» Articles » PMID: 6524904

In Vitro Activity of CGP 31523A, a Broad-spectrum Cephalosporin, in Comparison with Those of Other Agents

Overview
Specialty Pharmacology
Date 1984 Dec 1
PMID 6524904
Citations 2
Authors
Affiliations
Soon will be listed here.
Abstract

The in vitro activity of CGP 31523A, a new aminothiazolyl cephalosporin, was compared with those of cefoxitin, cefuroxime, moxalactam, piperacillin, ciprofloxacin, and other beta-lactams, when appropriate, against 533 recent clinical isolates and known resistant strains of bacteria. The MICs of CGP 31523A required to inhibit 90% (MIC90S) of the members of the family Enterobacteriaceae, Neisseria gonorrhoeae, and Streptococcus pneumoniae were less than or equal to 0.25 micrograms/ml. Of Staphylococcus aureus (excluding methicillin-resistant strains) and Haemophilus influenzae, 90% were susceptible to 0.5 micrograms/ml. Pseudomonas aeruginosa and Lancefield group D streptococci were resistant to CGP 31523A (MIC90, greater than or equal to 128 micrograms/ml). The activity against Bacteroides fragilis was modest (MIC90, 32 micrograms/ml). The susceptibility of known beta-lactamase-producing strains suggested that CGP 31523A was resistant to many beta-lactamases (but not those of Bacteroides fragilis). The serum protein binding of CGP 31523A was about 73%. The primary target site of CGP 31523A in Escherichia coli appeared to be penicillin-binding protein 3.

Citing Articles

Penetration of moxifloxacin into bone evaluated by Monte Carlo simulation.

Landersdorfer C, Kinzig M, Hennig F, Bulitta J, Holzgrabe U, Drusano G Antimicrob Agents Chemother. 2009; 53(5):2074-81.

PMID: 19223648 PMC: 2681494. DOI: 10.1128/AAC.01056-08.


Modulation of bacteriolysis by cooperative effects of penicillin-binding proteins 1a and 3 in Escherichia coli.

Tuomanen E, Gilbert K, Tomasz A Antimicrob Agents Chemother. 1986; 30(5):659-63.

PMID: 3541782 PMC: 176509. DOI: 10.1128/AAC.30.5.659.

References
1.
OCALLAGHAN C, Morris A, Kirby S, Shingler A . Novel method for detection of beta-lactamases by using a chromogenic cephalosporin substrate. Antimicrob Agents Chemother. 1972; 1(4):283-8. PMC: 444209. DOI: 10.1128/AAC.1.4.283. View

2.
Spratt B . Properties of the penicillin-binding proteins of Escherichia coli K12,. Eur J Biochem. 1977; 72(2):341-52. DOI: 10.1111/j.1432-1033.1977.tb11258.x. View

3.
Wise R . Bacteroides fragilis and HR 756. J Antimicrob Chemother. 1979; 5(1):115-6. DOI: 10.1093/jac/5.1.115. View

4.
Wise R, Andrews J, Bedford K . LY127935, a novel oxa-beta-lactam: an in vitro comparison with other beta-lactam antibiotics. Antimicrob Agents Chemother. 1979; 16(3):341-5. PMC: 352858. DOI: 10.1128/AAC.16.3.341. View

5.
Curtis N, Orr D, Ross G, Boulton M . Affinities of penicillins and cephalosporins for the penicillin-binding proteins of Escherichia coli K-12 and their antibacterial activity. Antimicrob Agents Chemother. 1979; 16(5):533-9. PMC: 352901. DOI: 10.1128/AAC.16.5.533. View