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Journal of Bacteriology, October 1999, p. 6552-6555, Vol. 181, No. 20
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Gene Disruption Studies of Penicillin-Binding Proteins 1a, 1b, and 2a in Streptococcus pneumoniae

JoAnn Hoskins,* Patti Matsushima, Deborah L. Mullen, Joseph Tang, Genshi Zhao, Timothy I. Meier, Thalia I. Nicas, and S. Richard Jaskunas

Lilly Research Laboratories, Eli Lilly and Company, Lilly Corporate Center, Indianapolis, Indiana 46285

Received 14 June 1999/Accepted 3 August 1999

The effects of inactivation of the genes encoding penicillin-binding protein 1a (PBP1a), PBP1b, and PBP2a in Streptococcus pneumoniae were examined. Insertional mutants did not exhibit detectable changes in growth rate or morphology, although a pbp1a pbp1b double-disruption mutant grew more slowly than its parent did. Attempts to generate a pbp1a pbp2a double-disruption mutant failed. The pbp2a mutants, but not the other mutants, were more sensitive to moenomycin, a transglycosylase inhibitor. These observations suggest that individually the pbp1a, pbp1b, and pbp2a genes are dispensable but that either pbp1a or pbp2a is required for growth in vitro. These results also suggest that PBP2a is a functional transglycosylase in S. pneumoniae.

* Corresponding author. Mailing address: Lilly Corporate Center, Eli Lilly and Company, Infectious Diseases Research, Drop Code 0438, Indianapolis, IN 46285. Phone: (317) 277-1934. Fax: (317) 277-0778. E-mail: Hoskins_JoAnn{at}Lilly.com.

Journal of Bacteriology, October 1999, p. 6552-6555, Vol. 181, No. 20
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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