Clindamycin is a lincosamide antibiotic that has been approved by the US 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, including Clostridium difficile colitis. (See "Clostridium difficile in adults: Epidemiology, microbiology, and pathophysiology".)
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 spectrum of activity, pharmacology, and adverse effects of clindamycin will be reviewed here. The clinical use of clindamycin is discussed separately in the appropriate topic reviews on 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. Clindamycin and the related drug lincomycin are often discussed along with the macrolides, but are not chemically related. (See "Azithromycin, clarithromycin, and telithromycin".)
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.