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Antimicrobial Agents and Chemotherapy, October 2004, p. 4020-4022, Vol. 48, No. 10
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.10.4020-4022.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Alterations of Penicillin-Binding Proteins 1A, 2X, and 2B in Streptococcus pneumoniae Isolates for Which Amoxicillin MICs Are Higher than Penicillin MICs

K. Kosowska,1 M. R. Jacobs,2 S. Bajaksouzian,2 L. Koeth,3* and P. C. Appelbaum1

Hershey Medical Center, Hershey, Pennsylvania,1 Case Western Reserve University, Cleveland,2 Laboratory Specialists, Inc., Westlake, Ohio3

Received 10 February 2004/ Returned for modification 7 May 2004/ Accepted 20 June 2004

Penicillin-binding proteins (PBPs) of 15 selected penicillin- and amoxicillin-resistant Streptococcus pneumoniae isolates (MICs of 2 to 8 and 8 to 16 µg/ml, respectively) were studied. In addition to typical changes in PBPs 1A and 2X, these strains had 10 unique changes in PBP 2B, including a 618A-G substitution, which may be the key alteration associated with amoxicillin resistance.

* Corresponding author. Mailing address: Laboratory Specialists, Inc., 1651 A Crossings Parkway, Westlake, OH 44145. Phone: (440) 835-4458. Fax: (440) 835-5786. E-mail: amdlmk{at}aol.com.

Antimicrobial Agents and Chemotherapy, October 2004, p. 4020-4022, Vol. 48, No. 10
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.10.4020-4022.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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