Previous Article | Next Article ![]()
Antimicrobial Agents and Chemotherapy, June 2000, p. 1518-1523, Vol. 44, No. 6
Discovery Research Laboratory, Tanabe Seiyaku
Co., Ltd., 2-2-50, Kawagishi, Toda-shi, Saitama 335-8505, Japan
Received 6 July 1999/Returned for modification 3 November
1999/Accepted 10 March 2000
Actinobacillus pleuropneumoniae, which was formerly
classified in the genus Haemophilus, is a pathogen causing
swine pleuropneumonia. We found that aspoxicillin showed strong
activity and that meropenem had better lytic activity against this
pathogen. In the present study, we for the first time identified
penicillin-binding proteins (PBPs) of A. pleuropneumoniae
in order to elucidate the relationship between the antibacterial and
lytic activities of
0066-4804/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Morphological Changes and Lysis Induced by
-Lactams Associated
with the Characteristic Profiles of Affinities of Penicillin-Binding
Proteins in Actinobacillus pleuropneumoniae
-lactam antibiotics and affinities of the PBPs.
The competitive assay using 3H-labeled benzylpenicillin
revealed seven PBPs in A. pleuropneumoniae; they were
determined to be PBPs 1a, 1b, 2, 3, 4, 5, and 6, and the molecular
masses of these PBPs were estimated to be 92, 80, 76, 72, 50, 44, and
30 kDa, respectively, by comparison with those of Haemophilus
influenzae. Our detailed analysis of the affinities of the PBPs
of A. pleuropneumoniae and of the bacterial lysis kinetics
for several
-lactam antibiotics revealed that the strong antibacterial activity of aspoxicillin against this strain could be
related to the higher affinity of PBP 3 and that preferential inactivation of PBP 1b could cause rapid lysis.
*
Corresponding author. Mailing address: Discovery
Research Laboratory, Tanabe Seiyaku Co., Ltd., 2-2-50, Kawagishi,
Toda-shi, Saitama 335-8505, Japan. Phone: 81-48-433-8071. Fax:
81-48-433-8161. E-mail: tksh{at}tanabe.co.jp.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»