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J. Med. Microbiol. -- Vol. 50 (2001), 828-832
© 2001 Society for General Microbiology
ISSN 0022-2615

ANTIMICROBIAL RESISTANCE

Alterations to penicillin-binding proteins 1A, 2B and 2X amongst penicillin-resistant clinical isolates of Streptococcus pneumoniae serotype 23F from the nasopharyngeal flora of children

AGNES FERRONI and PATRICK BERCHE

Service de Microbiologie, CHU Necker-Enfants-Malades, 149 rue de Sèvres, 75015 Paris, France

Corresponding author: Professor P. Berche (e-mail: berche{at}necker.fr).

Received 26 Oct. 2000; revised version accepted 26 March 2001.

Abstract

Various amino acid substitutions were identified in the three major penicillin-binding proteins (PBP1A, PBP2B and PBP2X) of eight clinical isolates of Streptococcus pneumoniae serotype 23F collected from children. The particular changes related to the level of penicillin resistance. Alterations were detected in an isolate with a penicillin MIC as low as 0.065mumg/L. These results confirm that the level of penicillin resistance in pneumococci reflects with sequential alterations of PBPs in clinical isolates.




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