Effect of subinhibitory concentrations of josamycin on the expression of M protein by group A streptococci.

In an attempt to inhibit the biosynthesis of the type-specific M protein usually expressed on surface fimbriae group A Streptococcus pyogenes delta 2305 was cultivated in Todd-Hewitt broth containing 10% human serum and subinhibitory concentrations of either josamycin, erythromycin or clindamycin. Electron microscopy revealed that the antibiotic-pretreatment had little visible effect on the surface structures of the streptococci. However, josamycin and clindamycin-pretreated bacteria adhered less to hydrophobic gels than erythromycin-pretreated or untreated control cultures. Due to the decrease in surface hydrophobicity, the drug-pretreated bacteria also activated complement more readily and fixed more C3 on their surface. Consequently the killing of josamycin and clindamycin-pretreated bacteria by polymorphonuclear leucocytes was significantly enhanced. Similar findings were obtained when the M protein was removed from the bacteria by digestion with trypsin. These results suggest that josamycin, like clindamycin, reverses the capacity of group A streptococci to resist opsonization by normal human serum and interferes with the adhesion of the organisms to host epithelial cell surfaces.