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Antimicrobial Agents and Chemotherapy, June 2000, p. 1745-1748, Vol. 44, No. 6
0066-4804/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Identification and Characterization of the Penicillin-Binding Protein 2a of Streptococcus pneumoniae and Its Possible Role in Resistance to beta -Lactam Antibiotics

Genshi Zhao,* Timothy I. Meier, Joann Hoskins, and Kelly A. McAllister

Infectious Diseases Research, Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285

Received 19 August 1999/Returned for modification 21 December 1999/Accepted 10 March 2000

To further understand the role of penicillin-binding protein 2a (PBP 2a) of Streptococcus pneumoniae in penicillin resistance, we confirmed the identity of the protein as PBP 2a. The PBP 2a protein migrated electrophoretically to a position corresponding to that of PBP 2x, PBP 2a, and PBP 2b of S. pneumoniae and was absent in a pbp2a insertional mutant of S. pneumoniae. We found that the affinities of PBP 2a for penicillins were lower than for cephalosporins and a carbapenem. When compared with other S. pneumoniae PBPs, PBP 2a exhibited lower affinities for beta -lactam antibiotics, especially penicillins. Therefore, PBP 2a is a low-affinity PBP for beta -lactam antibiotics in S. pneumoniae.

* Corresponding author. Mailing address: Infectious Diseases Research, Lilly Research Laboratories, Lilly Corporate Center, Eli Lilly and Company, Drop Code 0438, Indianapolis, IN 46285-0438. Phone: (317) 276-2040. Fax: (317) 276-1743. E-mail: Zhao_Genshi{at}Lilly.Com.

Antimicrobial Agents and Chemotherapy, June 2000, p. 1745-1748, Vol. 44, No. 6
0066-4804/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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