam antibiotics to treat infections. It has been found that sulbactam alone may be used to treat infections caused by A. baumannii, although the mechanism of the bactericidal effect remains unknown. In this study, proteomics was used to analyse protein intensity changes and to identify the proteins of A. baumannii following sulbactam treatment. In total, 54 proteins were found to exhibit significant changes in intensity. Proteins with reduced intensity included ATP-binding cassette (ABC) transporters as well as 30S and 50S ribosomal subunit proteins. These proteins are essential for nutrient import and protein synthesis and are vital for bacterial survival. The amplified proteins included glutamine synthetase, malic enzyme, RNA polymerase subunit α, and the molecular chaperones DnaK and GroEL, which function in metabolism, DNA and protein synthesis, and repair machinery. These amplified proteins were increased to rescue bacteria, however they could not overcome the effects of the reduced proteins and the bacteria were killed. This is the first report that the reduction of ABC transporters and 30S and 50S ribosomal subunit proteins plays an important role in the bactericidal effect of sulbactam against A. baumannii.