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Antimicrobial Agents and Chemotherapy, October 1999, p. 2534-2537, Vol. 43, No. 10
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Potent Bacteriolytic Activity of Ritipenem Associated with a Characteristic Profile of Affinities for Penicillin-Binding Proteins of Haemophilus influenzae

Takashi Inui,* Tadahiro Oshida, Toshio Endo, and Tadahiro Matsushita

Discovery Research Laboratory, Tanabe Seiyaku Co., Ltd., 2-2-50, Kawagishi, Toda-shi, Saitama 335-8505, Japan

Received 15 January 1999/Returned for modification 19 April 1999/Accepted 20 July 1999

Ritipenem is highly bacteriolytic against Haemophilus influenzae. Bacterial lysis was shown after treatments with ritipenem and cefsulodin at their MICs and after treatments with fropenem and cefdinir at four times their MICs, indicated by decreases in the culture turbidities and by morphological changes of the destroyed cells. These beta -lactams were preferentially bound to penicillin-binding protein (PBP) 1b. Ritipenem, fropenem, and cefsulodin exhibited poor affinities to PBPs 3a and 3b, but cefdinir showed high affinities to these PBPs. Microscopic examinations revealed that selective PBP 3 inhibitors, such as aztreonam and cefotaxime, inhibited lysis induced by ritipenem. These results suggest that the preferential inactivation of PBP 1b could be essential to induce the lysis of H. influenzae cells and that binding to PBPs 3a and 3b may interfere with lysis.

* Corresponding author. Mailing address: Discovery Research Laboratory, Tanabe Seiyaku Co., Ltd., 2-2-50, Kawagishi, Toda-shi, Saitama 335-8505, Japan. Phone: 81-48-433-8074. Fax: 81-48-433-8161. E-mail: tksh{at}tanabe.co.jp.

Antimicrobial Agents and Chemotherapy, October 1999, p. 2534-2537, Vol. 43, No. 10
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Inui, T., Endo, T., Matsushita, T. (2000). Morphological Changes and Lysis Induced by beta -Lactams Associated with the Characteristic Profiles of Affinities of Penicillin-Binding Proteins in Actinobacillus pleuropneumoniae. Antimicrob. Agents Chemother. 44: 1518-1523 [Abstract] [Full Text]  


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