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 -Lactam Antibiotic and -Lactamase Inhibitor Combinations
Nelson L. S. Lee, MRCP;
K. Y. Yuen, FRCPath;
Cyrus R. Kumana, FRCP
JAMA. 2001;285:386-388.
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INTRODUCTION
 -Lactam antibiotics act by binding to penicillin-binding proteins (PBPs), thus inhibiting bacterial cell wall synthesis. Increasingly, however, these antibiotics are rendered ineffective because of degradation by -lactamases. This family of enzymes, which are produced by gram-positive and gram-negative bacteria (including anaerobes) and mycobacteria,1-2 hydrolyze the -lactam ring, thereby inactivating the antibiotic molecule prior to binding with PBPs. In response, -lactamase inhibitors have been developed to conserve the activity and extend the spectrum of any accompanying -lactam drug against -lactamase–producing microorganisms.
Microbiology
More than 90% of Staphylococcus aureus strains worldwide now produce -lactamase, which is liberated extracellularly and hydrolyzes all penicillins other than those in the methicillin group. Most other gram-positive bacteria do not produce -lactamase, although resistance may occur by other means. In penicillin-resistant Streptococcus pneumoniae (PRSP), for instance, resistance occurs because of PBP mutations rather than -lactamase . . . [Full Text of this Article]
Pharmacology
Side Effects
Clinical Applications
Upper and Lower Respiratory Tract Infections Intra-abdominal Infections Urinary Tract Infections
Special Considerations
Staphylococcus aureus Gram-Negative Pathogens
Drug Resistance
Author Affiliations: Departments of Medicine (Drs Lee and Kumana) and Microbiology (Dr Yuen), The University of Hong Kong, Queen Mary Hospital, Hong Kong.
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