Arginine Modulates Carbapenem Deactivation by OXA-24/40 in Acinetobacter baumannii.

The resistance of Gram-negative bacteria to β-lactam antibiotics stems mainly from β-lactamase proteins that hydrolytically deactivate the β-lactams. Of particular concern are the β-lactamases that can deactivate a class of β-lactams known as carbapenems. Carbapenems are among the few anti-infectives that can treat multi-drug resistant bacterial infections.

Expanded Substrate Activity of OXA-24/40 in Carbapenem-Resistant Acinetobacter baumannii Involves Enhanced Binding Loop Flexibility.

Gram-negative bacteria resist β-lactam antibiotics primarily by deploying β-lactamase proteins that hydrolytically destroy the antibiotics. In clinical settings, these bacteria are producing variant β-lactamases with "gain-of-activity" mutations that inactivate a broader range of β-lactams. Learning how these mutations broaden substrate activity is important for coping with β-lactam resistance.

Investigation of signal transduction routes within the sensor/transducer protein BlaR1 of Staphylococcus aureus.

The transmembrane antibiotic sensor/signal transducer protein BlaR1 is part of a cohort of proteins that confer β-lactam antibiotic resistance in methicillin-resistant Staphylococcus aureus (MRSA) [Fisher, J. F., Meroueh, S.