Mechanism of Action
Clindamycin inhibits bacterial protein synthesis by binding to the 23S RNA of the 50S subunit of the ribosome. Clindamycin is predominantly bacteriostatic. Although clindamycin phosphate is inactive in vitro, rapid in vivo hydrolysis converts it to active clindamycin.
Resistance to clindamycin is most often caused by modification of the target site on the ribosome, usually by chemical modification of RNA bases by point mutations in RNA or occasionally in proteins. Cross resistance has been demonstrated between lincosamides, macrolides and streptogramins B in some organisms. Cross resistance has been demonstrated between clindamycin and lincomycin.
Culture and sensitivity testing of bacteria are not routinely performed to establish the diagnosis of bacterial vaginosis (see INDICATIONS AND USAGE); standard methodology for the susceptibility testing of the potential bacterial pathogens, Gardnerella vaginalis, Mobiluncus spp., or Mycoplasma hominis, has not been defined.
The following in vitro data are available but their clinical significance is unknown. Clindamycin is active in vitro against most isolates of the following organisms reported to be associated with bacterial vaginosis:
- Bacteroides spp.
- Gardnerella vaginalis
- Mobiluncus spp.
- Mycoplasma hominis
- Peptostreptococcus spp.