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Antimicrobial Agents and Chemotherapy, May 1999, p. 1252-1255, Vol. 43, No. 5
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Diversity of Substitutions within or Adjacent to Conserved Amino Acid Motifs of Penicillin-Binding Protein 2X in Cephalosporin-Resistant Streptococcus pneumoniae Isolates

Yasuko Asahi,1 Yasuo Takeuchi,1 and Kimiko Ubukata2,*

Pharmaceutical Research Center, Meiji Seika Kaisha, Ltd., Kohoku-ku, Yokohama 222-8567,1 and Institute of Microbial Chemistry, Shinagawa-ku, Tokyo 141-0021,2 Japan

Received 8 September 1998/Returned for modification 16 December 1998/Accepted 27 February 1999

The sequence of an approximately 1.1-kb DNA fragment of the pbp2x gene, which encodes the transpeptidase domain, was determined for 35 clinical isolates of Streptococcus pneumoniae for which the cefotaxime (CTX) MICs varied. Strains with substitutions within a conserved amino acid motif changing STMK to SAFK and a Leu-to-Val change just before the KSG motif were highly resistant to CTX (MIC, >= 2 µg/ml). Strains with substitutions adjacent to SSN or KSG motifs had low-level resistance. The amino acid substitutions were plotted on the three-dimensional crystallographic structure of the transpeptidase domain of PBP2X. Transformants containing pbp2x from strains with high-level CTX resistance increased the CTX MIC from 0.016 µg/ml to 0.5 to 1.0 µg/ml.

* Corresponding author. Present address: Pharmaceutical Research Center, Meiji Seika Kaisha, Ltd., 760 Morooka-cho, Kohoku-ku, Yokohama 222-8567, Japan. Phone: 81-45-545-3106. Fax: 81-45-545-3152. E-mail: kimiko_ubukata{at}meiji.co.jp.

Antimicrobial Agents and Chemotherapy, May 1999, p. 1252-1255, Vol. 43, No. 5
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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