Clindamycin: An overview

INTRODUCTION

Clindamycin is a lincosamide antibiotic which is approved in the United States by the Food and Drug Administration (FDA) for the treatment of anaerobic, streptococcal, and staphylococcal infections. Its major disadvantage is its propensity to cause antibiotic-associated diarrhea. (See "Epidemiology, microbiology, and pathophysiology of Clostridium difficile infection".)

There has been increased interest in the use of clindamycin because it achieves high intracellular levels in phagocytic cells, high levels in bone, and appears to have an antitoxin effect against toxin elaborating strains of streptococci and staphylococci. (See "Epidemiology, clinical manifestations, and diagnosis of streptococcal toxic shock syndrome".)

The pharmacology of clindamycin will be reviewed here. The clinical use of clindamycin is discussed separately on the appropriate topic reviews for the specific infections.

MECHANISM OF ACTION

Clindamycin works primarily by binding to the 50s ribosomal subunit of bacteria. This agent disrupts protein synthesis by interfering with the transpeptidation reaction which thereby inhibits early chain elongation. Chloramphenicol and macrolides such as erythromycin, clarithromycin, and azithromycin also act at the 50s ribosomal subunit and may compete for binding at this site. (See "Azithromycin, clarithromycin, and telithromycin".) Clindamycin and the related drug lincomycin are often discussed along with the macrolides but are not chemically related.

Clindamycin may potentiate the opsonization and phagocytosis of bacteria even at subinhibitory concentrations [1,2]. By disrupting bacterial protein synthesis, clindamycin causes changes in the cell wall surface which decreases adherence of bacteria to host cells and increases intracellular killing of organisms. The drug also exerts an extended postantibiotic effect against some strains of bacteria which may be attributed to persistence of the drug at the ribosomal binding site.