Alterations to penicillin-binding proteins 1A, 2B and 2X amongst penicillin-resistant clinical isolates of Streptococcus pneumoniae serotype 23F fromthe nasopharyngeal flora of children
A. Ferroni et P. Berche, Alterations to penicillin-binding proteins 1A, 2B and 2X amongst penicillin-resistant clinical isolates of Streptococcus pneumoniae serotype 23F fromthe nasopharyngeal flora of children, J MED MICRO, 50(9), 2001, pp. 828-832
Various amino acid substitutions were identified in the three major penicil
lin-binding proteins (PBP1A, PBP2B and PBP2X) of eight clinical isolates of
Streptococcus pneumoniae serotype 23F collected from children. The particu
lar changes related to the level of penicillin resistance. Alterations were
detected in an isolate with a penicillin MIC as low as 0.06 mg/L. These re
sults confirm that the level of penicillin resistance in pneumococci reflec
ts with sequential alterations of PBPs in clinical isolates.