An evaluation of the bacteriolytic and biochemical properties of ceftiolene (42980RP) - PubMed (original) (raw)
An evaluation of the bacteriolytic and biochemical properties of ceftiolene (42980RP)
R Williamson et al. J Antimicrob Chemother. 1984 Dec.
Abstract
Ceftiolene (42980RP) is a new cephalosporin with a broad antibacterial spectrum similar to cefotaxime or ceftriaxone. The characteristics of ceftiolene have been tested in a variety of assays involving various biochemical aspects of the mode of action of beta-lactam antibiotics. The affinities of ceftiolene for penicillin-binding proteins were very comparable with those of ceftriaxone and cefotaxime for Escherichia coli, and generally greater than those of latamoxef (moxalactam) for the higher molecular weight PBPs of E. coli. Enterobacter cloacae. Proteus mirabilis and Pseudomonas aeruginosa. The affinity of ceftiolene for PBP1 of Staphylococcus aureus was greater than those of cefotaxime or latamoxef, but comparable with these antibiotics for PBP3. The bacteriolytic activity of ceftiolene at defined concentrations against Gram-negative organisms was similar to that of ceftriaxone, and significantly better than that of the other third-generation cephalosporins tested. Introduction of plasmid-encoded beta-lactamases into E. coli reduced the wide variation in bacteriolytic effect of the different cephalosporins, and a significant inoculum effect was observed for the bacteriolysis. Chloramphenicol was less antagonistic against ceftiolene- or ceftriaxone-induced lysis than was observed for cefotaxime or latamoxef. Growth of Staph. aureus at low concentrations of ceftiolene caused the bacteria to become more sensitive to lysis by lysostaphin than organisms grown with cefotaxime or latamoxef under the same conditions. These observations confirm the necessity to use techniques other than routine MIC determinations to distinguish between antibiotics which would otherwise appear very similar.
Similar articles
- Cefotaxime: binding affinity to penicillin-binding proteins and morphological changes of Escherichia coli and Pseudomonas aeruginosa.
Masuyoshi S, Inoue M, Takaoka M, Mitsuhashi S. Masuyoshi S, et al. Arzneimittelforschung. 1981;31(7):1070-2. Arzneimittelforschung. 1981. PMID: 6268122 - Mode of action of the dual-action cephalosporin Ro 23-9424.
Georgopapadakou NH, Bertasso A, Chan KK, Chapman JS, Cleeland R, Cummings LM, Dix BA, Keith DD. Georgopapadakou NH, et al. Antimicrob Agents Chemother. 1989 Jul;33(7):1067-71. doi: 10.1128/AAC.33.7.1067. Antimicrob Agents Chemother. 1989. PMID: 2675755 Free PMC article. - Cefmenoxime (SCE-1365), a novel broad-spectrum cephalosporin: in vitro and in vivo antibacterial activities.
Tsuchiya K, Kondo M, Kida M, Nakao M, Iwahi T, Nishi T, Noji Y, Takeuchi M, Nozaki Y. Tsuchiya K, et al. Antimicrob Agents Chemother. 1981 Jan;19(1):56-65. doi: 10.1128/AAC.19.1.56. Antimicrob Agents Chemother. 1981. PMID: 6941742 Free PMC article. - Cefoperazone: a review of its antimicrobial spectrum, beta-lactamase stability, enzyme inhibition, and other in vitro characteristics.
Jones RN, Barry AL. Jones RN, et al. Rev Infect Dis. 1983 Mar-Apr;5 Suppl 1:S108-26. doi: 10.1093/clinids/5.supplement_1.s108. Rev Infect Dis. 1983. PMID: 6221381 Review. - Antimicrobial activity of ceftriaxone: a review.
Cleeland R, Squires E. Cleeland R, et al. Am J Med. 1984 Oct 19;77(4C):3-11. Am J Med. 1984. PMID: 6093515 Review.
Cited by
- Microbiological investigation of cephalosporins.
Hamilton-Miller JM. Hamilton-Miller JM. Drugs. 1987;34 Suppl 2:23-43. doi: 10.2165/00003495-198700342-00005. Drugs. 1987. PMID: 3319504 Review. - Modulation of bacteriolysis by cooperative effects of penicillin-binding proteins 1a and 3 in Escherichia coli.
Tuomanen E, Gilbert K, Tomasz A. Tuomanen E, et al. Antimicrob Agents Chemother. 1986 Nov;30(5):659-63. doi: 10.1128/AAC.30.5.659. Antimicrob Agents Chemother. 1986. PMID: 3541782 Free PMC article. - Target for bacteriostatic and bactericidal activities of beta-lactam antibiotics against Escherichia coli resides in different penicillin-binding proteins.
Satta G, Cornaglia G, Mazzariol A, Golini G, Valisena S, Fontana R. Satta G, et al. Antimicrob Agents Chemother. 1995 Apr;39(4):812-8. doi: 10.1128/AAC.39.4.812. Antimicrob Agents Chemother. 1995. PMID: 7785976 Free PMC article. - Involvement of penicillin-binding protein 2 with other penicillin-binding proteins in lysis of Escherichia coli by some beta-lactam antibiotics alone and in synergistic lytic effect of amdinocillin (mecillinam).
Gutmann L, Vincent S, Billot-Klein D, Acar JF, Mrèna E, Williamson R. Gutmann L, et al. Antimicrob Agents Chemother. 1986 Dec;30(6):906-12. doi: 10.1128/AAC.30.6.906. Antimicrob Agents Chemother. 1986. PMID: 3545069 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources