 |
|
 -Lactam Antibiotic and -Lactamase Inhibitor Combinations
Nelson L. S. Lee, MRCP;
K. Y. Yuen, FRCPath;
Cyrus R. Kumana, FRCP
JAMA. 2001;285:386-388.
|
|
| Since this article does not have an abstract, we have provided the first 150 words of the full text and any section headings. |
|
|
|
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.
RELATED ARTICLE
January 24/31, 2001
JAMA. 2001;285(4):475-476.
EXTRACT
| FULL TEXT
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES
Applying antimicrobial pharmacodynamics to resistant gram-negative pathogens.
Scheetz et al.
Am J Health Syst Pharm 2006;63:1346-1360.
ABSTRACT
| FULL TEXT
Probing the Dynamics of a Mobile Loop above the Active Site of L1, a Metallo-{beta}-lactamase from Stenotrophomonas maltophilia, via Site-directed Mutagenesis and Stopped-flow Fluorescence Spectroscopy
Garrity et al.
J. Biol. Chem. 2004;279:39663-39670.
ABSTRACT
| FULL TEXT
Metal Binding Asp-120 in Metallo-{beta}-lactamase L1 from Stenotrophomonas maltophilia Plays a Crucial Role in Catalysis
Garrity et al.
J. Biol. Chem. 2004;279:920-927.
ABSTRACT
| FULL TEXT
|
